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Conserved domains on  [gi|564365651|ref|XP_006243923|]
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cadherin EGF LAG seven-pass G-type receptor 3 isoform X5 [Rattus norvegicus]

Protein Classification

adhesion G protein-coupled receptor L2( domain architecture ID 11588040)

adhesion G protein-coupled receptor L2 (ADGRL2), also called latrophilin 2, is an adhesion G-protein-coupled receptor (GPCR) whose exogenous ligand is alpha-latrotoxin; adhesion GPCRs, also called LN-7TM or EGF-7TM receptors, are membrane-bound proteins with long N-termini containing multiple domains

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
7tm_GPCRs super family cl28897
seven-transmembrane G protein-coupled receptor superfamily; This hierarchical evolutionary ...
 2534-2724 1.77e-113

seven-transmembrane G protein-coupled receptor superfamily; This hierarchical evolutionary model represents the seven-transmembrane (7TM) receptors, often referred to as G protein-coupled receptors (GPCRs), which transmit physiological signals from the outside of the cell to the inside via G proteins. GPCRs constitute the largest known superfamily of transmembrane receptors across the three kingdoms of life that respond to a wide variety of extracellular stimuli including peptides, lipids, neurotransmitters, amino acids, hormones, and sensory stimuli such as light, smell and taste. All GPCRs share a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes. However, some 7TM receptors, such as the type 1 microbial rhodopsins, do not activate G proteins. Based on sequence similarity, GPCRs can be divided into six major classes: class A (the rhodopsin-like family), class B (the Methuselah-like, adhesion and secretin-like receptor family), class C (the metabotropic glutamate receptor family), class D (the fungal mating pheromone receptors), class E (the cAMP receptor family), and class F (the frizzled/smoothened receptor family). Nearly 800 human GPCR genes have been identified and are involved essentially in all major physiological processes. Approximately 40% of clinically marketed drugs mediate their effects through modulation of GPCR function for the treatment of a variety of human diseases including bacterial infections.


The actual alignment was detected with superfamily member cd15993:

Pssm-ID: 475119 [Multi-domain]  Cd Length: 254  Bit Score: 361.08  E-value: 1.77e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2534 LELLAVFTHVVVAASVTALVLTAAVLLSLRSLKSNVRGIHANVAAALGVAELLFLLGIHRTHNQLLCTVVAILLHYFFLS 2613
Cdd:cd15993     1 LETLAIVTYSSVSASLAALVLTFSVLTCLRGLKSNTRGIHSNIAAALFLSELLFLLGINRTENQFLCTVVAILLHYFFLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2614 TFAWLLVQGLHLYRMQVEPRNVDRGAMRFYHALGWGVPAVLLGLAVGLDPEGYGNPDFCWISIHEPLIWSFAGPIVLVIV 2693
Cdd:cd15993    81 TFAWLFVQGLHIYRMQTEARNVNFGAMRFYYAIGWGVPAIITGLAVGLDPEGYGNPDFCWISIHDKLVWSFAGPIVVVIV 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 564365651 2694 MNGIMFLLAARTSCSTGQREAKKTSVLVLPR 2724
Cdd:cd15993   161 MNGVMFLLVARMSCSPGQKETKKTSVLMTLR 191
GAIN pfam16489
GPCR-Autoproteolysis INducing (GAIN) domain; The GAIN a domain of alpha-helices and ...
 2200-2448 1.88e-45

GPCR-Autoproteolysis INducing (GAIN) domain; The GAIN a domain of alpha-helices and beta-strands that is found in cell-adhesion GPCRs and precedes the GPS motif where the autoproteolysis occurs, family, pfam01825. The full GAIN domain, comprises the GPS and the GAIN, in cell-adhesion GPCRs, and is the functional unit for autoproteolysis. The GPS motif at the end of the GAIN domain is an ancient domain that exists in primitive ancestor organizms, and the full GAIN + GPS is conserved in all cell-adhesion GPCRs and all PKD1-related proteins.


:

Pssm-ID: 465137  Cd Length: 205  Bit Score: 163.98  E-value: 1.88e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  2200 EAKKLAQRLREVTgQTDHYFSQDVRVTARLLAYLlafeshqqgFGLTATQDA----HFNENLLWAGSALLAPETGDLWAA 2275
Cdd:pfam16489    1 GAKELARELRNAT-RHGPLYGGDVLTAVELLSQL---------FDLLATQDAtlsnAFLENFVQTVSNLLDPENRESWED 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  2276 LGQRAPGGSpgSAGLVRHLEEYAATLARNMDltYLNPVGLVTPNIMLSIDRMEQPSSSQgaHRYPRYHSNlfrgQDAWDP 2355
Cdd:pfam16489   71 LQQTERGTA--ATKLLRTLEEYALLLAQNMK--YLTPFTIVTPNIVLSVDRLDTHNFKG--ARFPRFPMK----GERPKD 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  2356 HTHVLLpsqspqpspsevlptssnaenatasgvvsPPAPLEPESEPGISIVILLVYRALGGLLPAQ--FQAERRGARLPQ 2433
Cdd:pfam16489  141 EDSVKL-----------------------------PPKAFKPPDSNGTVVVVFILYRNLGSLLPPSsrYDPDRRSLRLPR 191

                          250
                   ....*....|....*
gi 564365651  2434 NpVMNSPVVSVAVFR 2448
Cdd:pfam16489  192 R-VVNSPVVSASVHS 205
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 646-743 4.88e-38

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


:

Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 138.60  E-value: 4.88e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  646 PFQVSVLENAPLGHSVIHIQAVDADHGENSRLEYSLTGVASDTPFVINSATGWVSVSGPLDRESVEHYFFGVEARDHGSP 725
Cdd:cd11304     1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGGGP 80

                          90
                  ....*....|....*...
gi 564365651  726 PLSASASVTVTVLDVNDN 743
Cdd:cd11304    81 PLSSTATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 956-1054 1.62e-35

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


:

Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 131.28  E-value: 1.62e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  956 HYTGLVSEDAPPFTSVLQISATDRDAHANGRVQYTFQNGeDGDGDFTIEPTSGIVRTVRRLDREAVPVYELTAYAVDRGV 1035
Cdd:cd11304     1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSG-NEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGGG 79

                          90
                  ....*....|....*....
gi 564365651 1036 PPLRTPVSIQVTVQDVNDN 1054
Cdd:cd11304    80 PPLSSTATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 541-638 1.75e-34

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


:

Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 128.20  E-value: 1.75e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  541 YVAQVREDVRPHTVVLRVTATDKDKDANGLVHYNIISGNSRGHFAIDSLTGEIQVMAPLDFEAEREYALRIRAQDAGRPP 620
Cdd:cd11304     2 YEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGGGPP 81

                          90
                  ....*....|....*...
gi 564365651  621 LSnNTGLASIQVVDINDH 638
Cdd:cd11304    82 LS-STATVTITVLDVNDN 98
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 1508-1691 1.42e-33

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


:

Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 127.92  E-value: 1.42e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 1508 ARSFPPSSFVMFRGLR-QRFHLTLSLSFATVQPSGLLFYNGRLNeKHDFLALELVAGQVRLTYSTGESSTVVSPTVPggL 1586
Cdd:cd00110     1 GVSFSGSSYVRLPTLPaPRTRLSISFSFRTTSPNGLLLYAGSQN-GGDFLALELEDGRLVLRYDLGSGSLVLSSKTP--L 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 1587 SDGQWHTVHLRYYNkprtdalggaqgpskdKVAVLSVDDCNVavaLRFGAEIGNYscaaagvqtsskkSLDLTGPLLLGG 1666
Cdd:cd00110    78 NDGQWHSVSVERNG----------------RSVTLSVDGERV---VESGSPGGSA-------------LLNLDGPLYLGG 125

                         170       180
                  ....*....|....*....|....*.
gi 564365651 1667 VPNLPENFPV-SRKDFIGCMRDLHID 1691
Cdd:cd00110   126 LPEDLKSPGLpVSPGFVGCIRDLKVN 151
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 321-420 1.65e-33

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


:

Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 125.50  E-value: 1.65e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  321 YQTLVPENEAAGTAVLRVVAQDPDPGEAGRLVYSLaalMNSRSLELFSIDPQSGLIRTAAALDRESMERHYLRVTAQDHG 400
Cdd:cd11304     2 YEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSI---VSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGG 78

                          90       100
                  ....*....|....*....|
gi 564365651  401 SPRLSATTMVAVTVADRNDH 420
Cdd:cd11304    79 GPPLSSTATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 428-532 2.02e-32

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


:

Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 122.42  E-value: 2.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  428 QYRETLRENVEEGYPILQLRATDGDAPPNANLRYRFVGSPAARTaaaaaFEIDPRSGLISTSGRVDREHMESYELVVEAS 507
Cdd:cd11304     1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDGL-----FSIDPSTGEITTAKPLDREEQSSYTLTVTAT 75

                          90       100
                  ....*....|....*....|....*
gi 564365651  508 DQGQEpgPRSATVRVHITVLDENDN 532
Cdd:cd11304    76 DGGGP--PLSSTATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 853-948 6.65e-31

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


:

Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 118.18  E-value: 6.65e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  853 HYSVSMNEDRPVGSTVVVISASDDDVGENARITYLL--EDNLPQFRIDADSGAITLQAPLDYEDQVTYTLAITARDNGIP 930
Cdd:cd11304     1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIvsGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGGGP 80

                          90
                  ....*....|....*...
gi 564365651  931 QKADTTYVEVMVNDVNDN 948
Cdd:cd11304    81 PLSSTATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 1062-1156 4.13e-30

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


:

Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 115.87  E-value: 4.13e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 1062 EFEVRVKENSIVGSVVAQITAVDPDDGPNAHIMYQIVEGNIPELFQMDIFSGELTALIDLDYEARQEYVIVVQAT---SA 1138
Cdd:cd11304     1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATdggGP 80

                          90
                  ....*....|....*...
gi 564365651 1139 PLVSRATVHVRLVDQNDN 1156
Cdd:cd11304    81 PLSSTATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 751-845 1.27e-21

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


:

Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 91.61  E-value: 1.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  751 EYHLRLNEDAAVGTSVVSVTAVDRD--ANSAISYQITGGNTRNRFAISTQggMGLVTLALPLDYKQERYFKLVLTASDR- 827
Cdd:cd11304     1 SYEVSVPENAPPGTVVLTVSATDPDsgENGEVTYSIVSGNEDGLFSIDPS--TGEITTAKPLDREEQSSYTLTVTATDGg 78

                          90       100
                  ....*....|....*....|
gi 564365651  828 --ALHDHCYVHINITDANTH 845
Cdd:cd11304    79 gpPLSSTATVTITVLDVNDN 98
HormR smart00008
Domain present in hormone receptors;
2117-2181 1.23e-19

Domain present in hormone receptors;


:

Pssm-ID: 214468  Cd Length: 70  Bit Score: 84.87  E-value: 1.23e-19
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564365651   2117 YDACPKSLRSGVWWPQTKFGVLATVPCPRGALGLRGTGAAVRLCDEDHGWLE--PDFFNCTSPAFRE 2181
Cdd:smart00008    2 DLGCPATWDGIICWPQTPAGQLVEVPCPKYFSGFSYKTGASRNCTENGGWSPpfPNYSNCTSNDYEE 68
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 1755-1911 2.94e-18

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


:

Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 84.01  E-value: 2.94e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 1755 PYHFQGNGTLSwdFGNDMPVSVPWYLGLSFRTRATKGVLMQV-QLGPHSVLLCKLDQGLLSVTLSRASGHAVhlLLDQMT 1833
Cdd:cd00110     1 GVSFSGSSYVR--LPTLPAPRTRLSISFSFRTTSPNGLLLYAgSQNGGDFLALELEDGRLVLRYDLGSGSLV--LSSKTP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 1834 VSDGRWHDLRLElqeepggRRGHHIFMvSLDFTLFQDTMAMGSELEGLKVKHLHVGGPPPSSKEEG---PQGLVGCIQGV 1910
Cdd:cd00110    77 LNDGQWHSVSVE-------RNGRSVTL-SVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGlpvSPGFVGCIRDL 148


                  .
gi 564365651 1911 W 1911
Cdd:cd00110   149 K 149
GPS smart00303
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ...
 2474-2527 2.47e-14

G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin REJ and polycystin.


:

Pssm-ID: 197639  Cd Length: 49  Bit Score: 69.34  E-value: 2.47e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 564365651   2474 SKAICVQWDPPGpadqhGMWTARDCELVHRNGSHARCRCSRTGTFGVLMDASPR 2527
Cdd:smart00303    1 FNPICVFWDESS-----GEWSTRGCELLETNGTHTTCSCNHLTTFAVLMDVPPI 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 2067-2105 8.76e-11

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


:

Pssm-ID: 238012  Cd Length: 50  Bit Score: 59.29  E-value: 8.76e-11
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 564365651 2067 PCDCYPVGSTSRSCAPHSGQCPCRPGALGRQCNSCDSPF 2105
Cdd:cd00055     1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGY 39
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 1176-1257 1.02e-09

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


:

Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 57.71  E-value: 1.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 1176 DTFPSGIIGRIPAYDPDVSD--HLFYSFERGNELQLLVVNQTSGELRLSRKLDNNRPLVASMLVTVTD-GLHSVTAQCVL 1252
Cdd:cd11304     9 NAPPGTVVLTVSATDPDSGEngEVTYSIVSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDgGGPPLSSTATV 88


                  ....*
gi 564365651 1253 RVVII 1257
Cdd:cd11304    89 TITVL 93
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1717-1748 5.40e-08

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 50.71  E-value: 5.40e-08
                          10        20        30
                  ....*....|....*....|....*....|...
gi 564365651 1717 CASG-PCKNGGLCSERWGGFSCDCPVGFGGKDC 1748
Cdd:cd00054     5 CASGnPCQNGGTCVNTVGSYRCSCPPGYTGRNC 37
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1973-2011 7.24e-08

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 50.71  E-value: 7.24e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 564365651 1973 VDACLL-NPCQNQGSCRHLQGGphgYTCDCASGYFGQHCE 2011
Cdd:cd00054     2 IDECASgNPCQNGGTCVNTVGS---YRCSCPPGYTGRNCE 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1428-1462 1.38e-07

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 49.56  E-value: 1.38e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 564365651 1428 DLCYS-NPCRNGGACARREGGYTCVCRPRFTGEDCE 1462
Cdd:cd00054     3 DECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1472-1505 2.66e-07

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 48.79  E-value: 2.66e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 564365651 1472 PGVCRNGGTCTNAPnGGFRCQCPAGgaFEGPRCE 1505
Cdd:cd00054     8 GNPCQNGGTCVNTV-GSYRCSCPPG--YTGRNCE 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1939-1973 6.91e-06

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 44.94  E-value: 6.91e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 564365651 1939 NPCASG-PCPPHANCKDLWQTFSCTCWPGYYGPGCV 1973
Cdd:cd00054     3 DECASGnPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 1994-2033 3.82e-04

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


:

Pssm-ID: 395007  Cd Length: 49  Bit Score: 40.41  E-value: 3.82e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 564365651  1994 PHGYTCDCASGYFGQHCEhrmdqQCPRGWWGSPTCGPCNC 2033
Cdd:pfam00053   15 PETGQCLCKPGVTGRHCD-----RCKPGYYGLPSDPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 2030-2054 2.11e-03

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


:

Pssm-ID: 238012  Cd Length: 50  Bit Score: 38.10  E-value: 2.11e-03
                          10        20
                  ....*....|....*....|....*
gi 564365651 2030 PCNCDVHKGFDPNCNKTSGQCHCKE 2054
Cdd:cd00055     1 PCDCNGHGSLSGQCDPGTGQCECKP 25
 
Name Accession Description Interval E-value
7tmB2_CELSR3 cd15993
Cadherin EGF LAG seven-pass G-type receptor 3, member of the class B2 family of ...
 2534-2724 1.77e-113

Cadherin EGF LAG seven-pass G-type receptor 3, member of the class B2 family of seven-transmembrane G protein-coupled receptors; The group IV adhesion GPCRs include the cadherin EGF LAG seven-pass G-type receptors (CELSRs) and their Drosophila homolog Flamingo (also known as Starry night). These receptors are also classified as that belongs to the EGF-TM7 group of subfamily B2 adhesion GPCRs, because they contain EGF-like domains. Functionally, the group IV receptors act as key regulators of many physiological processes such as endocrine cell differentiation, neuronal migration, dendrite growth, axon, guidance, lymphatic vessel and valve formation, and planar cell polarity (PCP) during embryonic development. Three mammalian orthologs of Flamingo, Celsr1-3, are widely expressed in the nervous system from embryonic development until the adult stage. Each Celsr exhibits different expression patterns in the developing brain, suggesting that they serve distinct functions. Mutations of CELSR1 cause neural tube defects in the nervous system, while mutations of CELSR2 are associated with coronary heart disease. Moreover, CELSR1 and several other PCP signaling molecules, such as dishevelled, prickle, frizzled, have been shown to be upregulated in B lymphocytes of chronic lymphocytic leukemia patients. Celsr3 is expressed in both the developing and adult mouse brain. It has been functionally implicated in proper neuronal migration and axon guidance in the CNS. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. In the case of CELSR/Flamingo/Starry night, their extracellular domains comprise nine cadherin repeats linked to a series of epidermal growth factor (EGF)-like and laminin globular (G)-like domains. The cadherin repeats contain sequence motifs that mediate calcium-dependent cell-cell adhesion by homophilic interactions. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320659 [Multi-domain]  Cd Length: 254  Bit Score: 361.08  E-value: 1.77e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2534 LELLAVFTHVVVAASVTALVLTAAVLLSLRSLKSNVRGIHANVAAALGVAELLFLLGIHRTHNQLLCTVVAILLHYFFLS 2613
Cdd:cd15993     1 LETLAIVTYSSVSASLAALVLTFSVLTCLRGLKSNTRGIHSNIAAALFLSELLFLLGINRTENQFLCTVVAILLHYFFLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2614 TFAWLLVQGLHLYRMQVEPRNVDRGAMRFYHALGWGVPAVLLGLAVGLDPEGYGNPDFCWISIHEPLIWSFAGPIVLVIV 2693
Cdd:cd15993    81 TFAWLFVQGLHIYRMQTEARNVNFGAMRFYYAIGWGVPAIITGLAVGLDPEGYGNPDFCWISIHDKLVWSFAGPIVVVIV 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 564365651 2694 MNGIMFLLAARTSCSTGQREAKKTSVLVLPR 2724
Cdd:cd15993   161 MNGVMFLLVARMSCSPGQKETKKTSVLMTLR 191
7tm_2 pfam00002
7 transmembrane receptor (Secretin family); This family is known as Family B, the ...
 2534-2720 2.48e-70

7 transmembrane receptor (Secretin family); This family is known as Family B, the secretin-receptor family or family 2 of the G-protein-coupled receptors (GCPRs). They have been described in many animal species, but not in plants, fungi or prokaryotes. Three distinct sub-families are recognized. Subfamily B1 contains classical hormone receptors, such as receptors for secretin and glucagon, that are all involved in cAMP-mediated signalling pathways. Subfamily B2 contains receptors with long extracellular N-termini, such as the leukocyte cell-surface antigen CD97; calcium-independent receptors for latrotoxin, and brain-specific angiogenesis inhibitors amongst others. Subfamily B3 includes Methuselah and other Drosophila proteins. Other than the typical seven-transmembrane region, characteriztic structural features include an amino-terminal extracellular domain involved in ligand binding, and an intracellular loop (IC3) required for specific G-protein coupling.


Pssm-ID: 459625 [Multi-domain]  Cd Length: 248  Bit Score: 237.18  E-value: 2.48e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  2534 LELLAVFTHVVVAASVTALVLTAAVLLSLRSLKSNVRGIHANVAAALGVAELLFLLGIHRTHNQ--------LLCTVVAI 2605
Cdd:pfam00002    1 ALSLKVIYTVGYSLSLVALLLAIAIFLLFRKLHCTRNYIHLNLFASFILRALLFLVGDAVLFNKqdldhcswVGCKVVAV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  2606 LLHYFFLSTFAWLLVQGLHLYRMQVEPRNVDRGAMRFYHALGWGVPAVLLGLAVGLDPEGYGNPDFCWISIHEPLIWSFA 2685
Cdd:pfam00002   81 FLHYFFLANFFWMLVEGLYLYTLLVEVFFSERKYFWWYLLIGWGVPALVVGIWAGVDPKGYGEDDGCWLSNENGLWWIIR 160

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 564365651  2686 GPIVLVIVMNGIMFLLAARTSCSTGQREAKKTSVL 2720
Cdd:pfam00002  161 GPILLIILVNFIIFINIVRILVQKLRETNMGKSDL 195
GAIN pfam16489
GPCR-Autoproteolysis INducing (GAIN) domain; The GAIN a domain of alpha-helices and ...
 2200-2448 1.88e-45

GPCR-Autoproteolysis INducing (GAIN) domain; The GAIN a domain of alpha-helices and beta-strands that is found in cell-adhesion GPCRs and precedes the GPS motif where the autoproteolysis occurs, family, pfam01825. The full GAIN domain, comprises the GPS and the GAIN, in cell-adhesion GPCRs, and is the functional unit for autoproteolysis. The GPS motif at the end of the GAIN domain is an ancient domain that exists in primitive ancestor organizms, and the full GAIN + GPS is conserved in all cell-adhesion GPCRs and all PKD1-related proteins.


Pssm-ID: 465137  Cd Length: 205  Bit Score: 163.98  E-value: 1.88e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  2200 EAKKLAQRLREVTgQTDHYFSQDVRVTARLLAYLlafeshqqgFGLTATQDA----HFNENLLWAGSALLAPETGDLWAA 2275
Cdd:pfam16489    1 GAKELARELRNAT-RHGPLYGGDVLTAVELLSQL---------FDLLATQDAtlsnAFLENFVQTVSNLLDPENRESWED 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  2276 LGQRAPGGSpgSAGLVRHLEEYAATLARNMDltYLNPVGLVTPNIMLSIDRMEQPSSSQgaHRYPRYHSNlfrgQDAWDP 2355
Cdd:pfam16489   71 LQQTERGTA--ATKLLRTLEEYALLLAQNMK--YLTPFTIVTPNIVLSVDRLDTHNFKG--ARFPRFPMK----GERPKD 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  2356 HTHVLLpsqspqpspsevlptssnaenatasgvvsPPAPLEPESEPGISIVILLVYRALGGLLPAQ--FQAERRGARLPQ 2433
Cdd:pfam16489  141 EDSVKL-----------------------------PPKAFKPPDSNGTVVVVFILYRNLGSLLPPSsrYDPDRRSLRLPR 191

                          250
                   ....*....|....*
gi 564365651  2434 NpVMNSPVVSVAVFR 2448
Cdd:pfam16489  192 R-VVNSPVVSASVHS 205
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 646-743 4.88e-38

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 138.60  E-value: 4.88e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  646 PFQVSVLENAPLGHSVIHIQAVDADHGENSRLEYSLTGVASDTPFVINSATGWVSVSGPLDRESVEHYFFGVEARDHGSP 725
Cdd:cd11304     1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGGGP 80

                          90
                  ....*....|....*...
gi 564365651  726 PLSASASVTVTVLDVNDN 743
Cdd:cd11304    81 PLSSTATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 956-1054 1.62e-35

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 131.28  E-value: 1.62e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  956 HYTGLVSEDAPPFTSVLQISATDRDAHANGRVQYTFQNGeDGDGDFTIEPTSGIVRTVRRLDREAVPVYELTAYAVDRGV 1035
Cdd:cd11304     1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSG-NEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGGG 79

                          90
                  ....*....|....*....
gi 564365651 1036 PPLRTPVSIQVTVQDVNDN 1054
Cdd:cd11304    80 PPLSSTATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 541-638 1.75e-34

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 128.20  E-value: 1.75e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  541 YVAQVREDVRPHTVVLRVTATDKDKDANGLVHYNIISGNSRGHFAIDSLTGEIQVMAPLDFEAEREYALRIRAQDAGRPP 620
Cdd:cd11304     2 YEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGGGPP 81

                          90
                  ....*....|....*...
gi 564365651  621 LSnNTGLASIQVVDINDH 638
Cdd:cd11304    82 LS-STATVTITVLDVNDN 98
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 1508-1691 1.42e-33

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 127.92  E-value: 1.42e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 1508 ARSFPPSSFVMFRGLR-QRFHLTLSLSFATVQPSGLLFYNGRLNeKHDFLALELVAGQVRLTYSTGESSTVVSPTVPggL 1586
Cdd:cd00110     1 GVSFSGSSYVRLPTLPaPRTRLSISFSFRTTSPNGLLLYAGSQN-GGDFLALELEDGRLVLRYDLGSGSLVLSSKTP--L 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 1587 SDGQWHTVHLRYYNkprtdalggaqgpskdKVAVLSVDDCNVavaLRFGAEIGNYscaaagvqtsskkSLDLTGPLLLGG 1666
Cdd:cd00110    78 NDGQWHSVSVERNG----------------RSVTLSVDGERV---VESGSPGGSA-------------LLNLDGPLYLGG 125

                         170       180
                  ....*....|....*....|....*.
gi 564365651 1667 VPNLPENFPV-SRKDFIGCMRDLHID 1691
Cdd:cd00110   126 LPEDLKSPGLpVSPGFVGCIRDLKVN 151
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 321-420 1.65e-33

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 125.50  E-value: 1.65e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  321 YQTLVPENEAAGTAVLRVVAQDPDPGEAGRLVYSLaalMNSRSLELFSIDPQSGLIRTAAALDRESMERHYLRVTAQDHG 400
Cdd:cd11304     2 YEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSI---VSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGG 78

                          90       100
                  ....*....|....*....|
gi 564365651  401 SPRLSATTMVAVTVADRNDH 420
Cdd:cd11304    79 GPPLSSTATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 428-532 2.02e-32

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 122.42  E-value: 2.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  428 QYRETLRENVEEGYPILQLRATDGDAPPNANLRYRFVGSPAARTaaaaaFEIDPRSGLISTSGRVDREHMESYELVVEAS 507
Cdd:cd11304     1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDGL-----FSIDPSTGEITTAKPLDREEQSSYTLTVTAT 75

                          90       100
                  ....*....|....*....|....*
gi 564365651  508 DQGQEpgPRSATVRVHITVLDENDN 532
Cdd:cd11304    76 DGGGP--PLSSTATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 853-948 6.65e-31

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 118.18  E-value: 6.65e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  853 HYSVSMNEDRPVGSTVVVISASDDDVGENARITYLL--EDNLPQFRIDADSGAITLQAPLDYEDQVTYTLAITARDNGIP 930
Cdd:cd11304     1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIvsGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGGGP 80

                          90
                  ....*....|....*...
gi 564365651  931 QKADTTYVEVMVNDVNDN 948
Cdd:cd11304    81 PLSSTATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 1062-1156 4.13e-30

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 115.87  E-value: 4.13e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 1062 EFEVRVKENSIVGSVVAQITAVDPDDGPNAHIMYQIVEGNIPELFQMDIFSGELTALIDLDYEARQEYVIVVQAT---SA 1138
Cdd:cd11304     1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATdggGP 80

                          90
                  ....*....|....*...
gi 564365651 1139 PLVSRATVHVRLVDQNDN 1156
Cdd:cd11304    81 PLSSTATVTITVLDVNDN 98
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 665-745 4.83e-30

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 115.14  E-value: 4.83e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651    665 QAVDADHGENSRLEYSLTGVASDTPFVINSATGWVSVSGPLDRESVEHYFFGVEARDHGSPPLSASASVTVTVLDVNDNR 744
Cdd:smart00112    1 SATDADSGENGKVTYSILSGNDDGLFSIDPETGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVLDVNDNA 80


                    .
gi 564365651    745 P 745
Cdd:smart00112   81 P 81
LamG smart00282
Laminin G domain;
1529-1693 7.67e-29

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 113.59  E-value: 7.67e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651   1529 TLSLSFATVQPSGLLFYNGRLNeKHDFLALELVAGQVRLTYSTGESSTVVSPTvPGGLSDGQWHTVHLRYYNkprtdalg 1608
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAGSKG-GGDYLALELRDGRLVLRYDLGSGPARLTSD-PTPLNDGQWHRVAVERNG-------- 70

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651   1609 gaqgpskdKVAVLSVDDCNVAVALRFGaeignyscaaagvqtsSKKSLDLTGPLLLGGVPNLPENFP-VSRKDFIGCMRD 1687
Cdd:smart00282   71 --------RSVTLSVDGGNRVSGESPG----------------GLTILNLDGPLYLGGLPEDLKLPPlPVTPGFRGCIRN 126


                    ....*.
gi 564365651   1688 LHIDGR 1693
Cdd:smart00282  127 LKVNGK 132
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 975-1056 3.28e-28

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 109.75  E-value: 3.28e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651    975 SATDRDAHANGRVQYTFqNGEDGDGDFTIEPTSGIVRTVRRLDREAVPVYELTAYAVDRGVPPLRTPVSIQVTVQDVNDN 1054
Cdd:smart00112    1 SATDADSGENGKVTYSI-LSGNDDGLFSIDPETGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVLDVNDN 79


                    ..
gi 564365651   1055 AP 1056
Cdd:smart00112   80 AP 81
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
 1534-1693 4.12e-28

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 460494 [Multi-domain]  Cd Length: 126  Bit Score: 111.36  E-value: 4.12e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  1534 FATVQPSGLLFYNGrlNEKHDFLALELVAGQVRLTYSTGESSTVVSPTvPGGLSDGQWHTVHLRYynkprtdalggaqgp 1613
Cdd:pfam02210    1 FRTRQPNGLLLYAG--GGGSDFLALELVNGRLVLRYDLGSGPESLLSS-GKNLNDGQWHSVRVER--------------- 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  1614 sKDKVAVLSVDDCNVAVALRFGAEIGnyscaaagvqtsskksLDLTGPLLLGGVPN-LPENFPVSRKDFIGCMRDLHIDG 1692
Cdd:pfam02210   63 -NGNTLTLSVDGQTVVSSLPPGESLL----------------LNLNGPLYLGGLPPlLLLPALPVRAGFVGCIRDVRVNG 125


                   .
gi 564365651  1693 R 1693
Cdd:pfam02210  126 E 126
Cadherin pfam00028
Cadherin domain;
541-632 7.77e-28

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 109.31  E-value: 7.77e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651   541 YVAQVREDVRPHTVVLRVTATDKDKDANGLVHYNIISGNSRGHFAIDSLTGEIQVMAPLDFEAEREYALRIRAQDAGRPP 620
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPNGRIFYSILGGGPGGNFRIDPDTGDISTTKPLDRESIGEYELTVEATDSGGPP 80

                           90
                   ....*....|..
gi 564365651   621 LSnNTGLASIQV 632
Cdd:pfam00028   81 LS-STATVTITV 91
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 447-534 5.46e-26

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 103.58  E-value: 5.46e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651    447 RATDGDAPPNANLRYRFVGSPAARTaaaaaFEIDPRSGLISTSGRVDREHMESYELVVEASDQGQEpgPRSATVRVHITV 526
Cdd:smart00112    1 SATDADSGENGKVTYSILSGNDDGL-----FSIDPETGEITTTKPLDREEQPEYTLTVEATDGGGP--PLSSTATVTITV 73


                    ....*...
gi 564365651    527 LDENDNAP 534
Cdd:smart00112   74 LDVNDNAP 81
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 559-640 8.97e-26

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 102.81  E-value: 8.97e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651    559 TATDKDKDANGLVHYNIISGNSRGHFAIDSLTGEIQVMAPLDFEAEREYALRIRAQDAGRPPLSnNTGLASIQVVDINDH 638
Cdd:smart00112    1 SATDADSGENGKVTYSILSGNDDGLFSIDPETGEITTTKPLDREEQPEYTLTVEATDGGGPPLS-STATVTITVLDVNDN 79


                    ..
gi 564365651    639 SP 640
Cdd:smart00112   80 AP 81
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 872-950 1.05e-25

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 102.81  E-value: 1.05e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651    872 SASDDDVGENARITYLLEDNLPQ--FRIDADSGAITLQAPLDYEDQVTYTLAITARDNGIPQKADTTYVEVMVNDVNDNA 949
Cdd:smart00112    1 SATDADSGENGKVTYSILSGNDDglFSIDPETGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVLDVNDNA 80


                    .
gi 564365651    950 P 950
Cdd:smart00112   81 P 81
Cadherin pfam00028
Cadherin domain;
647-738 3.76e-25

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 101.61  E-value: 3.76e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651   647 FQVSVLENAPLGHSVIHIQAVDADHGENSRLEYSLTGVASDTPFVINSATGWVSVSGPLDRESVEHYFFGVEARDHGSPP 726
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPNGRIFYSILGGGPGGNFRIDPDTGDISTTKPLDRESIGEYELTVEATDSGGPP 80

                           90
                   ....*....|..
gi 564365651   727 LSASASVTVTVL 738
Cdd:pfam00028   81 LSSTATVTITVL 92
Cadherin pfam00028
Cadherin domain;
957-1049 4.61e-25

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 101.22  E-value: 4.61e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651   957 YTGLVSEDAPPFTSVLQISATDRDAHANGRVQYTFQNGEDGdGDFTIEPTSGIVRTVRRLDREAVPVYELTAYAVDRGVP 1036
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPNGRIFYSILGGGPG-GNFRIDPDTGDISTTKPLDRESIGEYELTVEATDSGGP 79

                           90
                   ....*....|...
gi 564365651  1037 PLRTPVSIQVTVQ 1049
Cdd:pfam00028   80 PLSSTATVTITVL 92
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 339-422 2.03e-24

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 98.96  E-value: 2.03e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651    339 VAQDPDPGEAGRLVYSLAalmNSRSLELFSIDPQSGLIRTAAALDRESMERHYLRVTAQDHGSPRLSATTMVAVTVADRN 418
Cdd:smart00112    1 SATDADSGENGKVTYSIL---SGNDDGLFSIDPETGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVLDVN 77


                    ....
gi 564365651    419 DHAP 422
Cdd:smart00112   78 DNAP 81
Cadherin pfam00028
Cadherin domain;
429-527 7.09e-23

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 95.06  E-value: 7.09e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651   429 YRETLRENVEEGYPILQLRATDGDAPPNANLRYRFVGSPAARTaaaaaFEIDPRSGLISTSGRVDREHMESYELVVEASD 508
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPNGRIFYSILGGGPGGN-----FRIDPDTGDISTTKPLDRESIGEYELTVEATD 75

                           90
                   ....*....|....*....
gi 564365651   509 QGqePGPRSATVRVHITVL 527
Cdd:pfam00028   76 SG--GPPLSSTATVTITVL 92
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 1081-1158 8.44e-23

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 94.34  E-value: 8.44e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651   1081 TAVDPDDGPNAHIMYQIVEGNIPELFQMDIFSGELTALIDLDYEARQEYVIVVQAT---SAPLVSRATVHVRLVDQNDNS 1157
Cdd:smart00112    1 SATDADSGENGKVTYSILSGNDDGLFSIDPETGEITTTKPLDREEQPEYTLTVEATdggGPPLSSTATVTITVLDVNDNA 80


                    .
gi 564365651   1158 P 1158
Cdd:smart00112   81 P 81
Cadherin pfam00028
Cadherin domain;
321-414 7.11e-22

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 91.98  E-value: 7.11e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651   321 YQTLVPENEAAGTAVLRVVAQDPDPGEAGRLVYSLaalMNSRSLELFSIDPQSGLIRTAAALDRESMERHYLRVTAQDHG 400
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPNGRIFYSI---LGGGPGGNFRIDPDTGDISTTKPLDRESIGEYELTVEATDSG 77

                           90
                   ....*....|....
gi 564365651   401 SPRLSATTMVAVTV 414
Cdd:pfam00028   78 GPPLSSTATVTITV 91
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 751-845 1.27e-21

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 91.61  E-value: 1.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  751 EYHLRLNEDAAVGTSVVSVTAVDRD--ANSAISYQITGGNTRNRFAISTQggMGLVTLALPLDYKQERYFKLVLTASDR- 827
Cdd:cd11304     1 SYEVSVPENAPPGTVVLTVSATDPDsgENGEVTYSIVSGNEDGLFSIDPS--TGEITTAKPLDREEQSSYTLTVTATDGg 78

                          90       100
                  ....*....|....*....|
gi 564365651  828 --ALHDHCYVHINITDANTH 845
Cdd:cd11304    79 gpPLSSTATVTITVLDVNDN 98
Cadherin pfam00028
Cadherin domain;
854-942 1.61e-21

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 91.21  E-value: 1.61e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651   854 YSVSMNEDRPVGSTVVVISASDDDVGENARITY-LLEDNLPQ-FRIDADSGAITLQAPLDYEDQVTYTLAITARDNGIPQ 931
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPNGRIFYsILGGGPGGnFRIDPDTGDISTTKPLDRESIGEYELTVEATDSGGPP 80

                           90
                   ....*....|.
gi 564365651   932 KADTTYVEVMV 942
Cdd:pfam00028   81 LSSTATVTITV 91
Cadherin pfam00028
Cadherin domain;
1063-1150 1.83e-21

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 90.82  E-value: 1.83e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  1063 FEVRVKENSIVGSVVAQITAVDPDDGPNAHIMYQIVEGNIPELFQMDIFSGELTALIDLDYEARQEYVIVVQATSA---P 1139
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPNGRIFYSILGGGPGGNFRIDPDTGDISTTKPLDRESIGEYELTVEATDSggpP 80

                           90
                   ....*....|.
gi 564365651  1140 LVSRATVHVRL 1150
Cdd:pfam00028   81 LSSTATVTITV 91
HormR smart00008
Domain present in hormone receptors;
2117-2181 1.23e-19

Domain present in hormone receptors;


Pssm-ID: 214468  Cd Length: 70  Bit Score: 84.87  E-value: 1.23e-19
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564365651   2117 YDACPKSLRSGVWWPQTKFGVLATVPCPRGALGLRGTGAAVRLCDEDHGWLE--PDFFNCTSPAFRE 2181
Cdd:smart00008    2 DLGCPATWDGIICWPQTPAGQLVEVPCPKYFSGFSYKTGASRNCTENGGWSPpfPNYSNCTSNDYEE 68
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 1755-1911 2.94e-18

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 84.01  E-value: 2.94e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 1755 PYHFQGNGTLSwdFGNDMPVSVPWYLGLSFRTRATKGVLMQV-QLGPHSVLLCKLDQGLLSVTLSRASGHAVhlLLDQMT 1833
Cdd:cd00110     1 GVSFSGSSYVR--LPTLPAPRTRLSISFSFRTTSPNGLLLYAgSQNGGDFLALELEDGRLVLRYDLGSGSLV--LSSKTP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 1834 VSDGRWHDLRLElqeepggRRGHHIFMvSLDFTLFQDTMAMGSELEGLKVKHLHVGGPPPSSKEEG---PQGLVGCIQGV 1910
Cdd:cd00110    77 LNDGQWHSVSVE-------RNGRSVTL-SVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGlpvSPGFVGCIRDL 148


                  .
gi 564365651 1911 W 1911
Cdd:cd00110   149 K 149
Cadherin pfam00028
Cadherin domain;
752-840 6.10e-16

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 75.41  E-value: 6.10e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651   752 YHLRLNEDAAVGTSVVSVTAVDRD--ANSAISYQITGGNTRNRFAISTQGgmGLVTLALPLDYKQERYFKLVLTASDRAL 829
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDlgPNGRIFYSILGGGPGGNFRIDPDT--GDISTTKPLDRESIGEYELTVEATDSGG 78

                           90
                   ....*....|....
gi 564365651   830 H---DHCYVHINIT 840
Cdd:pfam00028   79 PplsSTATVTITVL 92
LamG smart00282
Laminin G domain;
1779-1911 9.42e-16

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 76.22  E-value: 9.42e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651   1779 YLGLSFRTRATKGVLMQV-QLGPHSVLLCKLDQGLLSVTLSRASGhAVHLLLDQMTVSDGRWHDLRLElqeepggRRGHH 1857
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAgSKGGGDYLALELRDGRLVLRYDLGSG-PARLTSDPTPLNDGQWHRVAVE-------RNGRS 72

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 564365651   1858 IFMvSLDFTLFQDTMAMGSElEGLKVK-HLHVGGPPPSSKEEG---PQGLVGCIQGVW 1911
Cdd:smart00282   73 VTL-SVDGGNRVSGESPGGL-TILNLDgPLYLGGLPEDLKLPPlpvTPGFRGCIRNLK 128
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 770-847 1.52e-14

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 70.84  E-value: 1.52e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651    770 TAVDRD--ANSAISYQITGGNTRNRFAISTQGGMglVTLALPLDYKQERYFKLVLTASDRA---LHDHCYVHINITDANT 844
Cdd:smart00112    1 SATDADsgENGKVTYSILSGNDDGLFSIDPETGE--ITTTKPLDREEQPEYTLTVEATDGGgppLSSTATVTITVLDVND 78


                    ...
gi 564365651    845 HRP 847
Cdd:smart00112   79 NAP 81
GPS smart00303
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ...
 2474-2527 2.47e-14

G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin REJ and polycystin.


Pssm-ID: 197639  Cd Length: 49  Bit Score: 69.34  E-value: 2.47e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 564365651   2474 SKAICVQWDPPGpadqhGMWTARDCELVHRNGSHARCRCSRTGTFGVLMDASPR 2527
Cdd:smart00303    1 FNPICVFWDESS-----GEWSTRGCELLETNGTHTTCSCNHLTTFAVLMDVPPI 49
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
 1784-1910 1.01e-13

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 460494 [Multi-domain]  Cd Length: 126  Bit Score: 70.14  E-value: 1.01e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  1784 FRTRATKGVLMQVQLGPHSVLLCKLDQGLLSVTLSRASGHaVHLLLDQMTVSDGRWHDLRLElqeepggRRGHHIFMvSL 1863
Cdd:pfam02210    1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGP-ESLLSSGKNLNDGQWHSVRVE-------RNGNTLTL-SV 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 564365651  1864 DFTLFQDTMAMGSELEGLKVKHLHVGGPPPSSKEEGP---QGLVGCIQGV 1910
Cdd:pfam02210   72 DGQTVVSSLPPGESLLLNLNGPLYLGGLPPLLLLPALpvrAGFVGCIRDV 121
HRM pfam02793
Hormone receptor domain; This extracellular domain contains four conserved cysteines that ...
 2117-2177 7.14e-13

Hormone receptor domain; This extracellular domain contains four conserved cysteines that probably for disulphide bridges. The domain is found in a variety of hormone receptors. It may be a ligand binding domain.


Pssm-ID: 397086  Cd Length: 64  Bit Score: 65.47  E-value: 7.14e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564365651  2117 YDACPKSLRSGVWWPQTKFGVLATVPCPRGALGLRGTGAAVRLCDEDHGWLEP---DFFNCTSP 2177
Cdd:pfam02793    1 GLGCPRTWDGILCWPRTPAGETVEVPCPDYFSGFDPRGNASRNCTEDGTWSEHppsNYSNCTSN 64
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 2067-2105 8.76e-11

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 59.29  E-value: 8.76e-11
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 564365651 2067 PCDCYPVGSTSRSCAPHSGQCPCRPGALGRQCNSCDSPF 2105
Cdd:cd00055     1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGY 39
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
2068-2113 1.10e-10

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 58.86  E-value: 1.10e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 564365651   2068 CDCYPVGSTSRSCAPHSGQCPCRPGALGRQCNSCDSPFAEVTASGC 2113
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 1176-1257 1.02e-09

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 57.71  E-value: 1.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 1176 DTFPSGIIGRIPAYDPDVSD--HLFYSFERGNELQLLVVNQTSGELRLSRKLDNNRPLVASMLVTVTD-GLHSVTAQCVL 1252
Cdd:cd11304     9 NAPPGTVVLTVSATDPDSGEngEVTYSIVSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDgGGPPLSSTATV 88


                  ....*
gi 564365651 1253 RVVII 1257
Cdd:cd11304    89 TITVL 93
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 2068-2101 3.13e-09

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 54.67  E-value: 3.13e-09
                           10        20        30
                   ....*....|....*....|....*....|....
gi 564365651  2068 CDCYPVGSTSRSCAPHSGQCPCRPGALGRQCNSC 2101
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRC 34
GPS pfam01825
GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for ...
 2476-2521 5.90e-09

GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for auto-proteolysis, so is thus named, GPS. The GPS motif is a conserved sequence of ~40 amino acids containing canonical cysteine and tryptophan residues, and is the most highly conserved part of the domain. In most, if not all, cell-adhesion GPCRs these undergo autoproteolysis in the GPS between a conserved aliphatic residue (usually a leucine) and a threonine, serine, or cysteine residue. In higher eukaryotes this motif is found embedded in the C-terminal beta-stranded part of a GAIN domain - GPCR-Autoproteolysis INducing (GAIN). The GAIN-GPS domain adopts a fold in which the GPS motif, at the C-terminus, forms five beta-strands that are tightly integrated into the overall GAIN domain. The GPS motif, evolutionarily conserved from tetrahymena to mammals, is the only extracellular domain shared by all human cell-adhesion GPCRs and PKD proteins, and is the locus of multiple human disease mutations. The GAIN-GPS domain is both necessary and sufficient functionally for autoproteolysis, suggesting an autoproteolytic mechanism whereby the overall GAIN domain fine-tunes the chemical environment in the GPS to catalyze peptide bond hydrolysis. In the cell-adhesion GPCRs and PKD proteins, the GPS motif is always located at the end of their long N-terminal extracellular regions, immediately before the first transmembrane helix of the respective protein.


Pssm-ID: 460350  Cd Length: 44  Bit Score: 53.85  E-value: 5.90e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 564365651  2476 AICVQWDPPGpaDQHGMWTARDCELVHRNGSHARCRCSRTGTFGVL 2521
Cdd:pfam01825    1 PQCVFWDFTN--STTGRWSTEGCTTVSLNDTHTVCSCNHLTSFAVL 44
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1717-1748 5.40e-08

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 50.71  E-value: 5.40e-08
                          10        20        30
                  ....*....|....*....|....*....|...
gi 564365651 1717 CASG-PCKNGGLCSERWGGFSCDCPVGFGGKDC 1748
Cdd:cd00054     5 CASGnPCQNGGTCVNTVGSYRCSCPPGYTGRNC 37
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1973-2011 7.24e-08

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 50.71  E-value: 7.24e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 564365651 1973 VDACLL-NPCQNQGSCRHLQGGphgYTCDCASGYFGQHCE 2011
Cdd:cd00054     2 IDECASgNPCQNGGTCVNTVGS---YRCSCPPGYTGRNCE 38
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 1717-1747 8.06e-08

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 50.07  E-value: 8.06e-08
                           10        20        30
                   ....*....|....*....|....*....|.
gi 564365651  1717 CASGPCKNGGLCSERWGGFSCDCPVGFGGKD 1747
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1428-1462 1.38e-07

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 49.56  E-value: 1.38e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 564365651 1428 DLCYS-NPCRNGGACARREGGYTCVCRPRFTGEDCE 1462
Cdd:cd00054     3 DECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1472-1505 2.66e-07

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 48.79  E-value: 2.66e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 564365651 1472 PGVCRNGGTCTNAPnGGFRCQCPAGgaFEGPRCE 1505
Cdd:cd00054     8 GNPCQNGGTCVNTV-GSYRCSCPPG--YTGRNCE 38
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 1976-2009 2.71e-06

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 45.84  E-value: 2.71e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 564365651  1976 CLLNPCQNQGSCRHlqgGPHGYTCDCASGYFGQH 2009
Cdd:pfam00008    1 CAPNPCSNGGTCVD---TPGGYTCICPEGYTGKR 31
EGF_CA smart00179
Calcium-binding EGF-like domain;
1472-1505 5.49e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 45.32  E-value: 5.49e-06
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 564365651   1472 PGVCRNGGTCTNAPnGGFRCQCPAGgaFE-GPRCE 1505
Cdd:smart00179    8 GNPCQNGGTCVNTV-GSYRCECPPG--YTdGRNCE 39
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1939-1973 6.91e-06

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 44.94  E-value: 6.91e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 564365651 1939 NPCASG-PCPPHANCKDLWQTFSCTCWPGYYGPGCV 1973
Cdd:cd00054     3 DECASGnPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 1430-1460 7.37e-06

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 44.68  E-value: 7.37e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 564365651  1430 CYSNPCRNGGACARREGGYTCVCRPRFTGED 1460
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
EGF_CA smart00179
Calcium-binding EGF-like domain;
1428-1462 1.63e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 43.77  E-value: 1.63e-05
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 564365651   1428 DLCYS-NPCRNGGACARREGGYTCVCRPRFT-GEDCE 1462
Cdd:smart00179    3 DECASgNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
EGF_CA smart00179
Calcium-binding EGF-like domain;
1717-1748 1.82e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 43.77  E-value: 1.82e-05
                            10        20        30
                    ....*....|....*....|....*....|....
gi 564365651   1717 CAS-GPCKNGGLCSERWGGFSCDCPVGF-GGKDC 1748
Cdd:smart00179    5 CASgNPCQNGGTCVNTVGSYRCECPPGYtDGRNC 38
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 1994-2033 3.82e-04

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 40.41  E-value: 3.82e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 564365651  1994 PHGYTCDCASGYFGQHCEhrmdqQCPRGWWGSPTCGPCNC 2033
Cdd:pfam00053   15 PETGQCLCKPGVTGRHCD-----RCKPGYYGLPSDPPQGC 49
hEGF pfam12661
Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six ...
 1475-1496 7.94e-04

Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six conserved residues disulfide-bonded into the characteriztic 'ababcc' pattern. They are involved in growth and proliferation of cells, in proteins of the Notch/Delta pathway, neurogulin and selectins. hEGFs are also found in mosaic proteins with four-disulfide laminin EGFs such as aggrecan and perlecan. The core fold of the EGF domain consists of two small beta-hairpins packed against each other. Two major structural variants have been identified based on the structural context of the C-terminal Cys residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In hEGFs the C-terminal thiol resides in the beta-turn, resulting in shorter loop-lengths between the Cys residues of disulfide 'c', typically C[8-9]XC. These shorter loop-lengths are also typical of the four-disulfide EGF domains, laminin ad integrin. Tandem hEGF domains have six linking residues between terminal cysteines of adjacent domains. hEGF domains may or may not bind calcium in the linker region. hEGF domains with the consensus motif CXD4X[F,Y]XCXC are hydroxylated exclusively in the Asp residue.


Pssm-ID: 463660  Cd Length: 22  Bit Score: 38.85  E-value: 7.94e-04
                           10        20
                   ....*....|....*....|..
gi 564365651  1475 CRNGGTCTNAPNgGFRCQCPAG 1496
Cdd:pfam12661    1 CQNGGTCVDGVN-GYKCQCPPG 21
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 1188-1257 1.77e-03

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 39.64  E-value: 1.77e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564365651   1188 AYDPDVSD--HLFYSFERGNELQLLVVNQTSGELRLSRKLDNNRPLVASMLVTVTD-GLHSVTAQCVLRVVII 1257
Cdd:smart00112    2 ATDADSGEngKVTYSILSGNDDGLFSIDPETGEITTTKPLDREEQPEYTLTVEATDgGGPPLSSTATVTITVL 74
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 2030-2054 2.11e-03

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 38.10  E-value: 2.11e-03
                          10        20
                  ....*....|....*....|....*
gi 564365651 2030 PCNCDVHKGFDPNCNKTSGQCHCKE 2054
Cdd:cd00055     1 PCDCNGHGSLSGQCDPGTGQCECKP 25
EGF_CA smart00179
Calcium-binding EGF-like domain;
1939-1973 2.11e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 38.00  E-value: 2.11e-03
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 564365651   1939 NPCAS-GPCPPHANCKDLWQTFSCTCWPGYY-GPGCV 1973
Cdd:smart00179    3 DECASgNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
2031-2054 3.31e-03

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 37.68  E-value: 3.31e-03
                            10        20
                    ....*....|....*....|....
gi 564365651   2031 CNCDVHKGFDPNCNKTSGQCHCKE 2054
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKP 24
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 2031-2067 3.75e-03

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 37.72  E-value: 3.75e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 564365651  2031 CNCDVHKGFDPNCNKTSGQCHCKEfHYRPRGSDSCLP 2067
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKP-GVTGRHCDRCKP 36
 
Name Accession Description Interval E-value
7tmB2_CELSR3 cd15993
Cadherin EGF LAG seven-pass G-type receptor 3, member of the class B2 family of ...
 2534-2724 1.77e-113

Cadherin EGF LAG seven-pass G-type receptor 3, member of the class B2 family of seven-transmembrane G protein-coupled receptors; The group IV adhesion GPCRs include the cadherin EGF LAG seven-pass G-type receptors (CELSRs) and their Drosophila homolog Flamingo (also known as Starry night). These receptors are also classified as that belongs to the EGF-TM7 group of subfamily B2 adhesion GPCRs, because they contain EGF-like domains. Functionally, the group IV receptors act as key regulators of many physiological processes such as endocrine cell differentiation, neuronal migration, dendrite growth, axon, guidance, lymphatic vessel and valve formation, and planar cell polarity (PCP) during embryonic development. Three mammalian orthologs of Flamingo, Celsr1-3, are widely expressed in the nervous system from embryonic development until the adult stage. Each Celsr exhibits different expression patterns in the developing brain, suggesting that they serve distinct functions. Mutations of CELSR1 cause neural tube defects in the nervous system, while mutations of CELSR2 are associated with coronary heart disease. Moreover, CELSR1 and several other PCP signaling molecules, such as dishevelled, prickle, frizzled, have been shown to be upregulated in B lymphocytes of chronic lymphocytic leukemia patients. Celsr3 is expressed in both the developing and adult mouse brain. It has been functionally implicated in proper neuronal migration and axon guidance in the CNS. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. In the case of CELSR/Flamingo/Starry night, their extracellular domains comprise nine cadherin repeats linked to a series of epidermal growth factor (EGF)-like and laminin globular (G)-like domains. The cadherin repeats contain sequence motifs that mediate calcium-dependent cell-cell adhesion by homophilic interactions. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320659 [Multi-domain]  Cd Length: 254  Bit Score: 361.08  E-value: 1.77e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2534 LELLAVFTHVVVAASVTALVLTAAVLLSLRSLKSNVRGIHANVAAALGVAELLFLLGIHRTHNQLLCTVVAILLHYFFLS 2613
Cdd:cd15993     1 LETLAIVTYSSVSASLAALVLTFSVLTCLRGLKSNTRGIHSNIAAALFLSELLFLLGINRTENQFLCTVVAILLHYFFLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2614 TFAWLLVQGLHLYRMQVEPRNVDRGAMRFYHALGWGVPAVLLGLAVGLDPEGYGNPDFCWISIHEPLIWSFAGPIVLVIV 2693
Cdd:cd15993    81 TFAWLFVQGLHIYRMQTEARNVNFGAMRFYYAIGWGVPAIITGLAVGLDPEGYGNPDFCWISIHDKLVWSFAGPIVVVIV 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 564365651 2694 MNGIMFLLAARTSCSTGQREAKKTSVLVLPR 2724
Cdd:cd15993   161 MNGVMFLLVARMSCSPGQKETKKTSVLMTLR 191
7tmB2_CELSR_Adhesion_IV cd15441
cadherin EGF LAG seven-pass G-type receptors, group IV adhesion GPCRs, member of the class B2 ...
 2536-2725 4.71e-93

cadherin EGF LAG seven-pass G-type receptors, group IV adhesion GPCRs, member of the class B2 family of seven-transmembrane G protein-coupled receptors; The group IV adhesion GPCRs include the cadherin EGF LAG seven-pass G-type receptors (CELSRs) and their Drosophila homolog Flamingo (also known as Starry night). These receptors are also classified as that belongs to the EGF-TM7 group of subfamily B2 adhesion GPCRs, because they contain EGF-like domains. Functionally, the group IV receptors act as key regulators of many physiological processes such as endocrine cell differentiation, neuronal migration, dendrite growth, axon, guidance, lymphatic vessel and valve formation, and planar cell polarity (PCP) during embryonic development. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. In the case of CELSR/Flamingo/Starry night, their extracellular domains comprise nine cadherin repeats linked to a series of epidermal growth factor (EGF)-like and laminin globular (G)-like domains. The cadherin repeats contain sequence motifs that mediate calcium-dependent cell-cell adhesion by homophilic interactions. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. Three mammalian orthologs of Flamingo, Celsr1-3, are widely expressed in the nervous system from embryonic development until the adult stage. Each Celsr exhibits different expression patterns in the developing brain, suggesting that they serve distinct functions. Mutations of CELSR1 cause neural tube defects in the nervous system, while mutations of CELSR2 are associated with coronary heart disease. Moreover, CELSR1 and several other PCP signaling molecules, such as dishevelled, prickle, frizzled, have been shown to be upregulated in B lymphocytes of chronic lymphocytic leukemia patients. Celsr3 is expressed in both the developing and adult mouse brain. It has been functionally implicated in proper neuron migration and axon guidance in the CNS.


Pssm-ID: 320557 [Multi-domain]  Cd Length: 254  Bit Score: 302.63  E-value: 4.71e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2536 LLAVFTHVVVAASVTALVLTAAVLLSLRSLKSNVRGIHANVAAALGVAELLFLLGIHRTHNQLLCTVVAILLHYFFLSTF 2615
Cdd:cd15441     3 LLKIVTYIGIGISLVLLVIAFLVLSCLRGLQSNSNSIHKNLVACLLLAELLFLLGINQTENLFPCKLIAILLHYFYLSAF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2616 AWLLVQGLHLYRMQVEPRNVDRGAMRFYHALGWGVPAVLLGLAVGLDPEGYGNPDFCWISIHEPLIWSFAGPIVLVIVMN 2695
Cdd:cd15441    83 SWLLVESLHLYRMLTEPRDINHGHMRFYYLLGYGIPAIIVGLSVGLRPDGYGNPDFCWLSVNETLIWSFAGPIAFVIVIT 162

                         170       180       190
                  ....*....|....*....|....*....|
gi 564365651 2696 GIMFLLAARTSCSTGQREAKKTSVLVLPRL 2725
Cdd:cd15441   163 LIIFILALRASCTLKRHVLEKASVRTDLRS 192
7tmB2_CELSR1 cd15991
Cadherin EGF LAG seven-pass G-type receptor 1, member of the class B2 family of ...
 2537-2724 5.61e-77

Cadherin EGF LAG seven-pass G-type receptor 1, member of the class B2 family of seven-transmembrane G protein-coupled receptors; The group IV adhesion GPCRs include the cadherin EGF LAG seven-pass G-type receptors (CELSRs) and their Drosophila homolog Flamingo (also known as Starry night). These receptors are also classified as that belongs to the EGF-TM7 group of subfamily B2 adhesion GPCRs, because they contain EGF-like domains. Functionally, the group IV receptors act as key regulators of many physiological processes such as endocrine cell differentiation, neuronal migration, dendrite growth, axon, guidance, lymphatic vessel and valve formation, and planar cell polarity (PCP) during embryonic development. Three mammalian orthologs of Flamingo, Celsr1-3, are widely expressed in the nervous system from embryonic development until the adult stage. Each Celsr exhibits different expression patterns in the developing brain, suggesting that they serve distinct functions. Mutations of CELSR1 cause neural tube defects in the nervous system, while mutations of CELSR2 are associated with coronary heart disease. Moreover, CELSR1 and several other PCP signaling molecules, such as dishevelled, prickle, frizzled, have been shown to be upregulated in B lymphocytes of chronic lymphocytic leukemia patients. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. In the case of CELSR/Flamingo/Starry night, their extracellular domains comprise nine cadherin repeats linked to a series of epidermal growth factor (EGF)-like and laminin globular (G)-like domains. The cadherin repeats contain sequence motifs that mediate calcium-dependent cell-cell adhesion by homophilic interactions. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320657 [Multi-domain]  Cd Length: 254  Bit Score: 256.31  E-value: 5.61e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2537 LAVFTHVVVAASVTALVLTAAVLLSLRSLKSNVRGIHANVAAALGVAELLFLLGIHRTHNQLLCTVVAILLHYFFLSTFA 2616
Cdd:cd15991     4 LKIITYTTVSLSLVALLITFILLVLIRTLRSNLHSIHKNLVAALFFSELIFLIGINQTENPFVCTVVAILLHYFYMSTFA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2617 WLLVQGLHLYRMQVEPRNVDRGAMRFYHALGWGVPAVLLGLAVGLDPEGYGNPDFCWISIHEPLIWSFAGPIVLVIVMNG 2696
Cdd:cd15991    84 WMFVEGLHIYRMLTEVRNINTGHMRFYYVVGWGIPAIITGLAVGLDPQGYGNPDFCWLSVQDTLIWSFAGPIGIVVIINT 163

                         170       180
                  ....*....|....*....|....*...
gi 564365651 2697 IMFLLAARTSCSTGQREAKKTSVLVLPR 2724
Cdd:cd15991   164 VIFVLAAKASCGRRQRYFEKSGVISMLR 191
7tm_2 pfam00002
7 transmembrane receptor (Secretin family); This family is known as Family B, the ...
 2534-2720 2.48e-70

7 transmembrane receptor (Secretin family); This family is known as Family B, the secretin-receptor family or family 2 of the G-protein-coupled receptors (GCPRs). They have been described in many animal species, but not in plants, fungi or prokaryotes. Three distinct sub-families are recognized. Subfamily B1 contains classical hormone receptors, such as receptors for secretin and glucagon, that are all involved in cAMP-mediated signalling pathways. Subfamily B2 contains receptors with long extracellular N-termini, such as the leukocyte cell-surface antigen CD97; calcium-independent receptors for latrotoxin, and brain-specific angiogenesis inhibitors amongst others. Subfamily B3 includes Methuselah and other Drosophila proteins. Other than the typical seven-transmembrane region, characteriztic structural features include an amino-terminal extracellular domain involved in ligand binding, and an intracellular loop (IC3) required for specific G-protein coupling.


Pssm-ID: 459625 [Multi-domain]  Cd Length: 248  Bit Score: 237.18  E-value: 2.48e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  2534 LELLAVFTHVVVAASVTALVLTAAVLLSLRSLKSNVRGIHANVAAALGVAELLFLLGIHRTHNQ--------LLCTVVAI 2605
Cdd:pfam00002    1 ALSLKVIYTVGYSLSLVALLLAIAIFLLFRKLHCTRNYIHLNLFASFILRALLFLVGDAVLFNKqdldhcswVGCKVVAV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  2606 LLHYFFLSTFAWLLVQGLHLYRMQVEPRNVDRGAMRFYHALGWGVPAVLLGLAVGLDPEGYGNPDFCWISIHEPLIWSFA 2685
Cdd:pfam00002   81 FLHYFFLANFFWMLVEGLYLYTLLVEVFFSERKYFWWYLLIGWGVPALVVGIWAGVDPKGYGEDDGCWLSNENGLWWIIR 160

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 564365651  2686 GPIVLVIVMNGIMFLLAARTSCSTGQREAKKTSVL 2720
Cdd:pfam00002  161 GPILLIILVNFIIFINIVRILVQKLRETNMGKSDL 195
7tmB2_CELSR2 cd15992
Cadherin EGF LAG seven-pass G-type receptor 2, member of the class B2 family of ...
 2537-2721 6.88e-68

Cadherin EGF LAG seven-pass G-type receptor 2, member of the class B2 family of seven-transmembrane G protein-coupled receptors; The group IV adhesion GPCRs include the cadherin EGF LAG seven-pass G-type receptors (CELSRs) and their Drosophila homolog Flamingo (also known as Starry night). These receptors are also classified as that belongs to the EGF-TM7 group of subfamily B2 adhesion GPCRs, because they contain EGF-like domains. Functionally, the group IV receptors act as key regulators of many physiological processes such as endocrine cell differentiation, neuronal migration, dendrite growth, axon, guidance, lymphatic vessel and valve formation, and planar cell polarity (PCP) during embryonic development. Three mammalian orthologs of Flamingo, Celsr1-3, are widely expressed in the nervous system from embryonic development until the adult stage. Each Celsr exhibits different expression patterns in the developing brain, suggesting that they serve distinct functions. Mutations of CELSR1 cause neural tube defects in the nervous system, while mutations of CELSR2 are associated with coronary heart disease. Moreover, CELSR1 and several other PCP signaling molecules, such as dishevelled, prickle, frizzled, have been shown to be upregulated in B lymphocytes of chronic lymphocytic leukemia patients. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. In the case of CELSR/Flamingo/Starry night, their extracellular domains comprise nine cadherin repeats linked to a series of epidermal growth factor (EGF)-like and laminin globular (G)-like domains. The cadherin repeats contain sequence motifs that mediate calcium-dependent cell-cell adhesion by homophilic interactions. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320658  Cd Length: 255  Bit Score: 230.48  E-value: 6.88e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2537 LAVFTHVVVAASVTALVLTAAVLLSLRSLKSNVRGIHANVAAALGVAELLFLLGIHRTHNQLLCTVVAILLHYFFLSTFA 2616
Cdd:cd15992     4 LKTLTWSSVGVTLGFLLLTFLFLLCLRALRSNKTSIRKNGATALFLSELVFILGINQADNPFACTVIAILLHFFYLCTFS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2617 WLLVQGLHLYRMQVEPRNVDRGAMRFYHALGWGVPAVLLGLAVGLDPEGYGNPDFCWISIHEPLIWSFAGPIVLVIVMNG 2696
Cdd:cd15992    84 WLFLEGLHIYRMLSEVRDINYGPMRFYYLIGWGVPAFITGLAVGLDPEGYGNPDFCWLSIYDTLIWSFAGPVAFAVSMNV 163

                         170       180
                  ....*....|....*....|....*
gi 564365651 2697 IMFLLAARTSCSTGQREAKKTSVLV 2721
Cdd:cd15992   164 FLYILSSRASCSAQQQSFEKKKGPV 188
7tmB2_latrophilin-like_invertebrate cd15440
invertebrate latrophilin-like receptors, member of the class B2 family of seven-transmembrane ...
 2536-2708 8.94e-54

invertebrate latrophilin-like receptors, member of the class B2 family of seven-transmembrane G protein-coupled receptors; This subgroup includes latrophilin-like proteins that are found in invertebrates such as insects and worms. Latrophilins (also called lectomedins or latrotoxin receptors) belong to Group I adhesion GPCRs, which also include ETL (EGF-TM7-latrophilin-related protein). These receptors are a member of the adhesion family (subclass B2) that belongs to the class B GPCRs. Three subtypes of vertebrate latrophilins have been identified: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 is a brain-specific calcium-independent receptor of alpha-latrotoxin, a potent presynaptic neurotoxin from the venom of the black widow spider that induces massive neurotransmitter release from sensory and motor neurons as well as endocrine cells, leading to nerve-terminal degeneration. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320556 [Multi-domain]  Cd Length: 259  Bit Score: 189.78  E-value: 8.94e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2536 LLAVFTHVVVAASVTALVLTAAVLLSLRSLKSNVRGIHANVAAALGVAELLFLLGIHRTHNQLLCTVVAILLHYFFLSTF 2615
Cdd:cd15440     3 ALTFITYIGCIISIVCLLLAFITFTCFRNLQCDRNTIHKNLCLCLLIAEIVFLLGIDQTENRTLCGVIAGLLHYFFLAAF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2616 AWLLVQGLHLYRMQVEPRNVDRGAMRFYHALGWGVPAVLLGLAVGLDPEGYGNPDFCWISIHEPLIWSFAGPIVLVIVMN 2695
Cdd:cd15440    83 SWMLLEGFQLYVMLVEVFEPEKSRIKWYYLFGYGLPALIVAVSAGVDPTGYGTEDHCWLSTENGFIWSFVGPVIVVLLAN 162

                         170
                  ....*....|...
gi 564365651 2696 GIMFLLAARTSCS 2708
Cdd:cd15440   163 LVFLGMAIYVMCR 175
7tmB2_GPR133-like_Adhesion_V cd15933
orphan GPR133 and related proteins, group V adhesion GPCRs, member of class B2 family of ...
 2536-2717 5.98e-51

orphan GPR133 and related proteins, group V adhesion GPCRs, member of class B2 family of seven-transmembrane G protein-coupled receptors; group V adhesion GPCRs include orphan receptors GPR133, GPR144, and closely related proteins. The function of GPR144 has not yet been characterized, whereas GPR133 is highly expressed in the pituitary gland and is coupled to the G(s) protein, leading to activation of adenylate cyclase pathway. Moreover, genetic variations in the GPR133 have been reported to be associated with adult height and heart rate. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS.


Pssm-ID: 320599 [Multi-domain]  Cd Length: 252  Bit Score: 181.37  E-value: 5.98e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2536 LLAVFTHVVVAASVTALVLTAAVLLSLRSLKSNVRGIHANVAAALGVAELLFLLGIHRTHNQLLCTVVAILLHYFFLSTF 2615
Cdd:cd15933     3 ALSIISYIGCGISIACLALTLIIFLVLRVLSSDRFQIHKNLCVALLLAQILLLAGEWAEGNKVACKVVAILLHFFFMAAF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2616 AWLLVQGLHLYRMQVEPRNVDRGaMRFYHALGWGVPAVLLGLAVGLDPEGYGNPDFCWISIHEPLIWSFAGPIVLVIVMN 2695
Cdd:cd15933    83 SWMLVEGLHLYLMIVKVFNYKSK-MRYYYFIGWGLPAIIVAISLAILFDDYGSPNVCWLSLDDGLIWAFVGPVIFIITVN 161

                         170       180
                  ....*....|....*....|..
gi 564365651 2696 GIMFLLAARTSCSTGQREAKKT 2717
Cdd:cd15933   162 TVILILVVKITVSLSTNDAKKS 183
7tmB2_Adhesion cd15040
adhesion receptors, subfamily B2 of the class B family of seven-transmembrane G ...
 2535-2725 2.67e-50

adhesion receptors, subfamily B2 of the class B family of seven-transmembrane G protein-coupled receptors; The B2 subfamily of class B GPCRs consists of cell-adhesion receptors with 33 members in humans and vertebrates. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing a variety of structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, linked to a class B seven-transmembrane domain. These include, for example, EGF (epidermal growth factor)-like domains in CD97, Celsr1 (cadherin family member), Celsr2, Celsr3, EMR1 (EGF-module-containing mucin-like hormone receptor-like 1), EMR2, EMR3, and Flamingo; two laminin A G-type repeats and nine cadherin domains in Flamingo and its human orthologs Celsr1, Celsr2 and Celsr3; olfactomedin-like domains in the latrotoxin receptors; and five or four thrombospondin type 1 repeats in BAI1 (brain-specific angiogenesis inhibitor 1), BAI2 and BAI3. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320168 [Multi-domain]  Cd Length: 253  Bit Score: 179.69  E-value: 2.67e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2535 ELLAVFTHVVVAASVTALVLTAAVLLSLRSLKSNVRG-IHANVAAALGVAELLFLLGIHRTHNQLLCTVVAILLHYFFLS 2613
Cdd:cd15040     2 KALSIITYIGCGLSLLGLLLTIITYILFRKLRKRKPTkILLNLCLALLLANLLFLFGINSTDNPVLCTAVAALLHYFLLA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2614 TFAWLLVQGLHLYRMQVEPRNVD-RGAMRFYHALGWGVPAVLLGLAVGLDPEGYGN-PDFCWISIHEPLIWSFAGPIVLV 2691
Cdd:cd15040    82 SFMWMLVEALLLYLRLVKVFGTYpRHFILKYALIGWGLPLIIVIITLAVDPDSYGNsSGYCWLSNGNGLYYAFLGPVLLI 161

                         170       180       190
                  ....*....|....*....|....*....|....
gi 564365651 2692 IVMNGIMFLLAARTSCSTGQREAKKTSVLVLPRL 2725
Cdd:cd15040   162 ILVNLVIFVLVLRKLLRLSAKRNKKKRKKTKAQL 195
GAIN pfam16489
GPCR-Autoproteolysis INducing (GAIN) domain; The GAIN a domain of alpha-helices and ...
 2200-2448 1.88e-45

GPCR-Autoproteolysis INducing (GAIN) domain; The GAIN a domain of alpha-helices and beta-strands that is found in cell-adhesion GPCRs and precedes the GPS motif where the autoproteolysis occurs, family, pfam01825. The full GAIN domain, comprises the GPS and the GAIN, in cell-adhesion GPCRs, and is the functional unit for autoproteolysis. The GPS motif at the end of the GAIN domain is an ancient domain that exists in primitive ancestor organizms, and the full GAIN + GPS is conserved in all cell-adhesion GPCRs and all PKD1-related proteins.


Pssm-ID: 465137  Cd Length: 205  Bit Score: 163.98  E-value: 1.88e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  2200 EAKKLAQRLREVTgQTDHYFSQDVRVTARLLAYLlafeshqqgFGLTATQDA----HFNENLLWAGSALLAPETGDLWAA 2275
Cdd:pfam16489    1 GAKELARELRNAT-RHGPLYGGDVLTAVELLSQL---------FDLLATQDAtlsnAFLENFVQTVSNLLDPENRESWED 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  2276 LGQRAPGGSpgSAGLVRHLEEYAATLARNMDltYLNPVGLVTPNIMLSIDRMEQPSSSQgaHRYPRYHSNlfrgQDAWDP 2355
Cdd:pfam16489   71 LQQTERGTA--ATKLLRTLEEYALLLAQNMK--YLTPFTIVTPNIVLSVDRLDTHNFKG--ARFPRFPMK----GERPKD 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  2356 HTHVLLpsqspqpspsevlptssnaenatasgvvsPPAPLEPESEPGISIVILLVYRALGGLLPAQ--FQAERRGARLPQ 2433
Cdd:pfam16489  141 EDSVKL-----------------------------PPKAFKPPDSNGTVVVVFILYRNLGSLLPPSsrYDPDRRSLRLPR 191

                          250
                   ....*....|....*
gi 564365651  2434 NpVMNSPVVSVAVFR 2448
Cdd:pfam16489  192 R-VVNSPVVSASVHS 205
7tm_classB cd13952
class B family of seven-transmembrane G protein-coupled receptors; The class B of ...
 2535-2718 4.09e-45

class B family of seven-transmembrane G protein-coupled receptors; The class B of seven-transmembrane GPCRs is classified into three major subfamilies: subfamily B1 (secretin-like receptor family), B2 (adhesion family), and B3 (Methuselah-like family). The class B receptors have been identified in all the vertebrates, from fishes to mammals, as well as invertebrates including Caenorhabditis elegans and Drosophila melanogaster, but are not present in plants, fungi or prokaryotes. The B1 subfamily comprises receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the subfamily B1 receptors preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. The subfamily B2 consists of cell-adhesion receptors with 33 members in humans and vertebrates. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing a variety of structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, linked to a class B seven-transmembrane domain. These include, for example, EGF (epidermal growth factor)-like domains in CD97, Celsr1 (cadherin family member), Celsr2, Celsr3, EMR1 (EGF-module-containing mucin-like hormone receptor-like 1), EMR2, EMR3, and Flamingo; two laminin A G-type repeats and nine cadherin domains in Flamingo and its human orthologs Celsr1, Celsr2 and Celsr3; olfactomedin-like domains in the latrotoxin receptors; and five or four thrombospondin type 1 repeats in BAI1 (brain-specific angiogenesis inhibitor 1), BAI2 and BAI3. Almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. Furthermore, the subfamily B3 includes Methuselah (Mth) protein, which was originally identified in Drosophila as a GPCR affecting stress resistance and aging, and its closely related proteins.


Pssm-ID: 410627 [Multi-domain]  Cd Length: 260  Bit Score: 165.08  E-value: 4.09e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2535 ELLAVFTHVVVAASVTALVLTAAVLLSLRSLKsNVRG-IHANVAAALGVAELLFLLGIHRTHNQ--LLCTVVAILLHYFF 2611
Cdd:cd13952     2 LALSIITYIGCSLSLVGLLLTIITYLLFPKLR-NLRGkILINLCLSLLLAQLLFLIGQLLTSSDrpVLCKALAILLHYFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2612 LSTFAWLLVQGLHLYRMQVEPRNVDRGA-MRFYHALGWGVPAVLLGLAVGLDPEGYGNP-----DFCWISIHEPLIWSFA 2685
Cdd:cd13952    81 LASFFWMLVEAFDLYRTFVKVFGSSERRrFLKYSLYGWGLPLLIVIITAIVDFSLYGPSpgyggEYCWLSNGNALLWAFY 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 564365651 2686 GPIVLVIVMNGIMFLLAARTSCSTGQREAKKTS 2718
Cdd:cd13952   161 GPVLLILLVNLVFFILTVRILLRKLRETPKQSE 193
7tmB2_EMR cd15439
epidermal growth factor-like module-containing mucin-like hormone receptors, member of the ...
 2533-2701 1.86e-40

epidermal growth factor-like module-containing mucin-like hormone receptors, member of the class B2 family of seven-transmembrane G protein-coupled receptors; group II adhesion GPCRs, including the epidermal growth factor (EGF)-module-containing, mucin-like hormone receptor (EMR1-4) and the leukocyte cell-surface antigen CD97, are primarily expressed in cells of the immune system. All EGF-TM7 receptors, which belong to the B2 subfamily of adhesion GPCRs, are members of group II, except for ETL (EGF-TM7-latrophilin related protein), which is classified into group I. Members of the EGF-TM7 receptors are characterized by the presence of varying number of N-terminal EGF-like domains, which play critical roles in ligand recognition and cell adhesion, linked by a stalk region to a class B seven-transmembrane domain. In the case of EMR2, alternative splicing results in four isoforms possessing either two (EGF1,2), three (EGF1,2,5), four (EGF1,2,3,5) or five (EGF1,2,3,4,5) EGF-like domains. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. EMR2 shares strong sequence homology with CD97, differing by only six amino acids. CD97 is widely expressed on lymphocytes, monocytes, macrophages, dendritic cells, granulocytes and smooth muscle cells as well as in a variety of human tumors including colorectal, gastric, esophageal pancreatic, and thyroid carcinoma. However, unlike CD97, EMR2 is not found in those of CD97-positive tumor cells and is not expressed on lymphocytes but instead on monocytes, macrophages and granulocytes. CD97 has three known ligands: CD55, decay-accelerating factor for regulation of complement system; chondroitin sulfate, a glycosaminoglycan found in the extracellular matrix; and the integrin alpha5beta1, which play a role in angiogenesis. Although EMR2 does not effectively interact with CD55, the fourth EGF-like domain of this receptor binds to chondroitin sulfate to mediate cell attachment.


Pssm-ID: 320555 [Multi-domain]  Cd Length: 263  Bit Score: 151.73  E-value: 1.86e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2533 DLELLaVFTHVVVAASVTALVLTAAVLLSLRSLKSNVRGIHANVAAALGVAELLFLLGIHRTHNQLLCTVVAILLHYFFL 2612
Cdd:cd15439     1 DLALT-VITYVGLIISLLCLFLAILTFLLCRSIRNTSTSLHLQLSLCLFLADLLFLVGIDRTDNKVLCSIIAGFLHYLFL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2613 STFAWLLVQGLHLYRMQvepRNVD--------RGAMRFYHALGWGVPAVLLGLAVGLDPEGYGNPDFCWISIHEPLIWSF 2684
Cdd:cd15439    80 ACFAWMFLEAVHLFLTV---RNLKvvnyfsshRFKKRFMYPVGYGLPAVIVAISAAVNPQGYGTPKHCWLSMEKGFIWSF 156

                         170
                  ....*....|....*..
gi 564365651 2685 AGPIVLVIVMNGIMFLL 2701
Cdd:cd15439   157 LGPVCVIIVINLVLFCL 173
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 646-743 4.88e-38

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 138.60  E-value: 4.88e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  646 PFQVSVLENAPLGHSVIHIQAVDADHGENSRLEYSLTGVASDTPFVINSATGWVSVSGPLDRESVEHYFFGVEARDHGSP 725
Cdd:cd11304     1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGGGP 80

                          90
                  ....*....|....*...
gi 564365651  726 PLSASASVTVTVLDVNDN 743
Cdd:cd11304    81 PLSSTATVTITVLDVNDN 98
7tmB2_CD97 cd15438
CD97 antigen, member of the class B2 family of seven-transmembrane G protein-coupled receptors; ...
 2537-2701 5.79e-38

CD97 antigen, member of the class B2 family of seven-transmembrane G protein-coupled receptors; group II adhesion GPCRs, including the leukocyte cell-surface antigen CD97 and the epidermal growth factor (EGF)-module-containing, mucin-like hormone receptor (EMR1-4), are primarily expressed in cells of the immune system. All EGF-TM7 receptors, which belong to the B2 subfamily B2 of adhesion GPCRs, are members of group II, except for ETL (EGF-TM7-latrophilin related protein), which is classified into group I. Members of the EGF-TM7 receptors are characterized by the presence of varying numbers of N-terminal EGF-like domains, which play critical roles in ligand recognition and cell adhesion, linked by a stalk region to a class B seven-transmembrane domain. In the case of CD97, alternative splicing results in three isoforms possessing either three (EGF1,2,5), four (EGF1,2,3,5) or five (EGF1,2,3,4,5) EGF-like domains. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. For example, CD97, which is involved in angiogenesis and the migration and invasion of tumor cells, has been shown to promote cell aggregation in a GPS proteolysis-dependent manner. CD97 is widely expressed on lymphocytes, monocytes, macrophages, dendritic cells, granulocytes and smooth muscle cells as well as in a variety of human tumors including colorectal, gastric, esophageal pancreatic, and thyroid carcinoma. EMR2 shares strong sequence homology with CD97, differing by only six amino acids. However, unlike CD97, EMR2 is not found in those of CD97-positive tumor cells and is not expressed on lymphocytes but instead on monocytes, macrophages and granulocytes. CD97 has three known ligands: CD55, decay-accelerating factor for regulation of complement system; chondroitin sulfate, a glycosaminoglycan found in the extracellular matrix; and the integrin alpha5beta1, which play a role in angiogenesis. Although EMR2 does not effectively interact with CD55, the fourth EGF-like domain of this receptor binds to chondroitin sulfate to mediate cell attachment.


Pssm-ID: 320554 [Multi-domain]  Cd Length: 261  Bit Score: 144.52  E-value: 5.79e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2537 LAVFTHVVVAASVTALVLTAAVLLSLRSLKSNVRGIHANVAAALGVAELLFLLGIHRTHNQLLCTVVAILLHYFFLSTFA 2616
Cdd:cd15438     4 LTLITKVGLSVSLFCLFLCILTFLFCRSIRGTRNTIHLHLCLSLFLAHLIFLLGINNTNNQVACAVVAGLLHYFFLAAFC 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2617 WLLVQGLHLYRMQVEPRNVDRGAMRFYHALGWGVPAVLLGLAVGLDPEGYGNPDFCWISIHEPLIWSFAGPIVLVIVMNG 2696
Cdd:cd15438    84 WMSLEGVELYLMVVQVFNTQSLKKRYLLLIGYGVPLVIVAISAAVNSKGYGTQRHCWLSLERGFLWSFLGPVCLIILVNA 163


                  ....*
gi 564365651 2697 IMFLL 2701
Cdd:cd15438   164 IIFVI 168
7tmB2_Latrophilin_Adhesion_I cd15252
Latrophilins and similar receptors, group I adhesion GPCRs, member of class B2 family of ...
 2536-2702 8.01e-38

Latrophilins and similar receptors, group I adhesion GPCRs, member of class B2 family of seven-transmembrane G protein-coupled receptors; Group I adhesion GPCRs consist of latrophilins (also called lectomedins or latrotoxin receptors) and ETL (EGF-TM7-latrophilin-related protein. These receptors are a member of the adhesion family (subclass B2) that belongs to the class B GPCRs. Three subtypes of latrophilins have been identified: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 is a brain-specific calcium-independent receptor of alpha-latrotoxin, a potent presynaptic neurotoxin from the venom of the black widow spider that induces massive neurotransmitter release from sensory and motor neurons as well as endocrine cells, leading to nerve-terminal degeneration. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320380 [Multi-domain]  Cd Length: 257  Bit Score: 143.80  E-value: 8.01e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2536 LLAVFTHVVVAASVTALVLTAAVLLSLRSLKSNVRGIHANVAAALGVAELLFLLGIHRTHNQLLCTVVAILLHYFFLSTF 2615
Cdd:cd15252     3 ILTRITQVGIIISLVCLAICIFTFWFFRGLQSDRTTIHKNLCISLFLAELVFLIGINTTTNKIFCSVIAGLLHYFFLAAF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2616 AWLLVQGLHLYRMQVEPRNVDRGAMRFYHALGWGVPAVLLGLAVGLDPEGYGNPDFCWISIHEPLIWSFAGPIVLVIVMN 2695
Cdd:cd15252    83 AWMFIEGIQLYLMLVEVFENEGSRHKNFYIFGYGSPAVIVGVSAALGYRYYGTTKVCWLSTENYFIWSFIGPATLIILLN 162


                  ....*..
gi 564365651 2696 GIMFLLA 2702
Cdd:cd15252   163 LIFLGVA 169
7tmB2_Latrophilin-1 cd16007
Latrophilin-1, member of the class B2 family of seven-transmembrane G protein-coupled ...
 2536-2701 1.05e-36

Latrophilin-1, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Latrophilins (also called lectomedins or latrotoxin receptors) belong to Group I adhesion GPCRs, which also include ETL (EGF-TM7-latrophilin-related protein). These receptors are a member of the adhesion family (subclass B2) that belongs to the class B GPCRs. Three subtypes of latrophilins have been identified: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 is a brain-specific calcium-independent receptor of alpha-latrotoxin, a potent presynaptic neurotoxin from the venom of the black widow spider that induces massive neurotransmitter release from sensory and motor neurons as well as endocrine cells, leading to nerve-terminal degeneration. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320673 [Multi-domain]  Cd Length: 258  Bit Score: 140.83  E-value: 1.05e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2536 LLAVFTHVVVAASVTALVLTAAVLLSLRSLKSNVRGIHANVAAALGVAELLFLLGIHRTHNQLLCTVVAILLHYFFLSTF 2615
Cdd:cd16007     3 LLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLIGIDKTQYQIACPIFAGLLHFFFLAAF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2616 AWLLVQGLHLYRMQVEPRNVDRGAMRFYHALGWGVPAVLLGLAVGLDPEGYGNPDFCWISIHEPLIWSFAGPIVLVIVMN 2695
Cdd:cd16007    83 SWLCLEGVQLYLMLVEVFESEYSRKKYYYLCGYCFPALVVGISAAIDYRSYGTEKACWLRVDNYFIWSFIGPVSFVIVVN 162


                  ....*.
gi 564365651 2696 gIMFLL 2701
Cdd:cd16007   163 -LVFLM 167
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 956-1054 1.62e-35

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 131.28  E-value: 1.62e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  956 HYTGLVSEDAPPFTSVLQISATDRDAHANGRVQYTFQNGeDGDGDFTIEPTSGIVRTVRRLDREAVPVYELTAYAVDRGV 1035
Cdd:cd11304     1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSG-NEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGGG 79

                          90
                  ....*....|....*....
gi 564365651 1036 PPLRTPVSIQVTVQDVNDN 1054
Cdd:cd11304    80 PPLSSTATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 541-638 1.75e-34

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 128.20  E-value: 1.75e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  541 YVAQVREDVRPHTVVLRVTATDKDKDANGLVHYNIISGNSRGHFAIDSLTGEIQVMAPLDFEAEREYALRIRAQDAGRPP 620
Cdd:cd11304     2 YEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGGGPP 81

                          90
                  ....*....|....*...
gi 564365651  621 LSnNTGLASIQVVDINDH 638
Cdd:cd11304    82 LS-STATVTITVLDVNDN 98
7tmB2_Latrophilin cd15436
Latrophilins, member of the class B2 family of seven-transmembrane G protein-coupled receptors; ...
 2536-2702 3.92e-34

Latrophilins, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Latrophilins (also called lectomedins or latrotoxin receptors) belong to Group I adhesion GPCRs, which also include ETL (EGF-TM7-latrophilin-related protein). These receptors are a member of the adhesion family (subclass B2) that belongs to the class B GPCRs. Three subtypes of latrophilins have been identified: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 is a brain-specific calcium-independent receptor of alpha-latrotoxin, a potent presynaptic neurotoxin from the venom of the black widow spider that induces massive neurotransmitter release from sensory and motor neurons as well as endocrine cells, leading to nerve-terminal degeneration. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320552 [Multi-domain]  Cd Length: 258  Bit Score: 133.38  E-value: 3.92e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2536 LLAVFTHVVVAASVTALVLTAAVLLSLRSLKSNVRGIHANVAAALGVAELLFLLGIHRTHNQLLCTVVAILLHYFFLSTF 2615
Cdd:cd15436     3 LLFVITWVGIVISLVCLLICIFTFCFFRGLQTDRNTIHKNLCINLFIAELLFLIGINRTQYTIACPIFAGLLHFFFLAAF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2616 AWLLVQGLHLYRMQVEPRNVDRGAMRFYHALGWGVPAVLLGLAVGLDPEGYGNPDFCWISIHEPLIWSFAGPIVLVIVMN 2695
Cdd:cd15436    83 CWLCLEGVQLYLLLVEVFESEYSRRKYFYLCGYSFPALVVAVSAAIDYRSYGTEKACWLRVDNYFIWSFIGPVTFVITLN 162


                  ....*..
gi 564365651 2696 GIMFLLA 2702
Cdd:cd15436   163 LVFLVIT 169
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 1508-1691 1.42e-33

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 127.92  E-value: 1.42e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 1508 ARSFPPSSFVMFRGLR-QRFHLTLSLSFATVQPSGLLFYNGRLNeKHDFLALELVAGQVRLTYSTGESSTVVSPTVPggL 1586
Cdd:cd00110     1 GVSFSGSSYVRLPTLPaPRTRLSISFSFRTTSPNGLLLYAGSQN-GGDFLALELEDGRLVLRYDLGSGSLVLSSKTP--L 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 1587 SDGQWHTVHLRYYNkprtdalggaqgpskdKVAVLSVDDCNVavaLRFGAEIGNYscaaagvqtsskkSLDLTGPLLLGG 1666
Cdd:cd00110    78 NDGQWHSVSVERNG----------------RSVTLSVDGERV---VESGSPGGSA-------------LLNLDGPLYLGG 125

                         170       180
                  ....*....|....*....|....*.
gi 564365651 1667 VPNLPENFPV-SRKDFIGCMRDLHID 1691
Cdd:cd00110   126 LPEDLKSPGLpVSPGFVGCIRDLKVN 151
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 321-420 1.65e-33

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 125.50  E-value: 1.65e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  321 YQTLVPENEAAGTAVLRVVAQDPDPGEAGRLVYSLaalMNSRSLELFSIDPQSGLIRTAAALDRESMERHYLRVTAQDHG 400
Cdd:cd11304     2 YEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSI---VSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGG 78

                          90       100
                  ....*....|....*....|
gi 564365651  401 SPRLSATTMVAVTVADRNDH 420
Cdd:cd11304    79 GPPLSSTATVTITVLDVNDN 98
7tmB2_GPR133 cd15256
orphan adhesion receptor GPR133, member of the class B2 family of seven-transmembrane G ...
 2537-2698 7.01e-33

orphan adhesion receptor GPR133, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR133 is an orphan receptor that belongs to the group V adhesion-GPCRs together with GPR144. The function of GPR144 has not yet been characterized, whereas GPR133 is highly expressed in the pituitary gland and is coupled to the Gs protein, leading to activation of adenylyl cyclase pathway. Moreover, genetic variations in the GPR133 have been reported to be associated with adult height and heart rate. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS.


Pssm-ID: 320384 [Multi-domain]  Cd Length: 260  Bit Score: 129.66  E-value: 7.01e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2537 LAVFTHVVVAASVTALVLTA---AVLLSLRSLKSNVRGIHANVAAALGVAELLFLLGIHRTHNQLLCTVVAILLHYFFLS 2613
Cdd:cd15256     4 LSSITYVGCSLSIFCLAITLvtfAVLSSVSTIRNQRYHIHANLSFAVLVAQILLLISFRFEPGTLPCKIMAILLHFFFLS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2614 TFAWLLVQGLHLYRMQVEPRNVDRGAMRFYHALGWGVPAVLLGLAVGLDPEGYGNPDFCWISIHEPLIWSFAGPIVLVIV 2693
Cdd:cd15256    84 AFAWMLVEGLHLYSMVIKVFGSEESKHFYYYGIGWGSPLLICIISLTSALDSYGESDNCWLSLENGAIWAFVAPALFVIV 163


                  ....*.
gi 564365651 2694 MN-GIM 2698
Cdd:cd15256   164 VNiGIL 169
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 428-532 2.02e-32

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 122.42  E-value: 2.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  428 QYRETLRENVEEGYPILQLRATDGDAPPNANLRYRFVGSPAARTaaaaaFEIDPRSGLISTSGRVDREHMESYELVVEAS 507
Cdd:cd11304     1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDGL-----FSIDPSTGEITTAKPLDREEQSSYTLTVTAT 75

                          90       100
                  ....*....|....*....|....*
gi 564365651  508 DQGQEpgPRSATVRVHITVLDENDN 532
Cdd:cd11304    76 DGGGP--PLSSTATVTITVLDVNDN 98
7tmB2_EMR_Adhesion_II cd15931
EGF-like module receptors, group II adhesion GPCRs, member of class B2 family of ...
 2537-2699 4.32e-32

EGF-like module receptors, group II adhesion GPCRs, member of class B2 family of seven-transmembrane G protein-coupled receptors; group II adhesion GPCRs, including the leukocyte cell-surface antigen CD97 and the epidermal growth factor (EGF)-module-containing, mucin-like hormone receptor (EMR1-4), are primarily expressed in cells of the immune system. All EGF-TM7 receptors, which belong to the B2 subfamily B2 of adhesion GPCRs, are members of group II, except for ETL (EGF-TM7-latrophilin related protein), which is classified into group I. Members of the EGF-TM7 receptors are characterized by the presence of varying numbers of N-terminal EGF-like domains, which play critical roles in ligand recognition and cell adhesion, linked by a stalk region to a class B seven-transmembrane domain. In the case of CD97, alternative splicing results in three isoforms possessing either three (EGF1,2,5), four (EGF1,2,3,5) or five (EGF1,2,3,4,5) EGF-like domains. On the other hand, EMR2 generates four isoforms possessing either two (EGF1,2), three (EGF1,2,5), four (EGF1,2,3,5) or five (EGF1,2,3,4,5) EGF-like domains. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. For example, CD97, which is involved in angiogenesis and the migration and invasion of tumor cells, has been shown to promote cell aggregation in a GPS proteolysis-dependent manner. CD97 is widely expressed on lymphocytes, monocytes, macrophages, dendritic cells, granulocytes and smooth muscle cells as well as in a variety of human tumors including colorectal, gastric, esophageal pancreatic, and thyroid carcinoma. EMR2 shares strong sequence homology with CD97, differing by only six amino acids. However, unlike CD97, EMR2 is not found in those of CD97-positive tumor cells and is not expressed on lymphocytes but instead on monocytes, macrophages and granulocytes. CD97 has three known ligands: CD55, decay-accelerating factor for regulation of complement system; chondroitin sulfate, a glycosaminoglycan found in the extracellular matrix; and the integrin alpha5beta1, which play a role in angiogenesis. Although EMR2 does not effectively interact with CD55, the fourth EGF-like domain of this receptor binds to chondroitin sulfate to mediate cell attachment.


Pssm-ID: 320597 [Multi-domain]  Cd Length: 262  Bit Score: 127.63  E-value: 4.32e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2537 LAVFTHVVVAASVTALVLTAAVLLSLRSLKSNVRGIHANVAAALGVAELLFLLGIHRTHNQLLCTVVAILLHYFFLSTFA 2616
Cdd:cd15931     4 LEWINRVGVIVSLFCLGLAIFTFLLCRWIPKINTTAHLHLCLCLSMSHTLFLAGIEYVENELACTVMAGLLHYLFLASFV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2617 WLLVQGLHLYRM-----QVEPRNVDRGAMRFYHALGWGVPAVLLGLAVGLDPEGYGNPDFCWISIHEPLIWSFAGPIVLV 2691
Cdd:cd15931    84 WMLLEALQLHLLvrrltKVQVIQRDGLPRPLLCLIGYGVPFLIVGVSALVYSDGYGEAKMCWLSQERGFNWSFLGPVIAI 163


                  ....*...
gi 564365651 2692 IVMNGIMF 2699
Cdd:cd15931   164 IGINWILF 171
7tmB2_Latrophilin-2 cd16006
Latrophilin-2, member of the class B2 family of seven-transmembrane G protein-coupled ...
 2536-2701 4.68e-32

Latrophilin-2, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Latrophilins (also called lectomedins or latrotoxin receptors) belong to Group I adhesion GPCRs, which also include ETL (EGF-TM7-latrophilin-related protein). These receptors are a member of the adhesion family (subclass B2) that belongs to the class B GPCRs. Three subtypes of latrophilins have been identified: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 is a brain-specific calcium-independent receptor of alpha-latrotoxin, a potent presynaptic neurotoxin from the venom of the black widow spider that induces massive neurotransmitter release from sensory and motor neurons as well as endocrine cells, leading to nerve-terminal degeneration. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320672 [Multi-domain]  Cd Length: 258  Bit Score: 127.34  E-value: 4.68e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2536 LLAVFTHVVVAASVTALVLTAAVLLSLRSLKSNVRGIHANVAAALGVAELLFLLGIHRTHNQLLCTVVAILLHYFFLSTF 2615
Cdd:cd16006     3 LLTVITWVGIVISLVCLAICIFTFCFFRGLQSDRNTIHKNLCINLFIAEFIFLIGIDKTEYKIACPIFAGLLHFFFLAAF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2616 AWLLVQGLHLYRMQVEPRNVDRGAMRFYHALGWGVPAVLLGLAVGLDPEGYGNPDFCWISIHEPLIWSFAGPIVLVIVMN 2695
Cdd:cd16006    83 AWMCLEGVQLYLMLVEVFESEYSRKKYYYVAGYLFPATVVGVSAAIDYKSYGTEKACWLRVDNYFIWSFIGPVTFIILLN 162


                  ....*.
gi 564365651 2696 GIMFLL 2701
Cdd:cd16006   163 LIFLVI 168
7tmB2_Latrophilin-3 cd16005
Latrophilin-3, member of the class B2 family of seven-transmembrane G protein-coupled ...
 2536-2702 4.91e-32

Latrophilin-3, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Latrophilins (also called lectomedins or latrotoxin receptors) belong to Group I adhesion GPCRs, which also include ETL (EGF-TM7-latrophilin-related protein). These receptors are a member of the adhesion family (subclass B2) that belongs to the class B GPCRs. Three subtypes of latrophilins have been identified: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 is a brain-specific calcium-independent receptor of alpha-latrotoxin, a potent presynaptic neurotoxin from the venom of the black widow spider that induces massive neurotransmitter release from sensory and motor neurons as well as endocrine cells, leading to nerve-terminal degeneration. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320671 [Multi-domain]  Cd Length: 258  Bit Score: 127.37  E-value: 4.91e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2536 LLAVFTHVVVAASVTALVLTAAVLLSLRSLKSNVRGIHANVAAALGVAELLFLLGIHRTHNQLLCTVVAILLHYFFLSTF 2615
Cdd:cd16005     3 LLDVITWVGILLSLVCLLICIFTFCFFRGLQSDRNTIHKNLCISLFVAELLFLIGINRTDQPIACAVFAALLHFFFLAAF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2616 AWLLVQGLHLYRMQVEPRNVDRGAMRFYHALGWGVPAVLLGLAVGLDPEGYGNPDFCWISIHEPLIWSFAGPIVLVIVMN 2695
Cdd:cd16005    83 TWMFLEGVQLYIMLVEVFESEHSRRKYFYLVGYGMPALIVAVSAAVDYRSYGTDKVCWLRLDTYFIWSFIGPATLIIMLN 162


                  ....*..
gi 564365651 2696 GIMFLLA 2702
Cdd:cd16005   163 VIFLGIA 169
7tmB2_GPR144 cd15255
orphan adhesion receptor GPR114, member of the class B2 family of seven-transmembrane G ...
 2536-2715 4.04e-31

orphan adhesion receptor GPR114, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR144 is an orphan receptor that belongs to the group V adhesion-GPCRs together with GPR133. The function of GPR144 has not yet been characterized, whereas GPR133 is highly expressed in the pituitary gland and is coupled to the Gs protein, leading to activation of adenylyl cyclase pathway. Moreover, genetic variations in the GPR133 have been reported to be associated with adult height and heart rate. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS.


Pssm-ID: 320383 [Multi-domain]  Cd Length: 263  Bit Score: 124.58  E-value: 4.04e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2536 LLAVFTHVVVAASVTALVLTAAVLLSLRSLKSNVRGIHANVAAALGVAELLFLLGIHRTHNQLLCTVVAILLHYFFLSTF 2615
Cdd:cd15255     3 TLRTLSFIGCGVSLCALIVTFILFLAVGVPKSERTTVHKNLIFALAAAEFLLMFSEWAKGNQVACWAVTALLHLFFLAAF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2616 AWLLVQGLHLYRMQVEPRNVDRGAMRFYHALGWGVPAVLLGLAVGLDPEGYGNPDFCWISIHEPLIWSFAGPIVLVIVMN 2695
Cdd:cd15255    83 SWMLVEGLLLWSKVVAVNMSEDRRMKFYYVTGWGLPVVIVAVTLATSFNKYVADQHCWLNVQTDIIWAFVGPVLFVLTVN 162

                         170       180
                  ....*....|....*....|
gi 564365651 2696 GIMFLLAARTSCSTGQREAK 2715
Cdd:cd15255   163 TFVLFRVVMVTVSSARRRAK 182
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 853-948 6.65e-31

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 118.18  E-value: 6.65e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  853 HYSVSMNEDRPVGSTVVVISASDDDVGENARITYLL--EDNLPQFRIDADSGAITLQAPLDYEDQVTYTLAITARDNGIP 930
Cdd:cd11304     1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIvsGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGGGP 80

                          90
                  ....*....|....*...
gi 564365651  931 QKADTTYVEVMVNDVNDN 948
Cdd:cd11304    81 PLSSTATVTITVLDVNDN 98
7tmB2_ETL cd15437
Epidermal Growth Factor, latrophilin and seven transmembrane domain-containing protein 1; ...
 2536-2699 2.44e-30

Epidermal Growth Factor, latrophilin and seven transmembrane domain-containing protein 1; member of the class B2 family of seven-transmembrane G protein-coupled receptors; ETL (EGF-TM7-latrophilin-related protein) belongs to Group I adhesion GPCRs, which also include latrophilins (also called lectomedins or latrotoxin receptors). All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. ETL, for instance, contains EGF-like repeats, which also present in other EGF-TM7 adhesion GPCRs, such as Cadherin EGF LAG seven-pass G-type receptors (CELSR1-3), EGF-like module receptors (EMR1-3), CD97, and Flamingo. ETL is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320553 [Multi-domain]  Cd Length: 258  Bit Score: 122.29  E-value: 2.44e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2536 LLAVFTHVVVAASVTALVLTAAVLLSLRSLKSNVRGIHANVAAALGVAELLFLLGIHRTHNQLLCTVVAILLHYFFLSTF 2615
Cdd:cd15437     3 VLTRITQLGIIISLICLSMCIFTFWFFSEIQSTRTTIHKNLCCSLFLAELIFLIGINMNANKLFCSIIAGLLHYFFLAAF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2616 AWLLVQGLHLYRMQVEPRnVDRGAM-RFYHALGWGVPAVLLGLAVGLDPEGYGNPDFCWISIHEPLIWSFAGPIVLVIVM 2694
Cdd:cd15437    83 AWMCIEGIHLYLIVVGVI-YNKGFLhKNFYIFGYGSPAVVVGISAALGYKYYGTTKVCWLSTENNFIWSFIGPACLIILV 161


                  ....*
gi 564365651 2695 NGIMF 2699
Cdd:cd15437   162 NLLAF 166
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 1062-1156 4.13e-30

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 115.87  E-value: 4.13e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 1062 EFEVRVKENSIVGSVVAQITAVDPDDGPNAHIMYQIVEGNIPELFQMDIFSGELTALIDLDYEARQEYVIVVQAT---SA 1138
Cdd:cd11304     1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATdggGP 80

                          90
                  ....*....|....*...
gi 564365651 1139 PLVSRATVHVRLVDQNDN 1156
Cdd:cd11304    81 PLSSTATVTITVLDVNDN 98
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 665-745 4.83e-30

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 115.14  E-value: 4.83e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651    665 QAVDADHGENSRLEYSLTGVASDTPFVINSATGWVSVSGPLDRESVEHYFFGVEARDHGSPPLSASASVTVTVLDVNDNR 744
Cdd:smart00112    1 SATDADSGENGKVTYSILSGNDDGLFSIDPETGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVLDVNDNA 80


                    .
gi 564365651    745 P 745
Cdd:smart00112   81 P 81
7tmB3_Methuselah-like cd15039
Methuselah-like subfamily B3, member of the class B family of seven-transmembrane G ...
 2535-2716 1.42e-29

Methuselah-like subfamily B3, member of the class B family of seven-transmembrane G protein-coupled receptors; The subfamily B3 of class B GPCRs consists of Methuselah (Mth) and its closely related proteins found in bilateria. Mth was originally identified in Drosophila as a GPCR affecting stress resistance and aging. In addition to the seven transmembrane helices, Mth contains an N-terminal extracellular domain involved in ligand binding, and a third intracellular loop (IC3) required for the specificity of G-protein coupling. Drosophila Mth mutants showed an increase in average lifespan by 35% and greater resistance to a variety of stress factors, including starvation, high temperature, and paraquat-induced oxidative toxicity. Moreover, mutations in two endogenous peptide ligands of Methuselah, Stunted A and B, showed an increased in lifespan and resistance to oxidative stress induced by dietary paraquat. These results strongly suggest that the Stunted-Methuselah system plays important roles in stress response and aging.


Pssm-ID: 410632 [Multi-domain]  Cd Length: 270  Bit Score: 120.41  E-value: 1.42e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2535 ELLAVFTHVVVAASVTALVLTAAVLLSLRSLksnvRGIH----ANVAAALGVAELLFLLGIHRTHN-QLLCTVVAILLHY 2609
Cdd:cd15039     2 SILGILTLIGLIISLVFLLLTLAVYALLPEL----RNLHgkclMCLVLSLFVAYLLLLIGQLLSSGdSTLCVALGILLHF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2610 FFLSTFAWLLVQGLHLYRM-----QVEPRNVDRGAMRFYHALGWGVPAVLLGLAVGLD---PEGYGNPDF----CWISIH 2677
Cdd:cd15039    78 FFLAAFFWLNVMSFDIWRTfrgkrSSSSRSKERKRFLRYSLYAWGVPLLLVAVTIIVDfspNTDSLRPGYgegsCWISNP 157

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 564365651 2678 EPLIWSFAGPIVLVIVMNGIMFLLAARTSCSTgQREAKK 2716
Cdd:cd15039   158 WALLLYFYGPVALLLLFNIILFILTAIRIRKV-KKETAK 195
LamG smart00282
Laminin G domain;
1529-1693 7.67e-29

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 113.59  E-value: 7.67e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651   1529 TLSLSFATVQPSGLLFYNGRLNeKHDFLALELVAGQVRLTYSTGESSTVVSPTvPGGLSDGQWHTVHLRYYNkprtdalg 1608
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAGSKG-GGDYLALELRDGRLVLRYDLGSGPARLTSD-PTPLNDGQWHRVAVERNG-------- 70

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651   1609 gaqgpskdKVAVLSVDDCNVAVALRFGaeignyscaaagvqtsSKKSLDLTGPLLLGGVPNLPENFP-VSRKDFIGCMRD 1687
Cdd:smart00282   71 --------RSVTLSVDGGNRVSGESPG----------------GLTILNLDGPLYLGGLPEDLKLPPlPVTPGFRGCIRN 126


                    ....*.
gi 564365651   1688 LHIDGR 1693
Cdd:smart00282  127 LKVNGK 132
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 975-1056 3.28e-28

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 109.75  E-value: 3.28e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651    975 SATDRDAHANGRVQYTFqNGEDGDGDFTIEPTSGIVRTVRRLDREAVPVYELTAYAVDRGVPPLRTPVSIQVTVQDVNDN 1054
Cdd:smart00112    1 SATDADSGENGKVTYSI-LSGNDDGLFSIDPETGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVLDVNDN 79


                    ..
gi 564365651   1055 AP 1056
Cdd:smart00112   80 AP 81
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
 1534-1693 4.12e-28

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 460494 [Multi-domain]  Cd Length: 126  Bit Score: 111.36  E-value: 4.12e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  1534 FATVQPSGLLFYNGrlNEKHDFLALELVAGQVRLTYSTGESSTVVSPTvPGGLSDGQWHTVHLRYynkprtdalggaqgp 1613
Cdd:pfam02210    1 FRTRQPNGLLLYAG--GGGSDFLALELVNGRLVLRYDLGSGPESLLSS-GKNLNDGQWHSVRVER--------------- 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  1614 sKDKVAVLSVDDCNVAVALRFGAEIGnyscaaagvqtsskksLDLTGPLLLGGVPN-LPENFPVSRKDFIGCMRDLHIDG 1692
Cdd:pfam02210   63 -NGNTLTLSVDGQTVVSSLPPGESLL----------------LNLNGPLYLGGLPPlLLLPALPVRAGFVGCIRDVRVNG 125


                   .
gi 564365651  1693 R 1693
Cdd:pfam02210  126 E 126
Cadherin pfam00028
Cadherin domain;
541-632 7.77e-28

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 109.31  E-value: 7.77e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651   541 YVAQVREDVRPHTVVLRVTATDKDKDANGLVHYNIISGNSRGHFAIDSLTGEIQVMAPLDFEAEREYALRIRAQDAGRPP 620
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPNGRIFYSILGGGPGGNFRIDPDTGDISTTKPLDRESIGEYELTVEATDSGGPP 80

                           90
                   ....*....|..
gi 564365651   621 LSnNTGLASIQV 632
Cdd:pfam00028   81 LS-STATVTITV 91
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 447-534 5.46e-26

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 103.58  E-value: 5.46e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651    447 RATDGDAPPNANLRYRFVGSPAARTaaaaaFEIDPRSGLISTSGRVDREHMESYELVVEASDQGQEpgPRSATVRVHITV 526
Cdd:smart00112    1 SATDADSGENGKVTYSILSGNDDGL-----FSIDPETGEITTTKPLDREEQPEYTLTVEATDGGGP--PLSSTATVTITV 73


                    ....*...
gi 564365651    527 LDENDNAP 534
Cdd:smart00112   74 LDVNDNAP 81
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 559-640 8.97e-26

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 102.81  E-value: 8.97e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651    559 TATDKDKDANGLVHYNIISGNSRGHFAIDSLTGEIQVMAPLDFEAEREYALRIRAQDAGRPPLSnNTGLASIQVVDINDH 638
Cdd:smart00112    1 SATDADSGENGKVTYSILSGNDDGLFSIDPETGEITTTKPLDREEQPEYTLTVEATDGGGPPLS-STATVTITVLDVNDN 79


                    ..
gi 564365651    639 SP 640
Cdd:smart00112   80 AP 81
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 872-950 1.05e-25

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 102.81  E-value: 1.05e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651    872 SASDDDVGENARITYLLEDNLPQ--FRIDADSGAITLQAPLDYEDQVTYTLAITARDNGIPQKADTTYVEVMVNDVNDNA 949
Cdd:smart00112    1 SATDADSGENGKVTYSILSGNDDglFSIDPETGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVLDVNDNA 80


                    .
gi 564365651    950 P 950
Cdd:smart00112   81 P 81
Cadherin pfam00028
Cadherin domain;
647-738 3.76e-25

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 101.61  E-value: 3.76e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651   647 FQVSVLENAPLGHSVIHIQAVDADHGENSRLEYSLTGVASDTPFVINSATGWVSVSGPLDRESVEHYFFGVEARDHGSPP 726
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPNGRIFYSILGGGPGGNFRIDPDTGDISTTKPLDRESIGEYELTVEATDSGGPP 80

                           90
                   ....*....|..
gi 564365651   727 LSASASVTVTVL 738
Cdd:pfam00028   81 LSSTATVTITVL 92
Cadherin pfam00028
Cadherin domain;
957-1049 4.61e-25

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 101.22  E-value: 4.61e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651   957 YTGLVSEDAPPFTSVLQISATDRDAHANGRVQYTFQNGEDGdGDFTIEPTSGIVRTVRRLDREAVPVYELTAYAVDRGVP 1036
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPNGRIFYSILGGGPG-GNFRIDPDTGDISTTKPLDRESIGEYELTVEATDSGGP 79

                           90
                   ....*....|...
gi 564365651  1037 PLRTPVSIQVTVQ 1049
Cdd:pfam00028   80 PLSSTATVTITVL 92
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 339-422 2.03e-24

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 98.96  E-value: 2.03e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651    339 VAQDPDPGEAGRLVYSLAalmNSRSLELFSIDPQSGLIRTAAALDRESMERHYLRVTAQDHGSPRLSATTMVAVTVADRN 418
Cdd:smart00112    1 SATDADSGENGKVTYSIL---SGNDDGLFSIDPETGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVLDVN 77


                    ....
gi 564365651    419 DHAP 422
Cdd:smart00112   78 DNAP 81
7tmB2_BAI_Adhesion_VII cd15251
brain-specific angiogenesis inhibitors, group VII adhesion GPCRs, member of the class B2 ...
 2546-2725 2.59e-24

brain-specific angiogenesis inhibitors, group VII adhesion GPCRs, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Brain-specific angiogenesis inhibitors (BAI1-3) constitute the group VII of cell-adhesion receptors that have been implicated in vascularization of glioblastomas. They belong to the B2 subfamily of class B GPCRs, are predominantly expressed in the brain, and are only present in vertebrates. Three BAIs, like all adhesion receptors, are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. For example, BAI1 N-terminus contain an integrin-binding RGD (Arg-Gly-Asp) motif in addition to five thrombospondin type 1 repeats (TSRs), which are known to regulate the anti-angiogenic activity of thrombospondin-1, whereas BAI2 and BAI3 have four TSRs, but do not possess RGD motifs. The TSRs are functionally involved in cell attachment, activation of latent TGF-beta, inhibition of angiogenesis and endothelial cell migration. The TSRs of BAI1 mediate direct binding to phosphatidylserine, which enables both recognition and internalization of apoptotic cells by phagocytes. Thus, BAI1 functions as a phosphatidylserine receptor that forms a trimeric complex with ELMO and Dock180, leading to activation of Rac-GTPase which promotes the binding and phagocytosis of apoptotic cells. BAI3 can also interact with the ELMO-Dock180 complex to activate the Rac pathway and can also bind to secreted C1ql proteins of the C1Q complement family via its N-terminal TSRs. BAI3 and its ligands C1QL1 are highly expressed during synaptogenesis and are involved in synapse specificity. Moreover, BAI2 acts as a transcription repressor to regulate vascular endothelial growth factor (VEGF) expression through interaction with GA-binding protein gamma (GABP). The N-terminal extracellular domains of all three BAIs also contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain, which undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif to generate N- and C-terminal fragments (NTF and CTF), a putative hormone-binding domain (HBD), and multiple N-glycosylation sites. The C-terminus of each BAI subtype ends with a conserved Gln-Thr-Glu-Val (QTEV) motif known to interact with PDZ domain-containing proteins, but only BAI1 possesses a proline-rich region, which may be involved in protein-protein interactions.


Pssm-ID: 320379  Cd Length: 253  Bit Score: 104.64  E-value: 2.59e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2546 AASVTALVLTAAVLLSL-RSLKSNVRGIHANVAAALGVAELLFLLGIHRTHNQLLCTVVAILLHYFFLSTFAWLLVQGLH 2624
Cdd:cd15251    13 GVSCLALLTLLAIYAAFwRYIRSERSIILINFCLSIISSNILILVGQTQTLNKGVCTMTAAFLHFFFLSSFCWVLTEAWQ 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2625 LYrMQVEPRNVDRGAMRFYHALGWGVPAVLLGLAVGLD-PEGYGNPDFCWISIHEPLIWSFAGP---IVLVIVMNGIMFL 2700
Cdd:cd15251    93 SY-MAVTGRMRTRLIRKRFLCLGWGLPALVVAVSVGFTrTKGYGTSSYCWLSLEGGLLYAFVGPaaaVVLVNMVIGILVF 171

                         170       180
                  ....*....|....*....|....*..
gi 564365651 2701 --LAARTSCSTGQREAKKTSVLVLPRL 2725
Cdd:cd15251   172 nkLVSRDGISDNAMASLWSSCVVLPLL 198
Laminin_G_1 pfam00054
Laminin G domain;
1534-1696 6.18e-23

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 96.62  E-value: 6.18e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  1534 FATVQPSGLLFYNGRlNEKHDFLALELVAGQVRLTYSTGESSTVVSPTVPggLSDGQWHTVHLrYYNKprtdalggaqgp 1613
Cdd:pfam00054    1 FRTTEPSGLLLYNGT-QTERDFLALELRDGRLEVSYDLGSGAAVVRSGDK--LNDGKWHSVEL-ERNG------------ 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  1614 skdKVAVLSVDDCNVAValrfgaeiGNYScaaagvqTSSKKSLDLTGPLLLGGVPNL---PENFPVSRkDFIGCMRDLHI 1690
Cdd:pfam00054   65 ---RSGTLSVDGEARPT--------GESP-------LGATTDLDVDGPLYVGGLPSLgvkKRRLAISP-SFDGCIRDVIV 125


                   ....*.
gi 564365651  1691 DGRRVD 1696
Cdd:pfam00054  126 NGKPLD 131
Cadherin pfam00028
Cadherin domain;
429-527 7.09e-23

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 95.06  E-value: 7.09e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651   429 YRETLRENVEEGYPILQLRATDGDAPPNANLRYRFVGSPAARTaaaaaFEIDPRSGLISTSGRVDREHMESYELVVEASD 508
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPNGRIFYSILGGGPGGN-----FRIDPDTGDISTTKPLDRESIGEYELTVEATD 75

                           90
                   ....*....|....*....
gi 564365651   509 QGqePGPRSATVRVHITVL 527
Cdd:pfam00028   76 SG--GPPLSSTATVTITVL 92
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 1081-1158 8.44e-23

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 94.34  E-value: 8.44e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651   1081 TAVDPDDGPNAHIMYQIVEGNIPELFQMDIFSGELTALIDLDYEARQEYVIVVQAT---SAPLVSRATVHVRLVDQNDNS 1157
Cdd:smart00112    1 SATDADSGENGKVTYSILSGNDDGLFSIDPETGEITTTKPLDREEQPEYTLTVEATdggGPPLSSTATVTITVLDVNDNA 80


                    .
gi 564365651   1158 P 1158
Cdd:smart00112   81 P 81
7tmB2_GPR124-like_Adhesion_III cd15259
orphan GPR124 and related proteins, group III adhesion GPCRs, member of class B2 family of ...
 2543-2707 1.02e-22

orphan GPR124 and related proteins, group III adhesion GPCRs, member of class B2 family of seven-transmembrane G protein-coupled receptors; group III adhesion GPCRs include orphan GPR123, GPR124, GPR125, and their closely related proteins. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. GPR123 is predominantly expressed in the CNS including thalamus, brain stem and regions containing large pyramidal cells. GPR124, also known as tumor endothelial marker 5 (TEM5), is highly expressed in tumor vessels and in the vasculature of the developing embryo. GPR124 is essentially required for proper angiogenic sprouting into neural tissue, CNS-specific vascularization, and formation of the blood-brain barrier. GPR124 also interacts with the PDZ domain of DLG1 (discs large homolog 1) through its PDZ-binding motif. Recently, studies of double-knockout mice showed that GPR124 functions as a co-activator of Wnt7a/Wnt7b-dependent beta-catenin signaling in brain endothelium. Furthermore, WNT7-stimulated beta-catenin signaling is regulated by GPR124's intracellular PDZ binding motif and leucine-rich repeats (LRR) in its N-terminal extracellular domain. GPR125 directly interacts with dishevelled (Dvl) via its intracellular C-terminus, and together, GPR125 and Dvl recruit a subset of planar cell polarity (PCP) components into membrane subdomains, a prerequisite for activation of Wnt/PCP signaling. Thus, GPR125 influences the noncanonical WNT/PCP pathway, which does not involve beta-catenin, through interacting with and modulating the distribution of Dvl.


Pssm-ID: 320387 [Multi-domain]  Cd Length: 260  Bit Score: 100.14  E-value: 1.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2543 VVVAASVTALVLTAAVLLSLRSLKSNVR----GIHA--NVAAALGVAELLFLLGIHRTHNQLLCTVVAILLHYFFLSTFA 2616
Cdd:cd15259     7 VVYAGAALCLLCLLATIITYIVFHRLIRisrkGRHMlvNLCLHLLLTCVVFVGGINRTANQLVCQAVGILLHYSTLCTLL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2617 WLLVQGLHLYR-------------MQVEPRnvdRGAMRFYhALGWGVPAVLLGLAVGLDPEGYGNPDFCWISiHEPLIWS 2683
Cdd:cd15259    87 WVGVTARNMYKqvtktakppqdedQPPRPP---KPMLRFY-LIGWGIPLIICGITAAVNLDNYSTYDYCWLA-WDPSLGA 161

                         170       180
                  ....*....|....*....|....
gi 564365651 2684 FAGPIVLVIVMNGIMFLlaaRTSC 2707
Cdd:cd15259   162 FYGPAALIVLVNCIYFL---RIYC 182
7tmB2_BAI2 cd15988
brain-specific angiogenesis inhibitor 2, a group VII adhesion GPCR, member of the class B2 ...
 2546-2732 1.86e-22

brain-specific angiogenesis inhibitor 2, a group VII adhesion GPCR, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Brain-specific angiogenesis inhibitors (BAI1-3) constitute the group VII of cell-adhesion receptors that have been implicated in vascularization of glioblastomas. They belong to the B2 subfamily of class B GPCRs, are predominantly expressed in the brain, and are only present in vertebrates. Three BAIs, like all adhesion receptors, are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. For example, BAI1 N-terminus contain an integrin-binding RGD (Arg-Gly-Asp) motif in addition to five thrombospondin type 1 repeats (TSRs), which are known to regulate the anti-angiogenic activity of thrombospondin-1, whereas BAI2 and BAI3 have four TSRs, but do not possess RGD motifs. The TSRs are functionally involved in cell attachment, activation of latent TGF-beta, inhibition of angiogenesis and endothelial cell migration. The TSRs of BAI1 mediates direct binding to phosphatidylserine, which enables both recognition and internalization of apoptotic cells by phagocytes. Thus, BAI1 functions as a phosphatidylserine receptor that forms a trimeric complex with ELMO and Dock180, leading to activation of Rac-GTPase which promotes the binding and phagocytosis of apoptotic cells. BAI3 can also interact with the ELMO-Dock180 complex to activate the Rac pathway and can also bind to secreted C1ql proteins of the C1Q complement family via its N-terminal TSRs. BAI3 and its ligands C1QL1 are highly expressed during synaptogenesis and are involved in synapse specificity. Moreover, BAI2 acts as a transcription repressor to regulate vascular endothelial growth factor (VEGF) expression through interaction with GA-binding protein gamma (GABP). The N-terminal extracellular domains of all three BAIs also contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain, which undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif to generate N- and C-terminal fragments (NTF and CTF), a putative hormone-binding domain (HBD), and multiple N-glycosylation sites. The C-terminus of each BAI subtype ends with a conserved Gln-Thr-Glu-Val (QTEV) motif known to interact with PDZ domain-containing proteins, but only BAI1 possesses a proline-rich region, which may be involved in protein-protein interactions.


Pssm-ID: 320654 [Multi-domain]  Cd Length: 291  Bit Score: 100.41  E-value: 1.86e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2546 AASVTALVLTAAVLLSL-RSLKSNVRGIHANVAAALGVAELLFLLGIHRTHNQLLCTVVAILLHYFFLSTFAWLLVQGLH 2624
Cdd:cd15988    13 AVSCMALLILLAIYAAFwRFIRSERSIILLNFCLSILASNILILVGQSQTLSKGVCTMTAAFLHFFFLSSFCWVLTEAWQ 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2625 LYrMQVEPRNVDRGAMRFYHALGWGVPAVLLGLAVGLD-PEGYGNPDFCWISIHEPLIWSFAGP---IVLVIVMNGIMFL 2700
Cdd:cd15988    93 SY-LAVIGRMRTRLVRKRFLCLGWGLPALVVAVSVGFTrTKGYGTASYCWLSLEGGLLYAFVGPaavIVLVNMLIGIIVF 171

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 564365651 2701 --LAARTSCSTGQREAKKTSvlvlPRLPC-----PCGRC 2732
Cdd:cd15988   172 nkLMSRDGISDKSKKQRAGS----EAEPCsslllKCSKC 206
7tmB2_GPR128 cd15257
orphan adhesion receptor GPR128, member of the class B2 family of seven-transmembrane G ...
 2537-2709 6.69e-22

orphan adhesion receptor GPR128, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR128 is an orphan receptor of the adhesion family (subclass B2) that belongs to the class B GPCRs. Expression of GPR128 was detected in the mouse intestinal mucosa and is thought to be involved in energy balance, as its knockout mice showed a decrease in body weight gain and an increase in intestinal contraction frequency compared to wild-type controls. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. These include, for example, EGF (epidermal growth factor)-like domains in CD97, Celsr1 (cadherin family member), Celsr2, Celsr3, EMR1 (EGF-module-containing mucin-like hormone receptor-like 1), EMR2, EMR3, and Flamingo; two laminin A G-type repeats and nine cadherin domains in Flamingo and its human orthologs Celsr1, Celsr2 and Celsr3; olfactomedin-like domains in the latrotoxin receptors; and five or four thrombospondin type 1 repeats in BAI1 (brain-specific angiogenesis inhibitor 1), BAI2 and BAI3. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320385 [Multi-domain]  Cd Length: 303  Bit Score: 98.79  E-value: 6.69e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2537 LAVFTHVVVAASVTALVLTAAVLLSLRSL-KSNVRGIHANVAAALGVAELLFLLGIHRTHNQL----------------- 2598
Cdd:cd15257     4 LDIISTIGCVLSIAGLVITIIFHLHTRKLrKSSVTWVLLNLCSSLLLFNIIFTSGVENTNNDYeistvpdretntvllse 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2599 --------LCTVVAILLHYFFLSTFAWLLVQGLHLY-----RMQVEPRNVdrgaMRFYHALGWGVPAVLLGLAVG----- 2660
Cdd:cd15257    84 eyvepdtdVCTAVAALLHYFLLVTFMWNAVYSAQLYlllirMMKPLPEMF----ILQASAIGWGIPAVVVAITLGatyrf 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564365651 2661 -----LDPEGYGNPDFCWI-------SIHEPLIWSFAGPIVLVIVMNGIMFLLAARTSCST 2709
Cdd:cd15257   160 ptslpVFTRTYRQEEFCWLaaldknfDIKKPLLWGFLLPVGLILITNVILFIMTSQKVLKK 220
Cadherin pfam00028
Cadherin domain;
321-414 7.11e-22

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 91.98  E-value: 7.11e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651   321 YQTLVPENEAAGTAVLRVVAQDPDPGEAGRLVYSLaalMNSRSLELFSIDPQSGLIRTAAALDRESMERHYLRVTAQDHG 400
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPNGRIFYSI---LGGGPGGNFRIDPDTGDISTTKPLDRESIGEYELTVEATDSG 77

                           90
                   ....*....|....
gi 564365651   401 SPRLSATTMVAVTV 414
Cdd:pfam00028   78 GPPLSSTATVTITV 91
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 751-845 1.27e-21

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 91.61  E-value: 1.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  751 EYHLRLNEDAAVGTSVVSVTAVDRD--ANSAISYQITGGNTRNRFAISTQggMGLVTLALPLDYKQERYFKLVLTASDR- 827
Cdd:cd11304     1 SYEVSVPENAPPGTVVLTVSATDPDsgENGEVTYSIVSGNEDGLFSIDPS--TGEITTAKPLDREEQSSYTLTVTATDGg 78

                          90       100
                  ....*....|....*....|
gi 564365651  828 --ALHDHCYVHINITDANTH 845
Cdd:cd11304    79 gpPLSSTATVTITVLDVNDN 98
Cadherin pfam00028
Cadherin domain;
854-942 1.61e-21

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 91.21  E-value: 1.61e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651   854 YSVSMNEDRPVGSTVVVISASDDDVGENARITY-LLEDNLPQ-FRIDADSGAITLQAPLDYEDQVTYTLAITARDNGIPQ 931
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPNGRIFYsILGGGPGGnFRIDPDTGDISTTKPLDRESIGEYELTVEATDSGGPP 80

                           90
                   ....*....|.
gi 564365651   932 KADTTYVEVMV 942
Cdd:pfam00028   81 LSSTATVTITV 91
Cadherin pfam00028
Cadherin domain;
1063-1150 1.83e-21

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 90.82  E-value: 1.83e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  1063 FEVRVKENSIVGSVVAQITAVDPDDGPNAHIMYQIVEGNIPELFQMDIFSGELTALIDLDYEARQEYVIVVQATSA---P 1139
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPNGRIFYSILGGGPGGNFRIDPDTGDISTTKPLDRESIGEYELTVEATDSggpP 80

                           90
                   ....*....|.
gi 564365651  1140 LVSRATVHVRL 1150
Cdd:pfam00028   81 LSSTATVTITV 91
7tmB2_BAI1 cd15990
brain-specific angiogenesis inhibitor 1, a group VII adhesion GPCR, member of the class B2 ...
 2543-2701 1.68e-20

brain-specific angiogenesis inhibitor 1, a group VII adhesion GPCR, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Brain-specific angiogenesis inhibitors (BAI1-3) constitute the group VII of cell-adhesion receptors that have been implicated in vascularization of glioblastomas. They belong to the B2 subfamily of class B GPCRs, are predominantly expressed in the brain, and are only present in vertebrates. Three BAIs, like all adhesion receptors, are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. For example, BAI1 N-terminus contain an integrin-binding RGD (Arg-Gly-Asp) motif in addition to five thrombospondin type 1 repeats (TSRs), which are known to regulate the anti-angiogenic activity of thrombospondin-1, whereas BAI2 and BAI3 have four TSRs, but do not possess RGD motifs. The TSRs are functionally involved in cell attachment, activation of latent TGF-beta, inhibition of angiogenesis and endothelial cell migration. The TSRs of BAI1 mediates direct binding to phosphatidylserine, which enables both recognition and internalization of apoptotic cells by phagocytes. Thus, BAI1 functions as a phosphatidylserine receptor that forms a trimeric complex with ELMO and Dock180, leading to activation of Rac-GTPase which promotes the binding and phagocytosis of apoptotic cells. BAI3 can also interact with the ELMO-Dock180 complex to activate the Rac pathway and can also bind to secreted C1ql proteins of the C1Q complement family via its N-terminal TSRs. BAI3 and its ligands C1QL1 are highly expressed during synaptogenesis and are involved in synapse specificity. Moreover, BAI2 acts as a transcription repressor to regulate vascular endothelial growth factor (VEGF) expression through interaction with GA-binding protein gamma (GABP). The N-terminal extracellular domains of all three BAIs also contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain, which undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif to generate N- and C-terminal fragments (NTF and CTF), a putative hormone-binding domain (HBD), and multiple N-glycosylation sites. The C-terminus of each BAI subtype ends with a conserved Gln-Thr-Glu-Val (QTEV) motif known to interact with PDZ domain-containing proteins, but only BAI1 possesses a proline-rich region, which may be involved in protein-protein interactions.


Pssm-ID: 320656  Cd Length: 267  Bit Score: 93.90  E-value: 1.68e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2543 VVVAASVTALVLTAAVLLSL---RSLKSNVRGIHANVAAALGVAELLFLLGIHRTHNQLLCTVVAILLHYFFLSTFAWLL 2619
Cdd:cd15990    11 LIVGCGVSSLTLLLLIIIYVsvwRYIRSERSVILINFCLSIISSNALILIGQTQTRNKVVCTLVAAFLHFFFLSSFCWVL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2620 VQGLHLYrMQVEPRNVDRGAMRFYHALGWGVPAVLLGLAVGL-DPEGYGNPDFCWISIHEPLIWSFAGPIVLVIVMNGIM 2698
Cdd:cd15990    91 TEAWQSY-MAVTGRLRNRIIRKRFLCLGWGLPALVVAISVGFtKAKGYGTVNYCWLSLEGGLLYAFVGPAAAVVLVNMVI 169


                  ...
gi 564365651 2699 FLL 2701
Cdd:cd15990   170 GIL 172
HormR smart00008
Domain present in hormone receptors;
2117-2181 1.23e-19

Domain present in hormone receptors;


Pssm-ID: 214468  Cd Length: 70  Bit Score: 84.87  E-value: 1.23e-19
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564365651   2117 YDACPKSLRSGVWWPQTKFGVLATVPCPRGALGLRGTGAAVRLCDEDHGWLE--PDFFNCTSPAFRE 2181
Cdd:smart00008    2 DLGCPATWDGIICWPQTPAGQLVEVPCPKYFSGFSYKTGASRNCTENGGWSPpfPNYSNCTSNDYEE 68
7tmB2_BAI3 cd15989
brain-specific angiogenesis inhibitor 3, a group VII adhesion GPCR, member of the class B2 ...
 2548-2701 1.55e-19

brain-specific angiogenesis inhibitor 3, a group VII adhesion GPCR, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Brain-specific angiogenesis inhibitors (BAI1-3) constitute the group VII of cell-adhesion receptors that have been implicated in vascularization of glioblastomas. They belong to the B2 subfamily of class B GPCRs, are predominantly expressed in the brain, and are only present in vertebrates. Three BAIs, like all adhesion receptors, are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. For example, BAI1 N-terminus contain an integrin-binding RGD (Arg-Gly-Asp) motif in addition to five thrombospondin type 1 repeats (TSRs), which are known to regulate the anti-angiogenic activity of thrombospondin-1, whereas BAI2 and BAI3 have four TSRs, but do not possess RGD motifs. The TSRs are functionally involved in cell attachment, activation of latent TGF-beta, inhibition of angiogenesis and endothelial cell migration. The TSRs of BAI1 mediates direct binding to phosphatidylserine, which enables both recognition and internalization of apoptotic cells by phagocytes. Thus, BAI1 functions as a phosphatidylserine receptor that forms a trimeric complex with ELMO and Dock180, leading to activation of Rac-GTPase which promotes the binding and phagocytosis of apoptotic cells. BAI3 can also interact with the ELMO-Dock180 complex to activate the Rac pathway and can also bind to secreted C1ql proteins of the C1Q complement family via its N-terminal TSRs. BAI3 and its ligands C1QL1 are highly expressed during synaptogenesis and are involved in synapse specificity. Moreover, BAI2 acts as a transcription repressor to regulate vascular endothelial growth factor (VEGF) expression through interaction with GA-binding protein gamma (GABP). The N-terminal extracellular domains of all three BAIs also contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain, which undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif to generate N- and C-terminal fragments (NTF and CTF), a putative hormone-binding domain (HBD), and multiple N-glycosylation sites. The C-terminus of each BAI subtype ends with a conserved Gln-Thr-Glu-Val (QTEV) motif known to interact with PDZ domain-containing proteins, but only BAI1 possesses a proline-rich region, which may be involved in protein-protein interactions.


Pssm-ID: 320655 [Multi-domain]  Cd Length: 293  Bit Score: 91.67  E-value: 1.55e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2548 SVTALVLTAAVLLSL-RSLKSNVRGIHANVAAALGVAELLFLLGIHRTHNQLLCTVVAILLHYFFLSTFAWLLVQGLHLY 2626
Cdd:cd15989    17 SCLALITLAVVYAALwRYIRSERSIILINFCLSIISSNILILVGQTQTHNKGICTMTTAFLHFFFLASFCWVLTEAWQSY 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564365651 2627 rMQVEPRNVDRGAMRFYHALGWGVPAVLLGLAVGLD-PEGYGNPDFCWISIHEPLIWSFAGPIVLVIVMNGIMFLL 2701
Cdd:cd15989    97 -MAVTGKIRTRLIRKRFLCLGWGLPALVVAISMGFTkAKGYGTPHYCWLSLEGGLLYAFVGPAAAVVLVNMVIGIL 171
7tmB2_GPR126-like_Adhesion_VIII cd15258
orphan GPR126 and related proteins, group VIII adhesion GPCRs, member of the class B2 family ...
 2537-2722 1.75e-19

orphan GPR126 and related proteins, group VIII adhesion GPCRs, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Group VIII adhesion GPCRs include orphan GPCRs such as GPR56, GPR64, GPR97, GPR112, GPR114, and GPR126. GPR56 is involved in the regulation of oligodendrocyte development and myelination in the central nervous system via coupling to G(12/13) proteins, which leads to the activation of RhoA GTPase. GPR126, on the other hand, is required for Schwann cells, but not oligodendrocyte myelination in the peripheral nervous system. Gpr64 is mainly expressed in the epididymis of male reproductive tract, and targeted deletion of GPR64 causes sperm stasis and efferent duct blockage due to abnormal fluid reabsorption, resulting in male infertility. GPR64 is also over-expressed in Ewing's sarcoma (ES), as well as upregulated in other carcinomas from kidney, prostate or lung, and promotes invasiveness and metastasis in ES via the upregulation of placental growth factor (PGF) and matrix metalloproteinase (MMP) 1. GPR97 is identified as a lymphatic adhesion receptor that is specifically expressed in lymphatic endothelium, but not in blood vascular endothelium, and is shown to regulate migration of lymphatic endothelial cells via the small GTPases RhoA and cdc42. GPR112 is specifically expressed in normal enterochromatin cells and gastrointestinal neuroendocrine carcinoma cells, but its biological function is unknown. GPR114 is mainly found in granulocytes (polymorphonuclear leukocytes), and GPR114-transfected cells induced an increase in cAMP levels via coupling to G(s) protein. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320386 [Multi-domain]  Cd Length: 267  Bit Score: 90.94  E-value: 1.75e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2537 LAVFTHVVVAASVTALVLTAAVLLSLRSL-KSNVRGIHANVAAALGVAELLFLL--GIHRTHNQLLCTVVAILLHYFFLS 2613
Cdd:cd15258     4 LTFISYVGCGISAIFLAITILTYIAFRKLrRDYPSKIHMNLCAALLLLNLAFLLssWIASFGSDGLCIAVAVALHYFLLA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2614 TFAWLLVQGLHLYRMQVEPRN--VDRGAMRFyHALGWGVPAVLLGLAVGLDPEGYG-----------NPDFCWisIHEPL 2680
Cdd:cd15258    84 CLTWMGLEAFHLYLLLVKVFNtyIRRYILKL-CLVGWGLPALLVTLVLSVRSDNYGpitipngegfqNDSFCW--IRDPV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 564365651 2681 IWSF--AGPIVLVIVMNGIMFLLAARTSCSTGQREAKKTSVLVL 2722
Cdd:cd15258   161 VFYItvVGYFGLTFLFNMVMLATVLVQICRLREKAQATPRKRAL 204
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 1755-1911 2.94e-18

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 84.01  E-value: 2.94e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 1755 PYHFQGNGTLSwdFGNDMPVSVPWYLGLSFRTRATKGVLMQV-QLGPHSVLLCKLDQGLLSVTLSRASGHAVhlLLDQMT 1833
Cdd:cd00110     1 GVSFSGSSYVR--LPTLPAPRTRLSISFSFRTTSPNGLLLYAgSQNGGDFLALELEDGRLVLRYDLGSGSLV--LSSKTP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 1834 VSDGRWHDLRLElqeepggRRGHHIFMvSLDFTLFQDTMAMGSELEGLKVKHLHVGGPPPSSKEEG---PQGLVGCIQGV 1910
Cdd:cd00110    77 LNDGQWHSVSVE-------RNGRSVTL-SVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGlpvSPGFVGCIRDL 148


                  .
gi 564365651 1911 W 1911
Cdd:cd00110   149 K 149
7tmB1_NPR_B4_insect-like cd15260
insect neuropeptide receptor subgroup B4 and related proteins, member of the class B family of ...
 2548-2700 7.05e-17

insect neuropeptide receptor subgroup B4 and related proteins, member of the class B family of seven-transmembrane G protein-coupled receptors; This subgroup includes a neuropeptide receptor found in Nilaparvata lugens (brown planthopper) and its closely related proteins from mollusks and annelid worms. They belong to the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. The class B GPCRs have been identified in all the vertebrates, from fishes to mammals, as well as invertebrates including Caenorhabditis elegans and Drosophila melanogaster, but are not present in plants, fungi, or prokaryotes.


Pssm-ID: 320388 [Multi-domain]  Cd Length: 267  Bit Score: 83.09  E-value: 7.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2548 SVTALVLTAAVLLSLRSLKSNVRGIHANVAAALGVAELLFLL-------GIHRTH-NQLLCTVVAILLHYFFLSTFAWLL 2619
Cdd:cd15260    15 SLIALIISLAIFFSFRSLRCTRITIHMNLFISFALNNLLWIVwyklvvdNPEVLLeNPIWCQALHVLLQYFMVCNYFWMF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2620 VQGLHLYRMQVEPRNVDRGAMRFYHALGWGVPAVLLGLAVGLDPEGYGNPDFCWISIHEPLiWSFAGPIVLVIVMNgIMF 2699
Cdd:cd15260    95 CEGLYLHTVLVVAFISEKSLMRWFIAIGWGVPLVITAIYAGVRASLPDDTERCWMEESSYQ-WILIVPVVLSLLIN-LIF 172


                  .
gi 564365651 2700 L 2700
Cdd:cd15260   173 L 173
7tmB1_DH_R cd15263
insect diuretic hormone receptors, member of the class B family of seven-transmembrane G ...
 2548-2702 1.05e-16

insect diuretic hormone receptors, member of the class B family of seven-transmembrane G protein-coupled receptors; This group includes G protein-coupled receptors that specifically bind to insect diuretic hormones found in Manduca sexta (moth) and Acheta domesticus (the house cricket), among others. Insect diuretic hormone and their GPCRs play critical roles in the regulation of water and ion balance. Thus they are attractive targets for developing new insecticides. Activation of the diuretic hormone receptors stimulate adenylate cyclase, thereby increasing cAMP levels in Malpighian tube. They belong to the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of Gs family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx.


Pssm-ID: 320391 [Multi-domain]  Cd Length: 272  Bit Score: 82.80  E-value: 1.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2548 SVTALVLTAAVLLS---LRSLKSNvrgIHANVAAALGVAELLFLLG----IHRTHNQLLCTVVAILLHYFFLSTFAWLLV 2620
Cdd:cd15263    15 SLVALSLALWIFLYfkdLRCLRNT---IHTNLMFTYILADLTWILTltlqVSIGEDQKSCIILVVLLHYFHLTNFFWMFV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2621 QGLHLYRMQVEPRNVDRGAMRFYHALGWGVPAVLLGLAV------------GLDPEGYgnPDFC-WISIHePLIWSFAGP 2687
Cdd:cd15263    92 EGLYLYMLVVETFSGENIKLRVYAFIGWGIPAVVIVIWAivkalaptapntALDPNGL--LKHCpWMAEH-IVDWIFQGP 168

                         170
                  ....*....|....*
gi 564365651 2688 IVLVIVMNgIMFLLA 2702
Cdd:cd15263   169 AILVLAVN-LVFLVR 182
7tmB1_hormone_R cd15041
The subfamily B1 of hormone receptors (secretin-like), member of the class B family ...
 2546-2701 1.17e-16

The subfamily B1 of hormone receptors (secretin-like), member of the class B family seven-transmembrane G protein-coupled receptors; The B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of this subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. Moreover, the B1 subfamily receptors play key roles in hormone homeostasis and are promising drug targets in various human diseases including diabetes, osteoporosis, obesity, neurodegenerative conditions (Alzheimer###s and Parkinson's), cardiovascular disease, migraine, and psychiatric disorders (anxiety, depression). Furthermore, the subfamilies B2 and B3 consist of receptors that are capable of interacting with epidermal growth factors (EGF) and the Drosophila melanogaster Methuselah gene product (Mth), respectively. The class B GPCRs have been identified in all the vertebrates, from fishes to mammals, as well as invertebrates including Caenorhabditis elegans and Drosophila melanogaster, but are not present in plants, fungi, or prokaryotes.


Pssm-ID: 341321 [Multi-domain]  Cd Length: 273  Bit Score: 82.66  E-value: 1.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2546 AASVTALVLTAAVLLSLRSLKSNVRGIHANVAAAL---GVAELLFLLGIHRT------------HNQLLCTVVAILLHYF 2610
Cdd:cd15041    13 SLSLVALLPAIVIFLYFRSLRCTRIRLHINLFLSFilrAVFWIIWDLLVVYDrltssgvetvlmQNPVGCKLLSVLKRYF 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2611 FLSTFAWLLVQGLHLYRMQV-----EPRNvdrgaMRFYHALGWGVPAVLLGLAVGLdpEGYGNPDFCWISIH-EPLIWSF 2684
Cdd:cd15041    93 KSANYFWMLCEGLYLHRLIVvaffsEPSS-----LKLYYAIGWGLPLVIVVIWAIV--RALLSNESCWISYNnGHYEWIL 165

                         170
                  ....*....|....*..
gi 564365651 2685 AGPIVLVIVMNgiMFLL 2701
Cdd:cd15041   166 YGPNLLALLVN--LFFL 180
Cadherin pfam00028
Cadherin domain;
752-840 6.10e-16

Cadherin domain;


Pssm-ID: 394985 [Multi-domain]  Cd Length: 92  Bit Score: 75.41  E-value: 6.10e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651   752 YHLRLNEDAAVGTSVVSVTAVDRD--ANSAISYQITGGNTRNRFAISTQGgmGLVTLALPLDYKQERYFKLVLTASDRAL 829
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDlgPNGRIFYSILGGGPGGNFRIDPDT--GDISTTKPLDRESIGEYELTVEATDSGG 78

                           90
                   ....*....|....
gi 564365651   830 H---DHCYVHINIT 840
Cdd:pfam00028   79 PplsSTATVTITVL 92
LamG smart00282
Laminin G domain;
1779-1911 9.42e-16

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 76.22  E-value: 9.42e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651   1779 YLGLSFRTRATKGVLMQV-QLGPHSVLLCKLDQGLLSVTLSRASGhAVHLLLDQMTVSDGRWHDLRLElqeepggRRGHH 1857
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAgSKGGGDYLALELRDGRLVLRYDLGSG-PARLTSDPTPLNDGQWHRVAVE-------RNGRS 72

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 564365651   1858 IFMvSLDFTLFQDTMAMGSElEGLKVK-HLHVGGPPPSSKEEG---PQGLVGCIQGVW 1911
Cdd:smart00282   73 VTL-SVDGGNRVSGESPGGL-TILNLDgPLYLGGLPEDLKLPPlpvTPGFRGCIRNLK 128
7tmB1_CRF-R cd15264
corticotropin-releasing factor receptors, member of the class B family of seven-transmembrane ...
 2548-2725 2.37e-15

corticotropin-releasing factor receptors, member of the class B family of seven-transmembrane G protein-coupled receptors; The vertebrate corticotropin-releasing factor (CRF) receptors are predominantly expressed in central nervous system with high levels in cortex tissue, brain stem, and pituitary. They have two isoforms as a result of alternative splicing of the same receptor gene: CRF-R1 and CRF-R2, which differ in tissue distribution and ligand binding affinities. Recently, a third CRF receptor (CRF-R3) has been identified in catfish pituitary. The catfish CRF-R1 is highly homologous to CRF-R3. CRF is a 41-amino acid neuropeptide that plays a central role in coordinating neuroendocrine, behavioral, and autonomic responses to stress by acting as the primary neuroregulator of the hypothalamic-pituitary-adrenal axis, which controls the levels of cortisol and other stress related hormones. In addition, the CRF family of neuropeptides also includes structurally related peptides such as mammalian urocortin, fish urotensin I, and frog sauvagine. The actions of CRF and CRF-related peptides are mediated through specific binding to CRF-R1 and CRF-R2. CRF and urocortin 1 bind and activate mammalian CRF-R1 with similar high affinities. By contrast, urocortin 2 and urocortin 3 do not bind to CRF-R1 or stimulate CRF-R1-mediated cAMP formation. Urocortin 1 also shows high affinity for mammalian CRF-R2, whereas CRF has significantly lower affinity for this receptor. These evidence suggest that urocortin 1 is an endogenous ligand for CRF-R1 and CRF-R2. The CRF receptors are members of the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, and parathyroid hormone (PTH). These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on its cellular location and function, CRF receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways.


Pssm-ID: 320392 [Multi-domain]  Cd Length: 265  Bit Score: 78.61  E-value: 2.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2548 SVTALVLTAAVLLSLRSLKSNVRGIHANVAAALGVAELLFLL------GIHRTHNQLLCTVVAILLHYFFLSTFAWLLVQ 2621
Cdd:cd15264    15 SLVALAVALIIFLYFRSLRCLRNNIHCNLIVTFILRNVTWFImqntltEIHHQSNQWVCRLIVTVYNYFQVTNFFWMFVE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2622 GLHLYRMQVEPRNVDRGAMRFYHALGWGVPAVLLgLAVGLDPEGYGNpDFCWISIHE--PLIWSFAGPIVLVIVMNgIMF 2699
Cdd:cd15264    95 GLYLHTMIVWAYSADKIRFWYYIVIGWCIPCPFV-LAWAIVKLLYEN-EHCWLPKSEnsYYDYIYQGPILLVLLIN-FIF 171

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 564365651 2700 L----------LAARTSCSTGQ-REAKKTSVLVLPRL 2725
Cdd:cd15264   172 LfnivwvlitkLRASNTLETIQyRKAVKATLVLLPLL 208
7tmB2_GPR112 cd15997
Probable G protein-coupled receptor 112, member of the class B2 family of seven-transmembrane ...
 2535-2720 5.36e-15

Probable G protein-coupled receptor 112, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR112 is an orphan receptor that has been classified as that belongs to the Group VIII of adhesion GPCRs. Other members of the Group VII include orphan GPCRs such as GPR56, GPR64, GPR97, GPR114, and GPR126. GPR112 is specifically expressed in normal enterochromatin cells and gastrointestinal neuroendocrine carcinoma cells, but its biological function is unknown. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320663  Cd Length: 269  Bit Score: 77.78  E-value: 5.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2535 ELLAVFTHVVVAASVTALVLTAAVLLSLRSL-KSNVRGIHANVAAALGVAELLFLLG--IHRTHNQLLCTVVAILLHYFF 2611
Cdd:cd15997     2 RILTLITYLGCGISSIFLGITLVTYLAFEKLrRDYPSKILINLCTALLMLNLVFLLNswLSSFNNYGLCITVAAFLHYFL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2612 LSTFAWLLVQGLHLYRMQVEPRNVdrgAMRFY----HALGWGVPAVLLGLAVGLDPEGYGN----------PDFCWISIH 2677
Cdd:cd15997    82 LASFTWMGLEAVHMYFALVKVFNI---YIPNYilkfCIAGWGIPAVVVALVLAINKDFYGNelssdslhpsTPFCWIQDD 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 564365651 2678 EPLIWSFAGPIVLVIVMNGIMF---LLAARTSCSTGQREAKKTSVL 2720
Cdd:cd15997   159 VVFYISVVAYFCLIFLCNISMFitvLIQIRSMKAKKPSRNWKQGFL 204
7tmB2_GPR116-like_Adhesion_VI cd15932
orphan GPR116 and related proteins, group IV adhesion GPCRs, member of the class B2 family of ...
 2536-2724 1.33e-14

orphan GPR116 and related proteins, group IV adhesion GPCRs, member of the class B2 family of seven-transmembrane G protein-coupled receptors; group VI adhesion GPCRs consist of orphan receptors GPR110, GPR111, GPR113, GPR115, GPR116, and closely related proteins. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. GPR110 possesses a SEA box in the N-terminal has been identified as an oncogene over-expressed in lung and prostate cancer. GPR113 contains a hormone binding domain and one EGF (epidermal grown factor) domain. GPR112 has extremely long N-terminus (about 2,400 amino acids) containing a number of Ser/Thr-rich glycosylation sites and a pentraxin (PTX) domain. GPR116 has two C2-set immunoglobulin-like repeats, which is found in the members of the immunoglobulin superfamily of cell surface proteins, and a SEA (sea urchin sperm protein, enterokinase, and a grin)-box, which is present in the extracellular domain of the transmembrane mucin (MUC) family and known to enhance O-glycosylation. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS.


Pssm-ID: 320598 [Multi-domain]  Cd Length: 268  Bit Score: 76.58  E-value: 1.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2536 LLAVFTHVVVAASVTALVLTAAV-LLSLRSLKSN----VRgiHA---NVAAALGVAELLFLLGIH---RTHNQLLCTVVA 2604
Cdd:cd15932     3 ALDYITYVGLGISILSLVLCLIIeALVWKSVTKNktsyMR--HVclvNIALSLLIADIWFIIGAAistPPNPSPACTAAT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2605 ILLHYFFLSTFAWLLVQGLHL-YRMQVEPRNVDRGAMR---FyhALGWGVPAVLLG--LAVGLDPEGYGNPDFCWISIHE 2678
Cdd:cd15932    81 FFIHFFYLALFFWMLTLGLLLfYRLVLVFHDMSKSTMMaiaF--SLGYGCPLIIAIitVAATAPQGGYTRKGVCWLNWDK 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564365651 2679 --PLIwSFAGPIVLVIVMNGIMFLLAA----RTSCSTGQREAKKTSVLVLPR 2724
Cdd:cd15932   159 tkALL-AFVIPALAIVVVNFIILIVVIfkllRPSVGERPSKDEKNALVQIGK 209
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 770-847 1.52e-14

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 70.84  E-value: 1.52e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651    770 TAVDRD--ANSAISYQITGGNTRNRFAISTQGGMglVTLALPLDYKQERYFKLVLTASDRA---LHDHCYVHINITDANT 844
Cdd:smart00112    1 SATDADsgENGKVTYSILSGNDDGLFSIDPETGE--ITTTKPLDREEQPEYTLTVEATDGGgppLSSTATVTITVLDVND 78


                    ...
gi 564365651    845 HRP 847
Cdd:smart00112   79 NAP 81
7tmB2_GPR114 cd15443
orphan adhesion receptor GPR114, member of the class B2 family of seven-transmembrane G ...
 2537-2715 1.92e-14

orphan adhesion receptor GPR114, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR114 is an orphan receptor that has been classified as that belongs to the Group VIII of adhesion GPCRs. Other members of the Group VII include GPR56, GPR64, GPR97, GPR112, and GPR126. GPR114 is mainly found in granulocytes (polymorphonuclear leukocytes), and GPR114-transfected cells induced an increase in cAMP levels via coupling to G(s) protein. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320559 [Multi-domain]  Cd Length: 268  Bit Score: 75.95  E-value: 1.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2537 LAVFTHV-VVAASVTALVLTAAVLLSLRSLK---SNVRGIHANVAAALGVAELLFLLG--IHRTHNQLLCTVVAILLHYF 2610
Cdd:cd15443     1 LEPLTYIsIVGCSISAAASLLTILLHFFSRKqpkDSTTRIHMNLLGSLFLLNGSFLLSppLATSQSTWLCRAAAALLHYS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2611 FLSTFAWLLVQGLHLYRMQVEPRNVdrgAMRFY----HALGWGVPAVLLGLAVGLDPEGYG-----------NPDFCWI- 2674
Cdd:cd15443    81 LLCCLTWMAIEGFHLYLLLVKVYNI---YIRRYvlklCVLGWGLPALIVLLVLIFKREAYGphtiptgtgyqNASMCWIt 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 564365651 2675 --SIHEPLIWSFAGpivLVIVMNGIMFLLAARTSCSTGQREAK 2715
Cdd:cd15443   158 ssKVHYVLVLGYAG---LTSLFNLVVLAWVVRMLRRLRSRKQE 197
GPS smart00303
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ...
 2474-2527 2.47e-14

G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin REJ and polycystin.


Pssm-ID: 197639  Cd Length: 49  Bit Score: 69.34  E-value: 2.47e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 564365651   2474 SKAICVQWDPPGpadqhGMWTARDCELVHRNGSHARCRCSRTGTFGVLMDASPR 2527
Cdd:smart00303    1 FNPICVFWDESS-----GEWSTRGCELLETNGTHTTCSCNHLTTFAVLMDVPPI 49
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
 1784-1910 1.01e-13

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 460494 [Multi-domain]  Cd Length: 126  Bit Score: 70.14  E-value: 1.01e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  1784 FRTRATKGVLMQVQLGPHSVLLCKLDQGLLSVTLSRASGHaVHLLLDQMTVSDGRWHDLRLElqeepggRRGHHIFMvSL 1863
Cdd:pfam02210    1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGP-ESLLSSGKNLNDGQWHSVRVE-------RNGNTLTL-SV 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 564365651  1864 DFTLFQDTMAMGSELEGLKVKHLHVGGPPPSSKEEGP---QGLVGCIQGV 1910
Cdd:pfam02210   72 DGQTVVSSLPPGESLLLNLNGPLYLGGLPPLLLLPALpvrAGFVGCIRDV 121
7tmB2_GPR126 cd15996
orphan adhesion receptor GPR126, member of the class B2 family of seven-transmembrane G ...
 2553-2717 4.48e-13

orphan adhesion receptor GPR126, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR126 is an orphan receptor that has been classified as that belongs to the Group VIII of adhesion GPCRs. Other members of the Group VII include orphan GPCRs such as GPR56, GPR64, GPR97, GPR112, and GPR114. GPR126 is required in Schwann cells for proper differentiation and myelination via G-Protein Activation. GPR126 is believed to couple to G(s)-protein, which leads to activation of adenylate cyclase for cAMP production. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320662  Cd Length: 271  Bit Score: 72.23  E-value: 4.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2553 VLTAAVLLSLRSLKSNVRG----IHANVAAALGVAELLFLLG--IHRTHNQLLCTVVAILLHYFFLSTFAWLLVQGLHLY 2626
Cdd:cd15996    17 IFSAATLLTYIAFEKLRRDypskILMNLSTALLFLNLVFLLDgwIASFEIDELCITVAVLLHFFLLATFTWMGLEAIHMY 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2627 RMQVEPRN--VDRGAMRFYhALGWGVPAVLLGLAV------------GLDPEGYGNPDFCWISIHEPLIWSFAGPIVLVI 2692
Cdd:cd15996    97 IALVKVFNtyIRRYILKFC-IIGWGLPALIVSIVLastndnygygyyGKDKDGQGGDEFCWIKNPVVFYVTCAAYFGIMF 175

                         170       180
                  ....*....|....*....|....*
gi 564365651 2693 VMNGIMFLLAARTSCSTGQREAKKT 2717
Cdd:cd15996   176 LMNVAMFIVVMVQICGRNGKRSNRT 200
7tmB1_GlucagonR-like cd15929
glucagon receptor-like subfamily, member of the class B family of seven-transmembrane G ...
 2534-2721 4.90e-13

glucagon receptor-like subfamily, member of the class B family of seven-transmembrane G protein-coupled receptors; This group represents the glucagon receptor family of G protein-coupled receptors, which includes glucagon receptor (GCGR), glucagon-like peptide-1 receptor (GLP1R), GLP2R, and closely related receptors. These receptors are activated by the members of the glucagon (GCG) peptide family including GCG, glucagon-like peptide 1 (GLP1), and GLP2, which are derived from the large proglucagon precursor. GCGR regulates blood glucose levels by control of hepatic glycogenolysis and gluconeogenesis and by regulation of insulin secretion from the pancreatic beta-cells. Activation of GLP1R stimulates glucose-dependent insulin secretion from pancreatic beta cells, whereas activation of GLP2R stimulates intestinal epithelial proliferation and increases villus height in the small intestine. Receptors in this group belong to the B1 (or secretin-like) subfamily of class B GPCRs, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on their cellular location, GCGR and GLP receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways.


Pssm-ID: 341353 [Multi-domain]  Cd Length: 279  Bit Score: 72.08  E-value: 4.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2534 LELLAVFTHVVVAASVTALVLTAAVLLSLRSLKSNVRGIHANVAAALGV--AELLFLLGIHRTH---------------N 2596
Cdd:cd15929     1 LSSLQVMYTVGYSLSLAALVLALAILLGLRKLHCTRNYIHANLFASFILraLSVLVKDALLPRRysqkgdqdlwstllsN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2597 QLL--CTVVAILLHYFFLSTFAWLLVQGLHLYRMQVEPRNVDRGAMRFYHALGWGVPAVLL---GLAVGLdpegYGNPDf 2671
Cdd:cd15929    81 QASlgCRVAQVLMQYCVAANYYWLLVEGLYLHTLLVLAVFSERSIFRLYLLLGWGAPVLFVvpwGIVKYL----YENTG- 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564365651 2672 CWISIHEPLIW-SFAGPIVLVIVMNGIMFL---------LAARTSCSTGQ--REAKKTSVLV 2721
Cdd:cd15929   156 CWTRNDNMAYWwIIRLPILLAILINFFIFVrilkilvskLRANQMCKTDYkfRLAKSTLTLI 217
7tmB2_GPR113 cd15253
orphan adhesion receptor GPR113, member of the class B2 family of seven-transmembrane G ...
 2537-2725 6.47e-13

orphan adhesion receptor GPR113, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR113 is an orphan receptor that belongs to group VI adhesion-GPCRs along with GPR110, GPR111, GPR115, and GPR116. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. GPR113 contains a hormone binding domain and one EGF (epidermal grown factor) domain, and is primarily expressed in a subset of taste receptor cells. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS.


Pssm-ID: 320381 [Multi-domain]  Cd Length: 271  Bit Score: 71.72  E-value: 6.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2537 LAVFTHVVVAASVTALVLTAAVL-----LSLRSLKSNVRGIH-ANVAAALGVAELLFLLG--IHRTHNQLLCTVVAILLH 2608
Cdd:cd15253     4 LDFLSQVGLGASILALLLCLGIYrlvwrSVVRNKISYFRHMTlVNIAFSLLLADTCFLGAtfLSAGHESPLCLAAAFLCH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2609 YFFLSTFAWLLVQGL-----------HLYRMQVEPRNVdrgamrfyhALGWGVPAVLLGLAVGL-DPEG-YGNPDFCWIS 2675
Cdd:cd15253    84 FFYLATFFWMLVQALmlfhqllfvfhQLAKRSVLPLMV---------TLGYLCPLLIAAATVAYyYPKRqYLHEGACWLN 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 564365651 2676 IHEPLIWSFAGPIVLVIVMNGIMFLLA----ARTSCSTGQR-EAKKTSVLVLPRL 2725
Cdd:cd15253   155 GESGAIYAFSIPVLAIVLVNLLVLFVVlmklMRPSVSEGPPpEERKALLSIFKAL 209
HRM pfam02793
Hormone receptor domain; This extracellular domain contains four conserved cysteines that ...
 2117-2177 7.14e-13

Hormone receptor domain; This extracellular domain contains four conserved cysteines that probably for disulphide bridges. The domain is found in a variety of hormone receptors. It may be a ligand binding domain.


Pssm-ID: 397086  Cd Length: 64  Bit Score: 65.47  E-value: 7.14e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564365651  2117 YDACPKSLRSGVWWPQTKFGVLATVPCPRGALGLRGTGAAVRLCDEDHGWLEP---DFFNCTSP 2177
Cdd:pfam02793    1 GLGCPRTWDGILCWPRTPAGETVEVPCPDYFSGFDPRGNASRNCTEDGTWSEHppsNYSNCTSN 64
7tmB2_GPR56 cd15995
orphan adhesion receptor GPR56, member of the class B2 family of seven-transmembrane G ...
 2535-2734 9.35e-13

orphan adhesion receptor GPR56, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR56 is an orphan receptor that has been classified as that belongs to the Group VIII of adhesion GPCRs. Other members of the Group VII include orphan GPCRs such as GPR64, GPR97, GPR112, GPR114, and GPR126. GPR56 is involved in the regulation of oligodendrocyte development and myelination in the central nervous system via coupling to G(12/13) proteins, which leads to the activation of RhoA GTPase. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320661  Cd Length: 269  Bit Score: 71.01  E-value: 9.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2535 ELLAVFTHV-VVAASVTALVLTAAVLLSLRSLKSNVRGIHANVAAALGVAELLFLLGIH--RTHNQLLCTVVAILLHYFF 2611
Cdd:cd15995     2 HYLTILTYVgCIISALASVFTIAFYLCSRRKPRDYTIYVHMNLLLAIFLLDTSFLISEPlaLTGSEAACRAGGMFLHFSL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2612 LSTFAWLLVQGLHLYRMQVEPRNVD-RGAMRFYHALGWGVPAVLLGLAVGLD--------------PEGYGNPDFCWISi 2676
Cdd:cd15995    82 LACLTWMGIEGYNLYRLVVEVFNTYvPHFLLKLCAVGWGLPIFLVTLIFLVDqdnygpiilavhrsPEKVTYATICWIT- 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564365651 2677 hEPLIWSFA--GPIVLVIVMNGIMFLLAARTSCSTGQREAKKTSVLVLPRLPC----PCGRCFF 2734
Cdd:cd15995   161 -DSLISNITnlGLFSLVFLFNMAMLATMVVEILRLRPRTHKWSHVLTLLGLSLvlgiPWALAFF 223
7tmB2_GPR123 cd16000
G protein-coupled receptor 123, member of the class B2 family of seven-transmembrane G ...
 2540-2700 1.36e-12

G protein-coupled receptor 123, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR123 is an orphan receptor that has been classified as that belongs to the group III of adhesion GPCRs, and also includes orphan receptors GPR124 and GPR125. GPR123 is predominantly expressed in the CNS including thalamus, brain stem and regions containing large pyramidal cells, yet its biological function remains to be determined. Adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320666 [Multi-domain]  Cd Length: 275  Bit Score: 70.75  E-value: 1.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2540 FTHVVVAA--SVTALVLTAAVLLSL---RSLKSNVRGIHA--NVAAALGVAELLFLLGIHRTHNQLLCTVVAILLHYFFL 2612
Cdd:cd16000     3 FLHPVVYActAVMLLCLFASIITYIvhhSTIRISRKGWHMllNFCFHTALTFAVFAGGINRTKYPIICQAVGIVLHYSTL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2613 STFAWLLVQGLHLYRMQVE----PRNVDRGA------MRFYHALGwGVPAVLLGLAVGLDPEGYGNPD----FCWISiHE 2678
Cdd:cd16000    83 STMLWIGVTARNIYKQVTKkphlCQDTDQPPypkqplLRFYLVSG-GVPFIICGITAATNINNYGTEDedtpYCWMA-WE 160

                         170       180
                  ....*....|....*....|..
gi 564365651 2679 PLIWSFAGPIVLVIVMNGIMFL 2700
Cdd:cd16000   161 PSLGAFYGPVAFIVLVTCIYFL 182
7tmB1_Secretin_R-like cd15930
secretin receptor-like group of hormone receptors, member of the class B family of ...
 2546-2700 1.73e-12

secretin receptor-like group of hormone receptors, member of the class B family of seven-transmembrane G protein-coupled receptors; This group represents G protein-coupled receptors for structurally similar peptide hormones that include secretin, growth-hormone-releasing hormone (GHRH), pituitary adenylate cyclase activating polypeptide (PACAP), and vasoactive intestinal peptide (VIP). These receptors are classified into the subfamily B1 of class B GRCRs that consists of the classical hormone receptors and have been identified in all the vertebrates, from fishes to mammals, but are not present in plants, fungi, or prokaryotes. For all class B receptors, the large N-terminal extracellular domain plays a critical role in peptide hormone recognition. Secretin, a polypeptide secreted by entero-endocrine S cells in the small intestine, is involved in maintaining body fluid balance. This polypeptide regulates the secretion of bile and bicarbonate into the duodenum from the pancreatic and biliary ducts, as well as regulates the duodenal pH by the control of gastric acid secretion. Studies with secretin receptor-null mice indicate that secretin plays a role in regulating renal water reabsorption. Secretin mediates its biological actions by elevating intracellular cAMP via G protein-coupled secretin receptors, which are expressed in the brain, pancreas, stomach, kidney, and liver. GHRHR is a specific receptor for the growth hormone-releasing hormone (GHRH) that controls the synthesis and release of growth hormone (GH) from the anterior pituitary somatotrophs. Mutations in the gene encoding GHRHR have been connected to isolated growth hormone deficiency (IGHD), a short-stature condition caused by deficient production of GH or lack of GH action. VIP and PACAP exert their effects through three G protein-coupled receptors, PACAP-R1, VIP-R1 (vasoactive intestinal receptor type 1, also known as VPAC1) and VIP-R2 (or VPAC2). PACAP-R1 binds only PACAP with high affinity, whereas VIP-R1 and -R2 specifically bind and respond to both VIP and PACAP. VIP and PACAP and their receptors are widely expressed in the brain and periphery. They are upregulated in neurons and immune cells in responses to CNS injury and/or inflammation and exert potent anti-inflammatory effects, as well as play important roles in the control of circadian rhythms and stress responses, among many others. All B1 subfamily GPCRs are able to increase intracellular cAMP levels by coupling to adenylate cyclase via a stimulatory Gs protein. However, depending on its cellular location, some members of subfamily B1 are also capable of coupling to additional G proteins such as G(i/o) and/or G(q) proteins, thereby leading to activation of phospholipase C and intracellular calcium influx.


Pssm-ID: 320596 [Multi-domain]  Cd Length: 268  Bit Score: 70.15  E-value: 1.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2546 AASVTALVLTAAVLLSLRSLKSNVRGIHANV-------AAALGVAE-LLFLLG--IHRTHNQLLCTVVAILLHYFFLSTF 2615
Cdd:cd15930    13 SLSLTSLTTAMIILCLFRKLHCTRNYIHMNLfvsfilrAIAVFIKDaVLFSSEdvDHCFVSTVGCKASMVFFQYCVMANF 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2616 AWLLVQGLHLYRMQVEPRNVDRGAMRFYHALGWGVPAVLLGL--AVGLDPEGYGnpdfCW-ISIHEPLIWSFAGPIVLVI 2692
Cdd:cd15930    93 FWLLVEGLYLHTLLVISFFSERRYFWWYVLIGWGAPTVFVTVwiVARLYFEDTG----CWdINDESPYWWIIKGPILISI 168


                  ....*...
gi 564365651 2693 VMNGIMFL 2700
Cdd:cd15930   169 LVNFVLFI 176
7tmB1_GLP2R cd15266
glucagon-like peptide-2 receptor, member of the class B family of seven-transmembrane G ...
 2548-2700 2.01e-12

glucagon-like peptide-2 receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; Glucagon-like peptide-2 receptor (GLP2R) is a member of the glucagon receptor family of G protein-coupled receptors, which also includes glucagon receptor (GCGR) and GLP1R. GLP2R is activated by glucagon-like peptide 2, which is derived from the large proglucagon precursor. Activation of GLP1R stimulates glucose-dependent insulin secretion from pancreatic beta cells, whereas activation of GLP2R stimulates intestinal epithelial proliferation and increases villus height in the small intestine. GCGR regulates blood glucose levels by control of hepatic glycogenolysis and gluconeogenesis and by regulation of insulin secretion from the pancreatic beta-cells. GLP2R belongs to the B1 (or secretin-like) subfamily of class B GPCRs, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on their cellular location, GCGR and GLP receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways.


Pssm-ID: 320394 [Multi-domain]  Cd Length: 280  Bit Score: 70.16  E-value: 2.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2548 SVTALVLTAAVLLSLRSLKSNVRGIHANVAAAL---GVAELLFLLGIHRTH-----------------NQLLCTVVAILL 2607
Cdd:cd15266    15 SLISLSLALLILLLLRKLHCTRNYIHMNLFASFilrALAVLIKDIVLYSTYskrpddetgwisylseeSSTSCRVAQVFM 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2608 HYFFLSTFAWLLVQGLHLYRMQVEPRNVDRGAMRFYHALGWGVPaVLLGLAVGLDPEGYGNPDfCWISIHEPLI-WSFAG 2686
Cdd:cd15266    95 HYFVGANYFWLLVEGLYLHTLLVTAVLSERRLLKKYMLIGWGTP-VLFVVPWGVAKILLENTG-CWGRNENMGIwWIIRG 172

                         170
                  ....*....|....
gi 564365651 2687 PIVLVIVMNGIMFL 2700
Cdd:cd15266   173 PILLCITVNFYIFL 186
7tmB2_GPR125 cd15999
G protein-coupled receptor 125, member of the class B2 family of seven-transmembrane G ...
 2543-2700 8.77e-12

G protein-coupled receptor 125, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR125 is an orphan receptor that has been classified as that belongs to the group III of adhesion GPCRs, which also includes orphan receptors GPR123 and GPR124. GPR125 directly interacts with dishevelled (Dvl) via its intracellular C-terminus, and together, GPR125 and Dvl recruit a subset of planar cell polarity (PCP) components into membrane subdomains, a prerequisite for activation of Wnt/PCP signaling. Thus, GPR125 influences the noncanonical WNT/PCP pathway, which does not involve beta-catenin, through interacting with and modulating the distribution of Dvl. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320665  Cd Length: 312  Bit Score: 68.74  E-value: 8.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2543 VVVAASVTALVLTAAVLLSL----RSLKSNVRGIH--ANVAAALGVAELLFLLGIHRTHNQLLCTVVAILLHYFFLSTFA 2616
Cdd:cd15999     7 VVYATAVVLLLCLLTIIVSYiyhhSLVRISRKSWHmlVNLCFHIFLTCAVFVGGINQTRNASVCQAVGIILHYSTLATVL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2617 WLLVQGLHLYRmQV-----------EPRNVDRGAMRFYhALGWGVPAVLLGLAVGLDPEGYG---NPDFCWISiHEPLIW 2682
Cdd:cd15999    87 WVGVTARNIYK-QVtrkakrcqdpdEPPPPPRPMLRFY-LIGGGIPIIVCGITAAANIKNYGsrpNAPYCWMA-WEPSLG 163

                         170
                  ....*....|....*...
gi 564365651 2683 SFAGPIVLVIVMNGIMFL 2700
Cdd:cd15999   164 AFYGPAGFIIFVNCMYFL 181
7tmB1_CRF-R2 cd15446
corticotropin-releasing factor receptor 2, member of the class B family of seven-transmembrane ...
 2548-2725 1.16e-11

corticotropin-releasing factor receptor 2, member of the class B family of seven-transmembrane G protein-coupled receptors; The vertebrate corticotropin-releasing factor (CRF) receptors are predominantly expressed in central nervous system with high levels in cortex tissue, brain stem, and pituitary. They have two isoforms as a result of alternative splicing of the same receptor gene: CRF-R1 and CRF-R2, which differ in tissue distribution and ligand binding affinities. Recently, a third CRF receptor (CRF-R3) has been identified in catfish pituitary. The catfish CRF-R1 is highly homologous to CRF-R3. CRF is a 41-amino acid neuropeptide that plays a central role in coordinating neuroendocrine, behavioral, and autonomic responses to stress by acting as the primary neuroregulator of the hypothalamic-pituitary-adrenal axis, which controls the levels of cortisol and other stress related hormones. In addition, the CRF family of neuropeptides also includes structurally related peptides such as mammalian urocortin, fish urotensin I, and frog sauvagine. The actions of CRF and CRF-related peptides are mediated through specific binding to CRF-R1 and CRF-R2. CRF and urocortin 1 bind and activate mammalian CRF-R1 with similar high affinities. By contrast, urocortin 2 and urocortin 3 do not bind to CRF-R1 or stimulate CRF-R1-mediated cAMP formation. Urocortin 1 also shows high affinity for mammalian CRF-R2, whereas CRF has significantly lower affinity for this receptor. These evidence suggest that urocortin 1 is an endogenous ligand for CRF-R1 and CRF-R2. The CRF receptors are members of the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, and parathyroid hormone (PTH). These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on its cellular location and function, CRF receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways.


Pssm-ID: 320562 [Multi-domain]  Cd Length: 264  Bit Score: 67.68  E-value: 1.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2548 SVTALVLTAAVLLSLRSLKSNVRGIHANVAAALGVAELL-FLLGI--HRTH--NQLLCTVVAILLHYFFLSTFAWLLVQG 2622
Cdd:cd15446    15 SVGALVVAFLLFLCLRSIRCLRNIIHWNLITTFILRNVMwFLLQMidHNIHesNEVWCRCITTIYNYFVVTNFFWMFVEG 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2623 LHLYRMQVEPRNVDRGAMRFYHALGWGVPA-VLLGLAVGldpEGYGNPDFCWISiHEP---LIWSFAGPIVLVIVMNGIM 2698
Cdd:cd15446    95 CYLHTAIVMTYSTDKLRKWVFLFIGWCIPCpIIVAWAIG---KLYYENEQCWFG-KEPgkyIDYIYQGPVILVLLINFVF 170

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 564365651 2699 F----------LLAARTSCSTGQREAKKTSVLVLPRL 2725
Cdd:cd15446   171 LfnivrilmtkLRASTTSETIQYRKAVKATLVLLPLL 207
7tmB2_GPR64 cd15444
orphan adhesion receptor GPR64 and related proteins, member of subfamily B2 of the class B ...
 2599-2707 3.75e-11

orphan adhesion receptor GPR64 and related proteins, member of subfamily B2 of the class B secretin-like receptors of seven-transmembrane G protein-coupled receptors; GPR64 is an orphan receptor that has been classified as that belongs to the Group VIII of adhesion GPCRs. Other members of the Group VII include orphan GPCRs such as GPR56, GPR97, GPR112, GPR114, and GPR126. GPR64 is mainly expressed in the epididymis of male reproductive tract, and targeted deletion of GPR64 causes sperm stasis and efferent duct blockage due to abnormal fluid reabsorption, resulting in male infertility. GPR64 is also over-expressed in Ewing's sarcoma (ES), as well as upregulated in other carcinomas from kidney, prostate or lung, and promotes invasiveness and metastasis in ES via the upregulation of placental growth factor (PGF) and matrix metalloproteinase (MMP) 1. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320560 [Multi-domain]  Cd Length: 271  Bit Score: 66.39  E-value: 3.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2599 LCTVVAILLHYFFLSTFAWLLVQGLHLYRMQVEPRN--VDRGAMRFYhALGWGVPAVLLGLAVGLDPEGYG--------- 2667
Cdd:cd15444    70 LCISVAVFLHYFLLVSFTWMGLEAFHMYLALVKVFNtyIRKYILKFC-IVGWGVPAVVVAIVLAVSKDNYGlgsygkspn 148

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 564365651 2668 --NPDFCWISIHEPLIWSFAGPIVLVIVMNGIMFLLAARTSC 2707
Cdd:cd15444   149 gsTDDFCWINNNIVFYITVVGYFCVIFLLNISMFIVVLVQLC 190
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 2067-2105 8.76e-11

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 59.29  E-value: 8.76e-11
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 564365651 2067 PCDCYPVGSTSRSCAPHSGQCPCRPGALGRQCNSCDSPF 2105
Cdd:cd00055     1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGY 39
7tmB1_CRF-R1 cd15445
corticotropin-releasing factor receptor 1, member of the class B family of seven-transmembrane ...
 2548-2725 9.64e-11

corticotropin-releasing factor receptor 1, member of the class B family of seven-transmembrane G protein-coupled receptors; The vertebrate corticotropin-releasing factor (CRF) receptors are predominantly expressed in central nervous system with high levels in cortex tissue, brain stem, and pituitary. They have two isoforms as a result of alternative splicing of the same receptor gene: CRF-R1 and CRF-R2, which differ in tissue distribution and ligand binding affinities. Recently, a third CRF receptor (CRF-R3) has been identified in catfish pituitary. The catfish CRF-R1 is highly homologous to CRF-R3. CRF is a 41-amino acid neuropeptide that plays a central role in coordinating neuroendocrine, behavioral, and autonomic responses to stress by acting as the primary neuroregulator of the hypothalamic-pituitary-adrenal axis, which controls the levels of cortisol and other stress related hormones. In addition, the CRF family of neuropeptides also includes structurally related peptides such as mammalian urocortin, fish urotensin I, and frog sauvagine. The actions of CRF and CRF-related peptides are mediated through specific binding to CRF-R1 and CRF-R2. CRF and urocortin 1 bind and activate mammalian CRF-R1 with similar high affinities. By contrast, urocortin 2 and urocortin 3 do not bind to CRF-R1 or stimulate CRF-R1-mediated cAMP formation. Urocortin 1 also shows high affinity for mammalian CRF-R2, whereas CRF has significantly lower affinity for this receptor. These evidence suggest that urocortin 1 is an endogenous ligand for CRF-R1 and CRF-R2. The CRF receptors are members of the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, and parathyroid hormone (PTH). These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on its cellular location and function, CRF receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways.


Pssm-ID: 320561 [Multi-domain]  Cd Length: 265  Bit Score: 64.96  E-value: 9.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2548 SVTALVLTAAVLLSLRSLKSNVRGIHANVAAAL-------GVAELLFLLGIHRThNQLLCTVVAILLHYFFLSTFAWLLV 2620
Cdd:cd15445    15 SLVALLVAFVLFLRLRSIRCLRNIIHWNLITAFilrnatwFVVQLTMSPEVHQS-NVVWCRLVTAAYNYFHVTNFFWMFG 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2621 QGLHLYRMQVEPRNVDRGAMRFYHALGWGVP-AVLLGLAVGldpEGYGNPDFCWISiHEPLIWS---FAGPIVLVIVMNG 2696
Cdd:cd15445    94 EGCYLHTAIVLTYSTDKLRKWMFICIGWCIPfPIIVAWAIG---KLYYDNEKCWFG-KRAGVYTdyiYQGPMILVLLINF 169

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 564365651 2697 I---------MFLLAARTSCSTGQ-REAKKTSVLVLPRL 2725
Cdd:cd15445   170 IflfnivrilMTKLRASTTSETIQyRKAVKATLVLLPLL 208
7tmB1_secretin cd15275
secretin receptor, member of the class B family of seven-transmembrane G protein-coupled ...
 2546-2700 9.74e-11

secretin receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; Secretin receptor is a member of the group of G protein-coupled receptors for structurally similar peptide hormones that also include vasoactive intestinal peptide (VIP), growth-hormone-releasing hormone (GHRH), and pituitary adenylate cyclase activating polypeptide (PACAP). These receptors are classified into the subfamily B1 of class B GRCRs that consists of the classical hormone receptors, and have been identified in all the vertebrates, from fishes to mammals, but are not present in plants, fungi, or prokaryotes. For all class B receptors, the large N-terminal extracellular domain plays a critical role in peptide hormone recognition. Secretin, a polypeptide secreted by entero-endocrine S cells in the small intestine, is involved in maintaining body fluid balance. This polypeptide regulates the secretion of bile and bicarbonate into the duodenum from the pancreatic and biliary ducts, as well as regulates the duodenal pH by the control of gastric acid secretion. Studies with secretin receptor-null mice indicate that secretin plays a role in regulating renal water reabsorption. Secretin mediates its biological actions by elevating intracellular cAMP via G protein-coupled secretin receptor, which is expressed in the brain, pancreas, stomach, kidney, and liver.


Pssm-ID: 320403 [Multi-domain]  Cd Length: 271  Bit Score: 65.15  E-value: 9.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2546 AASVTALVLTAAVLLSLRSLKSNVRGIHANV--------------AAALGVAELLFLLGIHRTHnqllCTVVAILLHYFF 2611
Cdd:cd15275    13 SVSLVSLAIALAILCSFRRLHCTRNYIHMQLflsfilraisifikDAVLFSSEDDNHCDIYTVG----CKVAMVFSNYCI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2612 LSTFAWLLVQGLHLYRMQVEPRNVDRGAMRFYHALGWGVPAVLL---GLAVGL-DPEGygnpdfCW-ISIHEPLIWSFAG 2686
Cdd:cd15275    89 MANYSWLLVEGLYLHSLLSISFFSERKHLWWYIALGWGSPLIFIiswAIARYLhENEG------CWdTRRNAWIWWIIRG 162

                         170
                  ....*....|....
gi 564365651 2687 PIVLVIVMNGIMFL 2700
Cdd:cd15275   163 PVILSIFVNFILFL 176
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
2068-2113 1.10e-10

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 58.86  E-value: 1.10e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 564365651   2068 CDCYPVGSTSRSCAPHSGQCPCRPGALGRQCNSCDSPFAEVTASGC 2113
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
7tmB1_GHRHR cd15270
growth-hormone-releasing hormone receptor, member of the class B family of seven-transmembrane ...
 2546-2700 2.46e-10

growth-hormone-releasing hormone receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; Growth hormone-releasing hormone receptor (GHRHR) is a member of the group of G protein-coupled receptors for structurally similar peptide hormones that also include secretin, pituitary adenylate cyclase activating polypeptide (PACAP), and vasoactive intestinal peptide. These receptors are classified into the subfamily B1 of class B GRCRs that consists of the classical hormone receptors and have been identified in all the vertebrates, from fishes to mammals, but are not present in plants, fungi, or prokaryotes. For all class B receptors, the large N-terminal extracellular domain plays a critical role in peptide hormone recognition. GHRHR is a specific receptor for the growth hormone-releasing hormone (GHRH) that controls the synthesis and release of growth hormone (GH) from the anterior pituitary somatotrophs. Mutations in the gene encoding GHRHR have been connected to isolated growth hormone deficiency (IGHD), a short-stature condition caused by deficient production of GH or lack of GH action. GHRH is preferentially coupled to a stimulatory G(s) protein, which leads to the activation of adenylate cyclase and thereby increases in intracellular cAMP level. GHRHR is found in mammals as well as zebrafish and chicken, whereas the GHRHR type 2, an ortholog of the GHRHR, has only been identified in ray-finned fish, chicken and Xenopus. Xenopus laevis GHRHR2 has been shown to interact with both endogenous GHRH and PACAP-related peptide (PRP).


Pssm-ID: 320398 [Multi-domain]  Cd Length: 268  Bit Score: 63.66  E-value: 2.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2546 AASVTALVLTAAVLLSLRSLKSNVRGIHANV-------AAALGVAELLFLLGIHRTHNQL---LCTVVAILLHYFFLSTF 2615
Cdd:cd15270    13 SISIVSLCVAVAILVAFRRLHCPRNYIHIQLfftfilkAIAVFIKDAALFQEDDTDHCSMstvLCKVSVVFCHYCVMTNF 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2616 AWLLVQGLHLYRMQVEPRNVDRGAMRFYHALGWGVPAVLLGLAVGldPEGYGNPDFCW-ISIHEPLIWSFAGPIVLVIVM 2694
Cdd:cd15270    93 FWLLVEAVYLNCLLASSFPRGKRYFWWLVLLGWGLPTLCTGTWIL--CKLYFEDTECWdINNDSPYWWIIKGPIVISVGV 170


                  ....*.
gi 564365651 2695 NGIMFL 2700
Cdd:cd15270   171 NFLLFL 176
7tmB1_GHRHR2 cd15271
growth-hormone-releasing hormone receptor type 2, member of the class B family of ...
 2542-2705 3.45e-10

growth-hormone-releasing hormone receptor type 2, member of the class B family of seven-transmembrane G protein-coupled receptors; Growth hormone-releasing hormone receptor type 2 (GHRHR2) is found in non-mammalian vertebrates such as chicken and frog. It is a member of the group of G protein-coupled receptors for structurally similar peptide hormones that also include secretin, pituitary adenylate cyclase activating polypeptide (PACAP), vasoactive intestinal peptide, and mammalian growth hormone-releasing hormone. These receptors are classified into the subfamily B1 of class B GRCRs that consists of the classical hormone receptors and have been identified in all the vertebrates, from fishes to mammals, but are not present in plants, fungi, or prokaryotes. For all class B receptors, the large N-terminal extracellular domain plays a critical role in peptide hormone recognition. Mammalian GHRHR is a specific receptor for the growth hormone-releasing hormone (GHRH) that controls the synthesis and release of growth hormone (GH) from the anterior pituitary somatotrophs. Mutations in the gene encoding GHRHR have been connected to isolated growth hormone deficiency (IGHD), a short-stature condition caused by deficient production of GH or lack of GH action. Mammalian GHRH is preferentially coupled to a stimulatory G(s) protein, which leads to the activation of adenylate cyclase and thereby increases in intracellular cAMP level. GHRHR is found in mammals as well as zebrafish and chicken, whereas the GHRHR type 2, an ortholog of the GHRHR, has only been identified in ray-finned fish, chicken and Xenopus. Xenopus laevis GHRHR2 has been shown to interact with both endogenous GHRH and PACAP-related peptide (PRP).


Pssm-ID: 320399 [Multi-domain]  Cd Length: 267  Bit Score: 63.21  E-value: 3.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2542 HVVVAASVTALVLTAAVLLSLRSLKSNVRGIHANV-------AAALGVAE-LLFLLGI--HRTHNQLLCTVVAILLHYFF 2611
Cdd:cd15271     9 TVGYGTSLTSLITAVLIFCTFRKLHCTRNYIHINLfvsfilrALAVFIKDaVLFADESvdHCTMSTVACKAAVTFFQFCV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2612 LSTFAWLLVQGLHLYRMQVEPRNVDRGAMRFYHALGWGVPAVLLGLAVGL----DPEGygnpdfCWISIHEPLIWSFAGP 2687
Cdd:cd15271    89 LANFFWLLVEGMYLQTLLLLTFTSDRKYFWWYILIGWGAPSVTVTVWVLTrlqyDNRG------CWDDLESRIWWIIKTP 162

                         170
                  ....*....|....*...
gi 564365651 2688 IVLVIVMNGIMFLLAART 2705
Cdd:cd15271   163 ILLSVFVNFLIFINVIRI 180
7tmB2_GPR111_115 cd15994
orphan adhesion receptors GPR111 and GPR115, member of the class B2 family of ...
 2575-2725 5.36e-10

orphan adhesion receptors GPR111 and GPR115, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR111 and GPR115 are highly homologous orphan receptors that belong to group VI adhesion-GPCRs along with GPR110, GPR113, and GPR116. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS. Both GPR111 and GPR5 are present only in land-living animals and are predominantly expressed in the developing skin.


Pssm-ID: 320660 [Multi-domain]  Cd Length: 267  Bit Score: 62.93  E-value: 5.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2575 NVAAALGVAELLFLLGIH---RTHNQLLCTVVAILLHYFFLSTFAWLLVQGLH-LYRMQVEPRNVDRGAM-RFYHALGWG 2649
Cdd:cd15994    48 NIATSLLIADVWFILASIvhnTALNYPLCVAATFFLHFFYLSLFFWMLTKALLiLYGILLVFFKITKSVFiATAFSIGYG 127

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564365651 2650 VPAVLLGLAVGL-DPE-GYGNPDFCWISIHE-PLIWSFAGPIVLVIVMNGIMFLLAARTSCSTGQREAKKTSVLVLPRL 2725
Cdd:cd15994   128 CPLVIAVLTVAItEPKkGYLRPEACWLNWDEtKALLAFIIPALSIVVVNLIVVGVVVVKTQRSSIGESCKQDVSNIIRI 206
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 1176-1257 1.02e-09

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637 [Multi-domain]  Cd Length: 98  Bit Score: 57.71  E-value: 1.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 1176 DTFPSGIIGRIPAYDPDVSD--HLFYSFERGNELQLLVVNQTSGELRLSRKLDNNRPLVASMLVTVTD-GLHSVTAQCVL 1252
Cdd:cd11304     9 NAPPGTVVLTVSATDPDSGEngEVTYSIVSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDgGGPPLSSTATV 88


                  ....*
gi 564365651 1253 RVVII 1257
Cdd:cd11304    89 TITVL 93
7tmB1_PACAP-R1 cd15987
pituitary adenylate cyclase-activating polypeptide type 1 receptor, member of the class B ...
 2534-2700 2.31e-09

pituitary adenylate cyclase-activating polypeptide type 1 receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; Pituitary adenylate cyclase-activating polypeptide type 1 receptor (PACAP-R1) is a member of the group of G protein-coupled receptors for structurally similar peptide hormones that also include secretin, growth-hormone-releasing hormone (GHRH), and vasoactive intestinal peptide (VIP). These receptors are classified into the subfamily B1 of class B GRCRs that consists of the classical hormone receptors and have been identified in all the vertebrates, from fishes to mammals, but are not present in plants, fungi, or prokaryotes. For all class B receptors, the large N-terminal extracellular domain plays a critical role in peptide hormone recognition. VIP and PACAP exert their effects through three G protein-coupled receptors, PACAP-R1, VIP-R1 (vasoactive intestinal receptor type 1, also known as VPAC1) and VIP-R2 (or VPAC2). PACAP-R1 binds only PACAP with high affinity, whereas VIP-R1 and -R2 specifically bind and respond to both VIP and PACAP. VIP and PACAP and their receptors are widely expressed in the brain and periphery. They are upregulated in neurons and immune cells in responses to CNS injury and/or inflammation and exert potent anti-inflammatory effects, as well as play important roles in the control of circadian rhythms and stress responses, among many others. PACAP-R1 is preferentially coupled to a stimulatory G(s) protein, which leads to the activation of adenylate cyclase and thereby increases in intracellular cAMP level.


Pssm-ID: 320653 [Multi-domain]  Cd Length: 268  Bit Score: 60.75  E-value: 2.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2534 LELLAVFThVVVAASVTALVLTAAVLLSLRSLKSNVRGIHANVAAALGVAELLFLL----------GIHRTHNQLLCTVV 2603
Cdd:cd15987     2 LSVKALYT-VGYSTSLVSLTTAMVILCRFRKLHCTRNFIHMNLFVSFILRAISVFIkdgvlyaeqdSDHCFVSTVECKAV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2604 AILLHYFFLSTFAWLLVQGLHLYRMQVEPRNVDRGAMRFYHALGWGVPAVLLGLAVGLdpEGYGNPDFCW-ISIHEPLIW 2682
Cdd:cd15987    81 MVFFHYCVMSNYFWLFIEGLYLFTLLVETFFPERRYFYWYTIIGWGTPTICVTVWAVL--RLHFDDTGCWdMNDNTALWW 158

                         170
                  ....*....|....*...
gi 564365651 2683 SFAGPIVLVIVMNGIMFL 2700
Cdd:cd15987   159 VIKGPVVGSIMINFVLFI 176
CA_like cd00031
Cadherin repeat-like domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 957-1054 2.56e-09

Cadherin repeat-like domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers. This family also includes the cadherin-like repeats of extracellular alpha-dystroglycan.


Pssm-ID: 206635  Cd Length: 98  Bit Score: 56.58  E-value: 2.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  957 YTGLVSEDAPPFtsVLQIsATDRDAHANGRVQYTFQNGEDGDGDFTIEPTSGIVRTVRRLDREAVPVYELTAYAVDRGVP 1036
Cdd:cd00031     4 GSAVEGRSRGSF--RVSI-PTDLIASSGEIIKISAAGKEALPSWLHWEPHSGILEGLEKLDREDKGVHYISVSAASLGAN 80

                          90
                  ....*....|....*...
gi 564365651 1037 PLRTPVSIQVTVQDVNDN 1054
Cdd:cd00031    81 VPQTSSVFSIEVYDENDN 98
7tmB1_PDFR cd15261
The pigment dispersing factor receptor, member of the class B seven-transmembrane G ...
 2548-2725 2.65e-09

The pigment dispersing factor receptor, member of the class B seven-transmembrane G protein-coupled receptors; The pigment dispersing factor receptor (PDFR) is a G protein-coupled receptor that binds the circadian clock neuropeptide PDF, a functional ortholog of the mammalian vasoactive intestinal peptide (VIP), on the pacemaker neurons. The PDFR is implicated in regulating flight circuit development and in modulating acute flight In Drosophila melanogaster. The PDFR activation stimulates adenylate cyclase, thereby increasing cAMP levels in many different pacemakers, and the receptor signaling has been shown to regulate behavioral circadian rhythms and geotaxis in Drosophila. The PDFR belongs to the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. . These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. They play key roles in hormone homeostasis in mammals and are promising drug targets in various human diseases including diabetes, osteoporosis, obesity, neurodegenerative conditions (Alzheimer###s and Parkinson's), cardiovascular disease, migraine, and psychiatric disorders (anxiety, depression).


Pssm-ID: 320389 [Multi-domain]  Cd Length: 282  Bit Score: 60.84  E-value: 2.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2548 SVTALVLTAAVLLSLRSLKSNVRGIHANVAAALGVAELLFL-----------------------LGIHRThnQLLCTVVA 2604
Cdd:cd15261    15 SLVSLIISLFIFSYFRTLRNHRTRIHKNLFLAILLQVIIRLvlyidqaitrsrgshtnaattegRTINST--PILCEGFY 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2605 ILLHYFFLSTFAWLLVQGLHLYRMQVEprNVDRGA--MRFYHALGWGVPAVLLGLAVGLDPEGYGNPDfCWISIH-EPLI 2681
Cdd:cd15261    93 VLLEYAKTVMFMWMFIEGLYLHNIIVV--SVFSGKpnYLFYYILGWGIPIVHTSAWAIVTLIKMKVNR-CWFGYYlTPYY 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 564365651 2682 WSFAGPIVLVIVMNgIMFLL-----------AARTSCSTGQREAKKTSVLVLPRL 2725
Cdd:cd15261   170 WILEGPRLAVILIN-LFFLLniirvlvsklrESHSREIEQVRKAVKAAIVLLPLL 223
7tmB1_GLP1R cd15268
glucagon-like peptide-1 receptor, member of the class B family of seven-transmembrane G ...
 2534-2721 2.76e-09

glucagon-like peptide-1 receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; Glucagon-like peptide-1 receptor (GLP1R) is a member of the glucagon receptor family of G protein-coupled receptors, which also includes glucagon receptor and GLP2R. GLP1R is activated by glucagon-like peptide 1 (GLP1), which is derived from the large proglucagon precursor. Activation of GLP1R stimulates glucose-dependent insulin secretion from pancreatic beta cells, whereas activation of GLP2R stimulates intestinal epithelial proliferation and increases villus height in the small intestine. GCGR regulates blood glucose levels by control of hepatic glycogenolysis and gluconeogenesis and by regulation of insulin secretion from the pancreatic beta-cells. Receptors in this group belong to the B1 (or secretin-like) subfamily of class B GPCRs, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on their cellular location, GCGR and GLP receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways.


Pssm-ID: 341342 [Multi-domain]  Cd Length: 279  Bit Score: 60.74  E-value: 2.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2534 LELLAVFThVVVAASVTALVLTAAVLLSLRSLKSNVRGIHANVAAALGVAELLFLL-------------------GIHRT 2594
Cdd:cd15268     2 LFLYIIYT-VGYALSFSALVIASAILLGFRHLHCTRNYIHLNLFASFILRALSVFIkdaalkwmystaaqqhqwdGLLSY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2595 HNQLLCTVVAILLHYFFLSTFAWLLVQGLHLYRMQVEPRNVDRGAMRFYHALGWGVP---AVLLGLAVGL-DPEGygnpd 2670
Cdd:cd15268    81 QDSLSCRLVFLLMQYCVAANYYWLLVEGVYLYTLLAFSVFSEQRIFRLYLSIGWGVPllfVIPWGIVKYLyEDEG----- 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564365651 2671 fCWISIHEPLIWSFAG-PIVLVIVMNGIMFL---------LAARTSCST--GQREAKKTSVLV 2721
Cdd:cd15268   156 -CWTRNSNMNYWLIIRlPILFAIGVNFLIFIrvicivvskLKANLMCKTdiKCRLAKSTLTLI 217
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 2068-2101 3.13e-09

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 54.67  E-value: 3.13e-09
                           10        20        30
                   ....*....|....*....|....*....|....
gi 564365651  2068 CDCYPVGSTSRSCAPHSGQCPCRPGALGRQCNSC 2101
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRC 34
GPS pfam01825
GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for ...
 2476-2521 5.90e-09

GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for auto-proteolysis, so is thus named, GPS. The GPS motif is a conserved sequence of ~40 amino acids containing canonical cysteine and tryptophan residues, and is the most highly conserved part of the domain. In most, if not all, cell-adhesion GPCRs these undergo autoproteolysis in the GPS between a conserved aliphatic residue (usually a leucine) and a threonine, serine, or cysteine residue. In higher eukaryotes this motif is found embedded in the C-terminal beta-stranded part of a GAIN domain - GPCR-Autoproteolysis INducing (GAIN). The GAIN-GPS domain adopts a fold in which the GPS motif, at the C-terminus, forms five beta-strands that are tightly integrated into the overall GAIN domain. The GPS motif, evolutionarily conserved from tetrahymena to mammals, is the only extracellular domain shared by all human cell-adhesion GPCRs and PKD proteins, and is the locus of multiple human disease mutations. The GAIN-GPS domain is both necessary and sufficient functionally for autoproteolysis, suggesting an autoproteolytic mechanism whereby the overall GAIN domain fine-tunes the chemical environment in the GPS to catalyze peptide bond hydrolysis. In the cell-adhesion GPCRs and PKD proteins, the GPS motif is always located at the end of their long N-terminal extracellular regions, immediately before the first transmembrane helix of the respective protein.


Pssm-ID: 460350  Cd Length: 44  Bit Score: 53.85  E-value: 5.90e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 564365651  2476 AICVQWDPPGpaDQHGMWTARDCELVHRNGSHARCRCSRTGTFGVL 2521
Cdd:pfam01825    1 PQCVFWDFTN--STTGRWSTEGCTTVSLNDTHTVCSCNHLTSFAVL 44
7tmB1_GCGR cd15267
glucagon receptor, member of the class B family of seven-transmembrane G protein-coupled ...
 2548-2700 6.18e-09

glucagon receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; Glucagon receptor (GCGR) is a member of the glucagon receptor family of G protein-coupled receptors, which also includes glucagon-like peptide-1 receptor (GLP1R) and GLP2R. GCGR is activated by glucagon, which is derived from the large proglucagon precursor. GCGR regulates blood glucose levels by control of hepatic glycogenolysis and gluconeogenesis and by regulation of insulin secretion from the pancreatic beta-cells. Activation of GLP1R stimulates glucose-dependent insulin secretion from pancreatic beta cells, whereas activation of GLP2R stimulates intestinal epithelial proliferation and increases villus height in the small intestine. GCGR belongs to the B1 (or secretin-like) subfamily of class B GPCRs, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on their cellular location, GCGR and GLP receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways.


Pssm-ID: 320395 [Multi-domain]  Cd Length: 281  Bit Score: 59.83  E-value: 6.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2548 SVTALVLTAAVLLSLRSLKSNVRGIHANVAAALGVAELLFLL--GIHRTHNQ-----------------LLCTVVAILLH 2608
Cdd:cd15267    17 SLGALLLALAILGGFSKLHCMRNAIHMNLFASFILKASSVLVidGLLRTRYSqkieddlsstwlsdeavAGCRVAAVFMQ 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2609 YFFLSTFAWLLVQGLHLYRMQVEPRNVDRGAMRFYHALGWGVPAVLLGLAVGLDpEGYGNPDfCWISIHEPLI-WSFAGP 2687
Cdd:cd15267    97 YGIVANYCWLLVEGIYLHNLLVLAVFPERSYFSLYLCIGWGAPALFVVPWVVVK-CLYENVQ-CWTSNDNMGFwWILRFP 174

                         170
                  ....*....|...
gi 564365651 2688 IVLVIVMNGIMFL 2700
Cdd:cd15267   175 VFLAILINFFIFV 187
7tmB1_VIP-R1 cd15269
vasoactive intestinal polypeptide (VIP) receptor 1, member of the class B family of ...
 2538-2704 6.91e-09

vasoactive intestinal polypeptide (VIP) receptor 1, member of the class B family of seven-transmembrane G protein-coupled receptors; Vasoactive intestinal peptide (VIP) receptor 1 is a member of the group of G protein-coupled receptors for structurally similar peptide hormones that also include secretin, growth-hormone-releasing hormone (GHRH), and pituitary adenylate cyclase activating polypeptide (PACAP). These receptors are classified into the subfamily B1 of class B GRCRs that consists of the classical hormone receptors and have been identified in all the vertebrates, from fishes to mammals, but are not present in plants, fungi, or prokaryotes. For all class B receptors, the large N-terminal extracellular domain plays a critical role in peptide hormone recognition. VIP and PACAP exert their effects through three G protein-coupled receptors, PACAP-R1, VIP-R1 (vasoactive intestinal receptor type 1, also known as VPAC1) and VIP-R2 (or VPAC2). PACAP-R1 binds only PACAP with high affinity, whereas VIP-R1 and -R2 specifically bind and respond to both VIP and PACAP. VIP and PACAP and their receptors are widely expressed in the brain and periphery. They are upregulated in neurons and immune cells in responses to CNS injury and/or inflammation and exert potent anti-inflammatory effects, as well as play important roles in the control of circadian rhythms and stress responses, among many others. VIP-R1 is preferentially coupled to a stimulatory G(s) protein, which leads to the activation of adenylate cyclase and thereby increases in intracellular cAMP level. However, depending on its cellular location, VIP-R1 is also capable of coupling to additional G proteins such as G(q) protein, thus leading to the activation of phospholipase C and intracellular calcium influx.


Pssm-ID: 320397 [Multi-domain]  Cd Length: 268  Bit Score: 59.48  E-value: 6.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2538 AVFTHVVVAASVTALVLTAA-VLLSL-RSLKSNVRGIHANV-------AAALGVAELLFLLGIHRTH---NQLLCTVVAI 2605
Cdd:cd15269     3 TVKTGYTIGHSLSLISLTAAmIILCLfRKLHCTRNYIHMHLfmsfilrAIAVFIKDAVLFESGEEDHcsvASVGCKAAMV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2606 LLHYFFLSTFAWLLVQGLHLYRMQVEPRNVDRGAMRFYHALGWGVPAVLlgLAVGLDPEGYGNPDFCW-ISIHEPLIWSF 2684
Cdd:cd15269    83 FFQYCIMANFFWLLVEGLYLHTLLAVSFFSERKYFWWYILIGWGAPSVF--ITAWSVARIYFEDVGCWdTIIESLLWWII 160

                         170       180
                  ....*....|....*....|
gi 564365651 2685 AGPIVLVIVMNGIMFLLAAR 2704
Cdd:cd15269   161 KTPILVSILVNFILFICIIR 180
7tmB2_GPR124 cd15998
G protein-coupled receptor 124, member of the class B2 family of seven-transmembrane G ...
 2575-2702 1.76e-08

G protein-coupled receptor 124, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR124 is an orphan receptor that has been classified as that belongs to the group III of adhesion GPCRs, which also includes orphan GPR123 and GPR125. GPR124, also known as tumor endothelial marker 5 (TEM5), is highly expressed in tumor vessels and in the vasculature of the developing embryo. GPR124 is essentially required for proper angiogenic sprouting into neural tissue, CNS-specific vascularization, and formation of the blood-brain barrier. GPR124 interacts with the PDZ domain of DLG1 (discs large homolog 1) through its PDZ-binding motif. Recently, studies of double-knockout mice showed that GPR124 functions as a co-activator of Wnt7a/Wnt7b-dependent beta-catenin signaling in brain endothelium. Moreover, WNT7-stimulated beta-catenin signaling is regulated by GPR124's intracellular PDZ binding motif and leucine-rich repeats (LRR) in its N-terminal extracellular domain. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320664 [Multi-domain]  Cd Length: 268  Bit Score: 58.43  E-value: 1.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2575 NVAAALGVAELLFLLGIHRTHNQLLCTVVAILLHYFFLSTFAWLLVQGLHLYR----MQVEPRNVD------RGAMRFYH 2644
Cdd:cd15998    45 NLCFHIAMTSAVFAGGITLTNYQMVCQAVGITLHYSSLSTLLWMGVKARVLHKeltwRAPPPQEGDpalptpRPMLRFYL 124

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 564365651 2645 ALGwGVPAVLLGLAVGLDPEGY-GNPDFCWIsIHEPLIWSFAGPIVLVIVMNGIMFLLA 2702
Cdd:cd15998   125 IAG-GIPLIICGITAAVNIHNYrDHSPYCWL-VWRPSLGAFYIPVALILLVTWIYFLCA 181
7tmB2_GPR97 cd15442
orphan adhesion receptor GPR97, member of the class B2 family of seven-transmembrane G ...
 2543-2674 3.52e-08

orphan adhesion receptor GPR97, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR97 is an orphan receptor that has been classified into the group VIII of adhesion GPCRs. Other members of the Group VII include GPR56, GPR64, GPR112, GPR114, and GPR126. GPR97 is identified as a lymphatic adhesion receptor that is specifically expressed in lymphatic endothelium, but not in blood vascular endothelium, and is shown to regulate migration of lymphatic endothelial cells via the small GTPases RhoA and cdc42. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320558 [Multi-domain]  Cd Length: 277  Bit Score: 57.50  E-value: 3.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2543 VVVAASVTALVLTAAVLLSLRSLKS-NVRGIHANVAAALGVAELLFLL--GIHRTHNQLLCTVVAILLHYFFLSTFAWLL 2619
Cdd:cd15442    14 VSMVFLIFTIILYFFLRFTYQKFKSeDAPKIHVNLSSSLLLLNLAFLLnsGVSSRAHPGLCKALGGVTHYFLLCCFTWMA 93

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564365651 2620 VQGLHLYRMQVEPRNVdrgAMRFYHA----LGWGVPAVLLGLAVGLDPEG-YGNPD--------FCWI 2674
Cdd:cd15442    94 IEAFHLYLLAIKVFNT---YIHHYFAklclVGWGFPALVVTITGSINSYGaYTIMDmanrttlhLCWI 158
7tm_GPCRs cd14964
seven-transmembrane G protein-coupled receptor superfamily; This hierarchical evolutionary ...
 2543-2705 3.85e-08

seven-transmembrane G protein-coupled receptor superfamily; This hierarchical evolutionary model represents the seven-transmembrane (7TM) receptors, often referred to as G protein-coupled receptors (GPCRs), which transmit physiological signals from the outside of the cell to the inside via G proteins. GPCRs constitute the largest known superfamily of transmembrane receptors across the three kingdoms of life that respond to a wide variety of extracellular stimuli including peptides, lipids, neurotransmitters, amino acids, hormones, and sensory stimuli such as light, smell and taste. All GPCRs share a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes. However, some 7TM receptors, such as the type 1 microbial rhodopsins, do not activate G proteins. Based on sequence similarity, GPCRs can be divided into six major classes: class A (the rhodopsin-like family), class B (the Methuselah-like, adhesion and secretin-like receptor family), class C (the metabotropic glutamate receptor family), class D (the fungal mating pheromone receptors), class E (the cAMP receptor family), and class F (the frizzled/smoothened receptor family). Nearly 800 human GPCR genes have been identified and are involved essentially in all major physiological processes. Approximately 40% of clinically marketed drugs mediate their effects through modulation of GPCR function for the treatment of a variety of human diseases including bacterial infections.


Pssm-ID: 410628 [Multi-domain]  Cd Length: 267  Bit Score: 57.05  E-value: 3.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2543 VVVAASVTALVLTAAVLLSLRSLKSNVRGIHANVAAALGVAELLFLLGI-------HRTHNQLLCTVVAILLHYFFLSTF 2615
Cdd:cd14964     7 LLTCLGLLGNLLVLLSLVRLRKRPRSTRLLLASLAACDLLASLVVLVLFfllglteASSRPQALCYLIYLLWYGANLASI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2616 AWLLVQGLHLYRMQVEPRNVDR----GAMRFYHALGWGVPAVL-LGLAVGLDPEG---YGNPDFCWISIHEPLIWSF-AG 2686
Cdd:cd14964    87 WTTLVLTYHRYFALCGPLKYTRlsspGKTRVIILGCWGVSLLLsIPPLVGKGAIPrynTLTGSCYLICTTIYLTWGFlLV 166

                         170
                  ....*....|....*....
gi 564365651 2687 PIVLVIVMNGIMFLLAART 2705
Cdd:cd14964   167 SFLLPLVAFLVIFSRIVLR 185
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1717-1748 5.40e-08

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 50.71  E-value: 5.40e-08
                          10        20        30
                  ....*....|....*....|....*....|...
gi 564365651 1717 CASG-PCKNGGLCSERWGGFSCDCPVGFGGKDC 1748
Cdd:cd00054     5 CASGnPCQNGGTCVNTVGSYRCSCPPGYTGRNC 37
7tmB1_PTHR cd15265
parathyroid hormone receptors, member of the class B family of seven-transmembrane G ...
 2600-2700 6.42e-08

parathyroid hormone receptors, member of the class B family of seven-transmembrane G protein-coupled receptors; The parathyroid hormone (PTH) receptor family has three subtypes: PTH1R, PTH2R and PTH3R. PTH1R is expressed in bone and kidney and is activated by two polypeptide ligands: PTH, an endocrine hormone that regulates calcium homoeostasis and bone maintenance, and PTH-related peptide (PTHrP), a paracrine factor that regulates endochondral bone development. PTH1R couples predominantly to a G(s)-protein that in turn activates adenylate cyclase thereby producing cAMP, but it can also couple to several G protein subtypes, including G(q/11), G(i/o), and G(12/13), resulting in activation of multiple intracellular signaling pathways. PTH2R is potently activated by tuberoinfundibular peptide-39 (TIP-39), but not by PTHrP. PTH also strongly activates human PTH2R, but only weakly activates rat and zebrafish PTH2Rs, suggesting that TIP-39 is a natural ligand for PTH2R. On the other hand, PTH3R binds and responds to both PTH and PTHrP, but not the TIP-39. Moreover, the PTH3R is more closely related to the PTH1R than PTH2R. PTH1R is found in all vertebrate species, whereas PTH2R is found in mammals and fish, but not in chicken or frog. The PTH3R is found in chicken and fish, but it is absent in mammals. The PTH receptors are members of the B1 (or secretin-like) subfamily of class B GPCRs, which include receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), and calcitonin gene-related peptide. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways.


Pssm-ID: 320393 [Multi-domain]  Cd Length: 289  Bit Score: 56.61  E-value: 6.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2600 CTVVAILLHYFFLSTFAWLLVQGLHLYRMQVEPRNVDRGAMRFYHALGWGVPAVLLGL-----AVGLDPEgygnpdfCWI 2674
Cdd:cd15265    95 CKVAVTLFLYFLATNYYWILVEGLYLHSLIFMAFFSDKKYLWGFTLIGWGFPAVFVIPwasvrATLADTR-------CWD 167

                          90       100
                  ....*....|....*....|....*.
gi 564365651 2675 SIHEPLIWSFAGPIVLVIVMNGIMFL 2700
Cdd:cd15265   168 LSAGNYKWIYQVPILAAIVVNFILFL 193
7tmB1_NPR_B7_insect-like cd15273
insect neuropeptide receptor subgroup B7 and related proteins, member of the class B family of ...
 2534-2721 6.50e-08

insect neuropeptide receptor subgroup B7 and related proteins, member of the class B family of seven-transmembrane G protein-coupled receptors; This subgroup includes a neuropeptide receptor found in Nilaparvata lugens (brown planthopper) and its closely related proteins from invertebrates. They belong to the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. The class B GPCRs have been identified in all the vertebrates, from fishes to mammals, as well as invertebrates including Caenorhabditis elegans and Drosophila melanogaster, but are not present in plants, fungi, or prokaryotes.


Pssm-ID: 320401 [Multi-domain]  Cd Length: 285  Bit Score: 56.61  E-value: 6.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2534 LELLAVFTHVVVAASVTALVLTAAVLLSLRSLKSNVRGIHANVAAALGVAELLFLL------------------------ 2589
Cdd:cd15273     1 LPIIKGISQIGYIVSLITLIIAFAIFLSFKKLHCARNKLHMHLFASFILRAFMTLLkdslfidglglladiverngggne 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2590 GIHRTHNQLLCTVVAILLHYFFLSTFAWLLVQGLHLYRMQVEPRNVDRGAMRFYHALGWGVPAVLLG--LAVGLDPEGyg 2667
Cdd:cd15273    81 VIANIGSNWVCKAITSLWQYFIIANYSWILMEGLYLHNLIFLALFSDENNIILYILLGWGLPLIFVVpwIVARILFEN-- 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564365651 2668 npDFCWISIHEPLI-WSFAGPIVLVIVMNGIMFLLAAR-------TSCSTG----QREAKKTSVLV 2721
Cdd:cd15273   159 --SLCWTTNSNLLNfLIIRIPIMISVLINFILFLNIVRvllvklrSSVNEDsrryKKWAKSTLVLV 222
7tmB1_NPR_B3_insect-like cd15262
insect neuropeptide receptor subgroup B3 and related proteins belong to subfamily B1 of ...
 2594-2723 6.54e-08

insect neuropeptide receptor subgroup B3 and related proteins belong to subfamily B1 of hormone receptors; member of the class B secretin-like seven-transmembrane G protein-coupled receptors; This subgroup includes a neuropeptide receptor found in Bombyx mori (silk worm) and its closely related proteins from arthropods. They belong to the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. The class B GPCRs have been identified in all the vertebrates, from fishes to mammals, as well as invertebrates including Caenorhabditis elegans and Drosophila melanogaster, but are not present in plants, fungi, or prokaryotes.


Pssm-ID: 320390 [Multi-domain]  Cd Length: 270  Bit Score: 56.69  E-value: 6.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2594 THNQLLCTVVAILLHYFFLSTFAWLLVQGLHLYRMQVEPRnVDRGAMRFYHALGWGV---PAVLLGLAVGLDpegygNPD 2670
Cdd:cd15262    76 NQNAVVCRLLSIFERAARNAVFACMFVEGFYLHRLIVAVF-AEKSSIRFLYVIGAVLplfPVIIWAIIRALH-----NDH 149

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564365651 2671 FCWISIHEPLIWSFAGPIVLVIVMNGIMFLLAAR--------TSCSTGQREAKKTSVLVLP 2723
Cdd:cd15262   150 SCWVVDIEGVQWVLDTPRLFILLVNTVLLVDIIRvlvtklrnTEENSQTKSTTRATLFLVP 210
7tmB2_GPR116_Ig-Hepta cd15254
The immunoglobulin-repeat-containing receptor Ig-hepta/GPR116, member of the class B2 family ...
 2575-2698 6.63e-08

The immunoglobulin-repeat-containing receptor Ig-hepta/GPR116, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR116 (also known as Ig-hepta) is an orphan receptor that belongs to group VI adhesion-GPCRs along with GPR110, GPR111, GPR113, and GPR115. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. GPR116 has four I-set immunoglobulin-like repeats, which is found in the members of the immunoglobulin superfamily of cell surface proteins, and a SEA (sea urchin sperm protein, enterokinase, and a grin)-box, which is present in the extracellular domain of the transmembrane mucin (MUC) family and known to enhance O-glycosylation. GPR116 is highly expressed in fetal and adult lung, and it has been shown to regulate lung surfactant levels as well as to stimulate breast cancer metastasis through a G(q)-p63-RhoGEF-Rho GTPase signaling pathway. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS.


Pssm-ID: 320382 [Multi-domain]  Cd Length: 275  Bit Score: 56.74  E-value: 6.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2575 NVAAALGVAELLFLL--GIHRTHNQL---LCTVVAILLHYFFLSTFAWLLVQGLHL-YRMQVEPRNVDRGAMR-FYHALG 2647
Cdd:cd15254    48 NIAVSLLIADIWFIVvaAIQDQNYAVngnVCVAATFFIHFFYLCVFFWMLALGLMLfYRLVFILHDTSKTIQKaVAFCLG 127

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 564365651 2648 WGVPAVL--LGLAVGLDPEGYGNPDFCWISIHEP-LIWSFAGPIVLVIVMNGIM 2698
Cdd:cd15254   128 YGCPLIIsvITIAVTLPRDSYTRKKVCWLNWEDSkALLAFVIPALIIVAVNSII 181
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1973-2011 7.24e-08

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 50.71  E-value: 7.24e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 564365651 1973 VDACLL-NPCQNQGSCRHLQGGphgYTCDCASGYFGQHCE 2011
Cdd:cd00054     2 IDECASgNPCQNGGTCVNTVGS---YRCSCPPGYTGRNCE 38
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 1717-1747 8.06e-08

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 50.07  E-value: 8.06e-08
                           10        20        30
                   ....*....|....*....|....*....|.
gi 564365651  1717 CASGPCKNGGLCSERWGGFSCDCPVGFGGKD 1747
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
7tmB1_calcitonin_R cd15274
calcitonin receptor, member of the class B family of seven-transmembrane G protein-coupled ...
 2537-2701 9.28e-08

calcitonin receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; This group includes G protein-coupled receptors for calcitonin (CT) and calcitonin gene-related peptides (CGRPs). Calcitonin, a 32-amino acid peptide hormone, is involved in calcium metabolism in many mammalian species and acts to reduce blood calcium levels and directly inhibits bone resorption by acting on osteoclast. Thus, CT acts as an antagonist to parathyroid hormone and is commonly used in the treatment of bone disorders. The CT receptor is predominantly found in osteoclasts, kidney, and brain, and is primarily coupled to stimulatory G(s) protein, which leads to activation of adenylate cyclase, thereby increasing cAMP production. CGRP, a member of the calcitonin family of peptides, is a potent vasodilator and may contribute to migraine. It is expressed in the peripheral and central nervous system and exists in two forms in humans (alpha-CGRP and beta-CGRP). CGRP meditates its physiological effects through calcitonin receptor-like receptor (CRLR) and receptor activity-modifying protein 1 (RAMP1), a single transmembrane domain protein. Thus, the CRLR/RAMP1 complex serves as a functional CGRP receptor. On the other hand, the CRLR/RAMP2 and CRLR/RAMP3 complexes function as adrenomedullin-specific receptors. The CT and CGRP receptors belong to the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide.


Pssm-ID: 341343 [Multi-domain]  Cd Length: 274  Bit Score: 55.94  E-value: 9.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2537 LAVFTHVVvaaSVTALVLTAAVLLSLRSLKSNVRGIHANVAAALGVAELLFLLGIHR--------THNQLLCTVVAILLH 2608
Cdd:cd15274     7 LAIVGHSL---SIATLLISLGIFFFFRSLSCQRVTLHKNLFLSYILNSIIIIIHLVAvvpngelvARNPVSCKILHFIHQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2609 YFFLSTFAWLLVQGLHLYRMQVEPRNVDRGAMRFYHALGWGVPAVLLGLAVgLDPEGYGNpDFCWISIHEPLIWSFAGPI 2688
Cdd:cd15274    84 YMMGCNYFWMLCEGIYLHTLIVVAVFAEKQRLMWYYLLGWGFPLIPTTIHA-ITRAVYYN-DNCWLSSETHLLYIIHGPI 161

                         170
                  ....*....|...
gi 564365651 2689 VLVIVMNgIMFLL 2701
Cdd:cd15274   162 MAALVVN-FFFLL 173
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1428-1462 1.38e-07

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 49.56  E-value: 1.38e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 564365651 1428 DLCYS-NPCRNGGACARREGGYTCVCRPRFTGEDCE 1462
Cdd:cd00054     3 DECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1472-1505 2.66e-07

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 48.79  E-value: 2.66e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 564365651 1472 PGVCRNGGTCTNAPnGGFRCQCPAGgaFEGPRCE 1505
Cdd:cd00054     8 GNPCQNGGTCVNTV-GSYRCSCPPG--YTGRNCE 38
7tmB1_VIP-R2 cd15986
vasoactive intestinal polypeptide (VIP) receptor 2, member of the class B family of ...
 2546-2700 2.20e-06

vasoactive intestinal polypeptide (VIP) receptor 2, member of the class B family of seven-transmembrane G protein-coupled receptors; Vasoactive intestinal peptide (VIP) receptor 2 is a member of the group of G protein-coupled receptors for structurally similar peptide hormones that also include secretin, growth-hormone-releasing hormone (GHRH), and pituitary adenylate cyclase activating polypeptide (PACAP). These receptors are classified into the subfamily B1 of class B GRCRs that consists of the classical hormone receptors and have been identified in all the vertebrates, from fishes to mammals, but are not present in plants, fungi, or prokaryotes. For all class B receptors, the large N-terminal extracellular domain plays a critical role in peptide hormone recognition. VIP and PACAP exert their effects through three G protein-coupled receptors, PACAP-R1, VIP-R1 (vasoactive intestinal receptor type 1, also known as VPAC1) and VIP-R2 (or VPAC2). PACAP-R1 binds only PACAP with high affinity, whereas VIP-R1 and -R2 specifically bind and respond to both VIP and PACAP. VIP and PACAP and their receptors are widely expressed in the brain and periphery. They are upregulated in neurons and immune cells in responses to CNS injury and/or inflammation and exert potent anti-inflammatory effects, as well as play important roles in the control of circadian rhythms and stress responses, among many others. VIP-R1 is preferentially coupled to a stimulatory G(s) protein, which leads to the activation of adenylate cyclase and thereby increases in intracellular cAMP level. However, depending on its cellular location, VIP-R1 is also capable of coupling to additional G proteins such as G(q) protein, thus leading to the activation of phospholipase C and intracellular calcium influx.


Pssm-ID: 320652 [Multi-domain]  Cd Length: 269  Bit Score: 51.73  E-value: 2.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2546 AASVTALVLTAAVLLSLRSLKSNVRGIHANVAAALGVAELLFLL--GIHRTHNQLL----------CTVVAILLHYFFLS 2613
Cdd:cd15986    13 SVSLIALTTGSTILCLFRKLHCTRNYIHLNLFFSFILRAISVLVkdDILYSSSNTEhctvppsligCKVSLVILQYCIMA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2614 TFAWLLVQGLHLYRMQVEPRNVDRgAMRFYHALGWGVPAVLLGL----AVGLDPEGygnpdfCWISIHEPLIWSFAG-PI 2688
Cdd:cd15986    93 NFYWLLVEGLYLHTLLVVIFSENR-HFIVYLLIGWGIPTVFIIAwivaRIYLEDTG------CWDTNDHSVPWWVIRiPI 165

                         170
                  ....*....|..
gi 564365651 2689 VLVIVMNGIMFL 2700
Cdd:cd15986   166 IISIILNFILFI 177
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 1976-2009 2.71e-06

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 45.84  E-value: 2.71e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 564365651  1976 CLLNPCQNQGSCRHlqgGPHGYTCDCASGYFGQH 2009
Cdd:pfam00008    1 CAPNPCSNGGTCVD---TPGGYTCICPEGYTGKR 31
7tmB1_PTH1R cd15984
parathyroid hormone 1 receptor, member of the class B family of seven-transmembrane G ...
 2600-2723 3.17e-06

parathyroid hormone 1 receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; The parathyroid hormone (PTH) receptor family has three subtypes: PTH1R, PTH2R and PTH3R. PTH1R is expressed in bone and kidney and is activated by two polypeptide ligands: PTH, an endocrine hormone that regulates calcium homoeostasis and bone maintenance, and PTH-related peptide (PTHrP), a paracrine factor that regulates endochondral bone development. PTH1R couples predominantly to G(s)-protein that in turn activates adenylate cyclase thereby producing cAMP, but it can also couple to several G protein subtypes, including G(q/11), G(i/o), and G(12/13), resulting in activation of multiple intracellular signaling pathways. PTH1R is found in all vertebrate species, whereas PTH2R is found in mammals and fish, but not in chicken or frog. PTH3R is found in chicken and fish, but it is absent in mammals. The PTH receptors are members of the B1 (or secretin-like) subfamily of class B GPCRs, which include receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), and calcitonin gene-related peptide. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways.


Pssm-ID: 320650 [Multi-domain]  Cd Length: 290  Bit Score: 51.49  E-value: 3.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2600 CTVVAILLHYFFLSTFAWLLVQGLHLYRMQVEPRNVDRGAMRFYHALGWGVPAVLLGL-----AVGLDPEgygnpdfCWI 2674
Cdd:cd15984    95 CKVAVTFFLYFLATNYYWILVEGLYLHSLIFMAFFSEKKYLWGFTLFGWGLPAVFVTIwasvrATLADTG-------CWD 167

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564365651 2675 SIHEPLIWSFAGPIVLVIVMNGIMFLLAART-----------SCSTGQ--REAKKTSVLVLP 2723
Cdd:cd15984   168 LSAGNLKWIIQVPILAAIVVNFILFINIVRVlatklretnagRCDTRQqyRKLLKSTLVLMP 229
EGF_CA smart00179
Calcium-binding EGF-like domain;
1472-1505 5.49e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 45.32  E-value: 5.49e-06
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 564365651   1472 PGVCRNGGTCTNAPnGGFRCQCPAGgaFE-GPRCE 1505
Cdd:smart00179    8 GNPCQNGGTCVNTV-GSYRCECPPG--YTdGRNCE 39
7tmE_cAMP_R_Slime_mold cd14940
slime mold cyclic AMP receptor, member of the class E family of seven-transmembrane G ...
 2543-2705 6.20e-06

slime mold cyclic AMP receptor, member of the class E family of seven-transmembrane G protein-coupled receptors; This family represents the class E of seven-transmembrane G-protein coupled receptors found in soil-living amoebas, commonly referred to as slime molds. The class E family includes cAMP receptors (cAR1-4) and cAMP receptors-like proteins (CrlA-C) from Dictyostelium discoideum, and their highly homologous cAMP receptors (TasA and TasB) from Polysphondylium pallidum. So far, four subtypes of cAMP receptors (cAR1-4) have been identified that play an essential role in the detection and transmit of the periodic extracellular cAMP waves that regulate chemotactic cell movement during Dictyostelium development, from the unicellular amoeba aggregate into many multicellular slugs and then differentiate into a sporocarp, a fruiting body with cells specialized for different functions. These four subtypes differ in their expression levels and patterns during development. cAR1 is high-affinity receptor that is the first one to be expressed highly during early aggregation and continues to be expressed at low levels during later developmental stages. cAR1 detects extracellular cAMP and is coupled to G-alpha2 protein. Cells lacking cAR1 fail to aggregate, demonstrating that cAR1 is responsible for aggregation. During later aggregation the high-affinity cAR3 receptor is expressed at low levels. Nonetheless, cells lacking cAR3 do not show an obviously altered pattern of development and are still able to aggregate into fruiting bodies. In contrast, cAR2 and cAR4 are low affinity receptors expressed predominantly after aggregation in pre-stalk cells. cAR2 is essential for normal tip formation and deletion of the receptor arrests development at the mound stage. On the other hand, CAR4 regulates axial patterning and cellular differentiation, and deletion of the receptor results in defects during culmination. Furthermore, three cAMP receptor-like proteins (CrlA-C) were identified in Dictyostelium that show limited sequence similarity to the cAMP receptors. Of these CrlA is thought to be required for normal cell growth and tip formation in developing aggregates.


Pssm-ID: 320094 [Multi-domain]  Cd Length: 256  Bit Score: 50.43  E-value: 6.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2543 VVVAASVTALVLTAAVLLS---LRSLKSNV-RGIHANVAAAL--GVAELLFLLGIHRTHNQLLCTVVAILLHYFFLSTFA 2616
Cdd:cd14940     5 ILLFADFSSIIGCLFVLVGfwlLKLLRNHItRVISCFCLTSLlkDIIYTMLTLTQSARPDGFLCYLYAIVITYGSLSCWL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2617 WLLVQGLHLYRMQVEPRNVDRGAMRFYHALGWGVPavLLGLAVGLDPEGYGNP-DFCWIsIHEPLIWSFA---GPIVLVI 2692
Cdd:cd14940    85 WTLCLAISIYLLIVKREPEPEKFEKYYHFVCWGLP--LISTIIMLIKHHYGPVgNWCWI-GNQYTGYRFGlfyGPFFIIF 161

                         170
                  ....*....|...
gi 564365651 2693 VMNGIMFLLAART 2705
Cdd:cd14940   162 GISAVLVGLTSHY 174
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1939-1973 6.91e-06

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 44.94  E-value: 6.91e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 564365651 1939 NPCASG-PCPPHANCKDLWQTFSCTCWPGYYGPGCV 1973
Cdd:cd00054     3 DECASGnPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 1430-1460 7.37e-06

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 44.68  E-value: 7.37e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 564365651  1430 CYSNPCRNGGACARREGGYTCVCRPRFTGED 1460
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
CA_like cd00031
Cadherin repeat-like domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 650-743 1.06e-05

Cadherin repeat-like domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers. This family also includes the cadherin-like repeats of extracellular alpha-dystroglycan.


Pssm-ID: 206635  Cd Length: 98  Bit Score: 46.18  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  650 SVLENAPLGHSVIHIQAvdaDHGENSRLEYSLTGVASDTP---FVINSATGWVSVSGPLDRESVEHYFFGVEARDHGSPP 726
Cdd:cd00031     5 SAVEGRSRGSFRVSIPT---DLIASSGEIIKISAAGKEALpswLHWEPHSGILEGLEKLDREDKGVHYISVSAASLGANV 81

                          90
                  ....*....|....*..
gi 564365651  727 LSASASVTVTVLDVNDN 743
Cdd:cd00031    82 PQTSSVFSIEVYDENDN 98
EGF_CA smart00179
Calcium-binding EGF-like domain;
1428-1462 1.63e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 43.77  E-value: 1.63e-05
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 564365651   1428 DLCYS-NPCRNGGACARREGGYTCVCRPRFT-GEDCE 1462
Cdd:smart00179    3 DECASgNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
EGF_CA smart00179
Calcium-binding EGF-like domain;
1717-1748 1.82e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 43.77  E-value: 1.82e-05
                            10        20        30
                    ....*....|....*....|....*....|....
gi 564365651   1717 CAS-GPCKNGGLCSERWGGFSCDCPVGF-GGKDC 1748
Cdd:smart00179    5 CASgNPCQNGGTCVNTVGSYRCECPPGYtDGRNC 38
7tmB1_PTH3R cd15983
parathyroid hormone 3 receptor, member of the class B family of seven-transmembrane G ...
 2600-2708 2.00e-05

parathyroid hormone 3 receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; The parathyroid hormone 3 receptor (PTH3R), one of the three subtypes of PTH receptor family, is found in chicken and fish, but it is absent in mammals. On the other hand, the PTH1R is found in all vertebrate species, whereas PTH2R is found in mammals and fish, but not in chicken or frog. PTH1R is activated by two polypeptide ligands: PTH, an endocrine hormone that regulates calcium homoeostasis and bone maintenance, and PTH-related peptide (PTHrP), a paracrine factor that regulates endochondral bone development. PTH2R is potently activated by tuberoinfundibular peptide-39 (TIP-39), but not by PTHrP. PTH also strongly activates human PTH2R, but only weakly activates rat and zebrafish PTH2Rs, suggesting that TIP-39 is a natural ligand for PTH2R. Conversely, PTH3R binds and responds to both PTH and PTHrP, but not the TIP-39. The PTH family receptors are members of the B1 (or secretin-like) subfamily of class B GPCRs, which include receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), and calcitonin gene-related peptide. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways.


Pssm-ID: 320649 [Multi-domain]  Cd Length: 285  Bit Score: 49.15  E-value: 2.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2600 CTVVAILLHYFFLSTFAWLLVQGLHLYRMQVEPRNVDRGAMRFYHALGWGVPAVLLGLAVGL-----DPEgygnpdfCWI 2674
Cdd:cd15983    90 CKVTVTLFLYFLATNHYWILVEGLYLHSLIFMAFLSDKNYLWALTIIGWGLPAVFVSVWASVrvslaDTQ-------CWD 162

                          90       100       110
                  ....*....|....*....|....*....|....
gi 564365651 2675 SIHEPLIWSFAGPIVLVIVMNGIMFLLAARTSCS 2708
Cdd:cd15983   163 LSAGNLKWIYQVPILAAILVNFFLFLNIVRVLAS 196
7tmB1_PTH2R cd15982
parathyroid hormone 2 receptor, member of the class B family of seven-transmembrane G ...
 2600-2704 2.31e-05

parathyroid hormone 2 receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; The parathyroid hormone 2 receptor (PTH2R), one of the three subtypes of PTH receptor family, is found in mammals and fish, but not in chicken or frog. PTH2R is potently activated by tuberoinfundibular peptide-39 (TIP-39) but not by PTH-related peptide (PTHrP), a paracrine factor that regulates endochondral bone development. PTH, an endocrine hormone that regulates calcium homoeostasis and bone maintenance, strongly activates human PTH2R, but only weakly activates rat and zebrafish PTH2Rs. These results suggest that TIP-39 is a natural ligand for PTH2R. Conversely, PTH1R is activated by PTH and PTHrP, but not by TIP-39. The PTH family receptors are members of the B1 (or secretin-like) subfamily of class B GPCRs, which include receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), and calcitonin gene-related peptide. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways.


Pssm-ID: 320648 [Multi-domain]  Cd Length: 289  Bit Score: 48.78  E-value: 2.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2600 CTVVAILLHYFFLSTFAWLLVQGLHLYRMQVEPRNVDRGAMRFYHALGWGVPAVLLGL-----AVGLDPEgygnpdfCWI 2674
Cdd:cd15982    95 CKIAVVMFIYFLATNYYWILVEGLYLHSLIFVAFFSDTKYLWGFTLIGWGFPAVFVAAwavvrATLADAR-------CWE 167

                          90       100       110
                  ....*....|....*....|....*....|
gi 564365651 2675 SIHEPLIWSFAGPIVLVIVMNGIMFLLAAR 2704
Cdd:cd15982   168 LSAGDIKWIYQAPILAAIGLNFILFLNTVR 197
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 1717-1746 2.78e-05

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 43.23  E-value: 2.78e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 564365651 1717 CA-SGPCKNGGLCSERWGGFSCDCPVGFGGK 1746
Cdd:cd00053     2 CAaSNPCSNGGTCVNTPGSYRCVCPPGYTGD 32
7tmB1_GlucagonR-like_1 cd15985
uncharacterized group of glucagon receptor-like proteins, member of the class B family of ...
 2545-2700 2.84e-05

uncharacterized group of glucagon receptor-like proteins, member of the class B family of seven-transmembrane G protein-coupled receptors; This group consists of uncharacterized proteins with similarity to members of the glucagon receptor family of G protein-coupled receptors, which include glucagon receptor (GCGR), and glucagon-like peptide-1 receptor (GLP1R), and GLP2R. The glucagon receptors are activated by the members of the glucagon (GCG) peptide family including GCG, glucagon-like peptide 1 (GLP1), and GLP2, which are derived from the large proglucagon precursor. GCGR regulates blood glucose levels by control of hepatic glycogenolysis and gluconeogenesis and by regulation of insulin secretion from the pancreatic beta-cells. Activation of GLP1R stimulates glucose-dependent insulin secretion from pancreatic beta cells, whereas activation of GLP2R stimulates intestinal epithelial proliferation and increases villus height in the small intestine. Receptors in this group belong to the B1 (or secretin-like) subfamily of class B GPCRs, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on their cellular location, GCGR and GLP receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways.


Pssm-ID: 320651 [Multi-domain]  Cd Length: 280  Bit Score: 48.39  E-value: 2.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2545 VAASVTALVLTAA--VLLSLRSLKSNVRGIHANVAAALGV-----------------AELLFL--LGIHRTHNQLL-CTV 2602
Cdd:cd15985    10 VGYTLSLLTLVSAllILTSIRKLHCTRNYIHANLFASFILravsvivkdtllerrwgREIMRVadWGELLSHKAAIgCRM 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2603 VAILLHYFFLSTFAWLLVQGLHLYRMQVEPRNVDRGAMRFYHALGWGVPA--VLLGLAVGLDPEgygNPDfCWiSIHEPL 2680
Cdd:cd15985    90 AQVVMQYCILANHYWFFVEAVYLYKLLIGAVFSEKNYYLLYLYLGWGTPVlfVVPWMLAKYLKE---NKE-CW-ALNENM 164

                         170       180
                  ....*....|....*....|..
gi 564365651 2681 I--WSFAGPIVLVIVMNGIMFL 2700
Cdd:cd15985   165 AywWIIRIPILLASLINLLIFM 186
7tmF_Frizzled_SMO cd13951
class F frizzled/smoothened family, member of the 7-transmembrane G protein-coupled receptor ...
 2600-2702 3.39e-05

class F frizzled/smoothened family, member of the 7-transmembrane G protein-coupled receptor superfamily; The class F G protein-coupled receptors includes the frizzled (FZD) family of seven-transmembrane proteins consisting of 10 isoforms (FZD1-10) in mammals. The FZDs are activated by the wingless/int-1 (WNT) family of secreted lipoglycoproteins and preferentially couple to stimulatory G proteins of the Gs family, which activate adenylate cyclase, but can also couple to G proteins of the Gi/Gq families. In the WNT/beta-catenin signaling pathway, the WNT ligand binds to FZD and a lipoprotein receptor-related protein (LRP) co-receptor. This leads to the stabilization and translocation of beta-catenin to the nucleus, where it induces the activation of TCF/LEF family transcription factors. The conserved cytoplasmic motif of FZD, Lys-Thr-X-X-X-Trp, is required for activation of the WNT/beta-catenin pathway, and for membrane localization and phosphorylation of Dsh (dishevelled) protein, a key component of the WNT pathway that relays the WNT signals from the activated receptor to downstream effector proteins. Also included in the class F family is the closely related smoothened (SMO), which is a transmembrane G protein-coupled receptor that acts as the transducer of the hedgehog (HH) signaling pathway. SMO is activated by the hedgehog (HH) family of proteins acting on the 12-transmembrane domain receptor patched (PTCH), which constitutively inhibits SMO. Thus, in the absence of HH proteins, PTCH inhibits SMO signaling. On the other hand, binding of HH to the PTCH receptor activates its internalization and degradation, thereby releasing the PTCH inhibition of SMO. This allows SMO to trigger intracellular signaling and the subsequent activation of the Gli family of zinc finger transcriptional factors and induction of HH target gene expression (PTCH, Gli1, cyclin, Bcl-2, etc). The WNT and HH signaling pathways play critical roles in many developmental processes, such as cell-fate determination, cell proliferation, neural patterning, stem cell renewal, tissue homeostasis and repair, and tumorigenesis, among many others.


Pssm-ID: 320089  Cd Length: 314  Bit Score: 48.47  E-value: 3.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2600 CTVVAILLHYFFLSTFAWLLVQGLHLYRM--------QVEPRNvdrgamRFYHALGWGVPAVL--LGLAVGL-DPEGYGN 2668
Cdd:cd13951    94 CAIVFLLTYYFGMAASIWWVILTLTWFLSaglkwsseAIEKKS------SYFHLVAWGLPAVLtiAVLVLRKvDGDELTG 167

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 564365651 2669 pdFCWISIHEP--LIWSFAGPIVLVIVMnGIMFLLA 2702
Cdd:cd13951   168 --ICFVGNQNLdaLRGFVLAPLFLYLIL-GTVFLLC 200
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 1432-1462 3.41e-05

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 42.85  E-value: 3.41e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 564365651 1432 SNPCRNGGACARREGGYTCVCRPRFTGE-DCE 1462
Cdd:cd00053     5 SNPCSNGGTCVNTPGSYRCVCPPGYTGDrSCE 36
Frizzled pfam01534
Frizzled/Smoothened family membrane region; This family contains the membrane spanning region ...
 2594-2703 4.16e-05

Frizzled/Smoothened family membrane region; This family contains the membrane spanning region of frizzled and smoothened receptors. This membrane region is predicted to contain seven transmembrane alpha helices. Proteins related to Drosophila frizzled are receptors for Wnt (mediating the beta-catenin signalling pathway), but also the planar cell polarity (PCP) pathway and the Wnt/calcium pathway. The predominantly alpha-helical Cys-rich ligand-binding region (CRD) of Frizzled is both necessary and sufficient for Wnt binding. The smoothened receptor mediates hedgehog signalling.


Pssm-ID: 460242  Cd Length: 321  Bit Score: 48.37  E-value: 4.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  2594 THNqLLCTVVAILLHYFFLS--------TFAWLLVQGLHLYRMQVEPRNVdrgamrFYHALGWGVPAVL--LGLAVG-LD 2662
Cdd:pfam01534   89 TEN-LSCTVVFLLLYYFGMAasiwwvilTLTWFLAAGLKWGSEAIEKKSS------YFHLAAWGIPAVLtiTVLALGkVD 161

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 564365651  2663 PE--------GYGNPDFcwisihepLIWSFAGPIVLVIVMnGIMFLLAA 2703
Cdd:pfam01534  162 GDeltgicfvGNQNSDA--------LRGFVLAPLLVYLLL-GTYFLLAG 201
Laminin_G_1 pfam00054
Laminin G domain;
1784-1911 4.82e-05

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 45.39  E-value: 4.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  1784 FRTRATKGVLMQVQLGPHSV-LLCKLDQGLLSVTLSRASGHAVHLLLDqmTVSDGRWHDLRLElqeepggrRGHHIFMVS 1862
Cdd:pfam00054    1 FRTTEPSGLLLYNGTQTERDfLALELRDGRLEVSYDLGSGAAVVRSGD--KLNDGKWHSVELE--------RNGRSGTLS 70

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 564365651  1863 LDFTLFQDTMAMGSELEGLKV-KHLHVGGPPPSSKEEGPQ----GLVGCIQGVW 1911
Cdd:pfam00054   71 VDGEARPTGESPLGATTDLDVdGPLYVGGLPSLGVKKRRLaispSFDGCIRDVI 124
CA_like cd00031
Cadherin repeat-like domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 325-420 6.85e-05

Cadherin repeat-like domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers. This family also includes the cadherin-like repeats of extracellular alpha-dystroglycan.


Pssm-ID: 206635  Cd Length: 98  Bit Score: 43.87  E-value: 6.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  325 VPENEAAGTAVLRVVAqdpDPGEAGRLVYSLAALMNSRSLELFSIDPQSGLIRTAAALDRESMERHYLRVTAQDHGSPRL 404
Cdd:cd00031     6 AVEGRSRGSFRVSIPT---DLIASSGEIIKISAAGKEALPSWLHWEPHSGILEGLEKLDREDKGVHYISVSAASLGANVP 82

                          90
                  ....*....|....*.
gi 564365651  405 SATTMVAVTVADRNDH 420
Cdd:cd00031    83 QTSSVFSIEVYDENDN 98
7tmB1_PTH-R_related cd15272
invertebrate parathyroid hormone-related receptors, member of the class B family of ...
 2534-2721 1.38e-04

invertebrate parathyroid hormone-related receptors, member of the class B family of seven-transmembrane G protein-coupled receptors; This group includes parathyroid hormone (PTH)-related receptors found in invertebrates such as mollusks and annelid worms. The PTH family receptors are members of the B1 subfamily of class B GPCRs, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), and calcitonin gene-related peptide. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. The parathyroid hormone type 1 receptor (PTH1R) is found in all vertebrate species and is activated by two polypeptide ligands: parathyroid hormone (PTH), an endocrine hormone that regulates calcium homoeostasis and bone maintenance, and PTH-related peptide (PTHrP), a paracrine factor that regulates endochondral bone development. PTH1R couples predominantly to G(s)- protein that in turn activates adenylyl cyclase thereby producing cAMP, but it can also couple to several G protein subtypes, including G(q/11), G(i/o), and G(12/13), resulting in activation of multiple signaling pathways.


Pssm-ID: 320400 [Multi-domain]  Cd Length: 285  Bit Score: 46.61  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2534 LELLAvftHVVVAASVTALVLTAAVLLSLRSLKSNVRGIHAN------VAAALG-VAELLFLLG------IHRTHNQLL- 2599
Cdd:cd15272     4 IRLMY---NIGYGLSLVSLLIAVIIMLYFKKLHCPRNTIHINlfvsfiLRAVLSfIKENLLVQGvgfpgdVYYDSNGVIe 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2600 ---------CTVVAILLHYFFLSTFAWLLVQGLHLYRMQVEPRNVDRGAMRFYHALGWGVPA--VLLGLAVgldpEGYGN 2668
Cdd:cd15272    81 fkdegshweCKLFFTMFNYILGANYMWIFVEGLYLHMLIFVAVFSENSRVKWYILLGWLSPLlfVLPWVFV----RATLE 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564365651 2669 PDFCWISIHEPL-IWSFAGPIVLVIVMNGIMF----------LLAARTSCSTGQRE---AKKTSVLV 2721
Cdd:cd15272   157 DTLCWNTNTNKGyFWIIRGPIVISIAINFLFFinivrvlftkLKASNTQESRPFRYrklAKSTLVLI 223
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 1472-1505 1.92e-04

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 40.92  E-value: 1.92e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 564365651 1472 PGVCRNGGTCTNAPnGGFRCQCPAGgaFEGP-RCE 1505
Cdd:cd00053     5 SNPCSNGGTCVNTP-GSYRCVCPPG--YTGDrSCE 36
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 1979-2011 2.29e-04

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 40.54  E-value: 2.29e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 564365651 1979 NPCQNQGSCRHLQGgphGYTCDCASGYFGQ-HCE 2011
Cdd:cd00053     6 NPCSNGGTCVNTPG---SYRCVCPPGYTGDrSCE 36
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 1994-2033 3.82e-04

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 40.41  E-value: 3.82e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 564365651  1994 PHGYTCDCASGYFGQHCEhrmdqQCPRGWWGSPTCGPCNC 2033
Cdd:pfam00053   15 PETGQCLCKPGVTGRHCD-----RCKPGYYGLPSDPPQGC 49
CA_like cd00031
Cadherin repeat-like domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
 854-948 5.20e-04

Cadherin repeat-like domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers. This family also includes the cadherin-like repeats of extracellular alpha-dystroglycan.


Pssm-ID: 206635  Cd Length: 98  Bit Score: 41.56  E-value: 5.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651  854 YSVSMNEDRPvgSTVVVISAS-DDDVGENARITYLLEDNLPQ-FRIDADSGAITLQAPLDYEDQVTYTLAITARDNGIPQ 931
Cdd:cd00031     4 GSAVEGRSRG--SFRVSIPTDlIASSGEIIKISAAGKEALPSwLHWEPHSGILEGLEKLDREDKGVHYISVSAASLGANV 81

                          90
                  ....*....|....*..
gi 564365651  932 KADTTYVEVMVNDVNDN 948
Cdd:cd00031    82 PQTSSVFSIEVYDENDN 98
hEGF pfam12661
Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six ...
 1475-1496 7.94e-04

Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six conserved residues disulfide-bonded into the characteriztic 'ababcc' pattern. They are involved in growth and proliferation of cells, in proteins of the Notch/Delta pathway, neurogulin and selectins. hEGFs are also found in mosaic proteins with four-disulfide laminin EGFs such as aggrecan and perlecan. The core fold of the EGF domain consists of two small beta-hairpins packed against each other. Two major structural variants have been identified based on the structural context of the C-terminal Cys residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In hEGFs the C-terminal thiol resides in the beta-turn, resulting in shorter loop-lengths between the Cys residues of disulfide 'c', typically C[8-9]XC. These shorter loop-lengths are also typical of the four-disulfide EGF domains, laminin ad integrin. Tandem hEGF domains have six linking residues between terminal cysteines of adjacent domains. hEGF domains may or may not bind calcium in the linker region. hEGF domains with the consensus motif CXD4X[F,Y]XCXC are hydroxylated exclusively in the Asp residue.


Pssm-ID: 463660  Cd Length: 22  Bit Score: 38.85  E-value: 7.94e-04
                           10        20
                   ....*....|....*....|..
gi 564365651  1475 CRNGGTCTNAPNgGFRCQCPAG 1496
Cdd:pfam12661    1 CQNGGTCVDGVN-GYKCQCPPG 21
hEGF pfam12661
Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six ...
 1722-1743 9.02e-04

Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six conserved residues disulfide-bonded into the characteriztic 'ababcc' pattern. They are involved in growth and proliferation of cells, in proteins of the Notch/Delta pathway, neurogulin and selectins. hEGFs are also found in mosaic proteins with four-disulfide laminin EGFs such as aggrecan and perlecan. The core fold of the EGF domain consists of two small beta-hairpins packed against each other. Two major structural variants have been identified based on the structural context of the C-terminal Cys residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In hEGFs the C-terminal thiol resides in the beta-turn, resulting in shorter loop-lengths between the Cys residues of disulfide 'c', typically C[8-9]XC. These shorter loop-lengths are also typical of the four-disulfide EGF domains, laminin ad integrin. Tandem hEGF domains have six linking residues between terminal cysteines of adjacent domains. hEGF domains may or may not bind calcium in the linker region. hEGF domains with the consensus motif CXD4X[F,Y]XCXC are hydroxylated exclusively in the Asp residue.


Pssm-ID: 463660  Cd Length: 22  Bit Score: 38.47  E-value: 9.02e-04
                           10        20
                   ....*....|....*....|..
gi 564365651  1722 CKNGGLCSERWGGFSCDCPVGF 1743
Cdd:pfam12661    1 CQNGGTCVDGVNGYKCQCPPGY 22
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
 1188-1257 1.77e-03

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520 [Multi-domain]  Cd Length: 81  Bit Score: 39.64  E-value: 1.77e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564365651   1188 AYDPDVSD--HLFYSFERGNELQLLVVNQTSGELRLSRKLDNNRPLVASMLVTVTD-GLHSVTAQCVLRVVII 1257
Cdd:smart00112    2 ATDADSGEngKVTYSILSGNDDGLFSIDPETGEITTTKPLDREEQPEYTLTVEATDgGGPPLSSTATVTITVL 74
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 2030-2054 2.11e-03

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 38.10  E-value: 2.11e-03
                          10        20
                  ....*....|....*....|....*
gi 564365651 2030 PCNCDVHKGFDPNCNKTSGQCHCKE 2054
Cdd:cd00055     1 PCDCNGHGSLSGQCDPGTGQCECKP 25
EGF_CA smart00179
Calcium-binding EGF-like domain;
1939-1973 2.11e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 38.00  E-value: 2.11e-03
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 564365651   1939 NPCAS-GPCPPHANCKDLWQTFSCTCWPGYY-GPGCV 1973
Cdd:smart00179    3 DECASgNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
2031-2054 3.31e-03

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 37.68  E-value: 3.31e-03
                            10        20
                    ....*....|....*....|....
gi 564365651   2031 CNCDVHKGFDPNCNKTSGQCHCKE 2054
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKP 24
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 2031-2067 3.75e-03

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 37.72  E-value: 3.75e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 564365651  2031 CNCDVHKGFDPNCNKTSGQCHCKEfHYRPRGSDSCLP 2067
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKP-GVTGRHCDRCKP 36
EGF_2 pfam07974
EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.
 1981-2010 4.40e-03

EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.


Pssm-ID: 400365  Cd Length: 26  Bit Score: 36.94  E-value: 4.40e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 564365651  1981 CQNQGSCRHLQGGphgytCDCASGYFGQHC 2010
Cdd:pfam07974    2 CSGRGTCVNQCGK-----CVCDSGYQGATC 26
7tmF_FZD3 cd15033
class F frizzled subfamily 3, member of 7-transmembrane G protein-coupled receptors; This ...
 2594-2702 5.73e-03

class F frizzled subfamily 3, member of 7-transmembrane G protein-coupled receptors; This group includes subfamily 3 of the frizzled (FZD) family of seven transmembrane-spanning proteins, which constitute a novel and separate class of GPCRs, and its closely related proteins. This class F protein family consists of 10 isoforms (FZD1-10) in mammals. The FZDs are activated by the wingless/int-1 (WNT) family of secreted lipoglycoproteins and preferentially couple to stimulatory G proteins of the Gs family, which activate adenylate cyclase, but can also couple to G proteins of the Gi/Gq families. In the WNT/beta-catenin signaling pathway, the WNT ligand binds to FZD and a lipoprotein receptor-related protein (LRP) co-receptor. This leads to the stabilization and translocation of beta-catenin to the nucleus, where it induces the activation of TCF/LEF family transcription factors. The conserved cytoplasmic motif of FZD, Lys-Thr-X-X-X-Trp, is required for activation of the WNT/beta-catenin pathway, and for membrane localization and phosphorylation of Dsh (dishevelled) protein, a key component of the WNT pathway that relays the WNT signals from the activated receptor to downstream effector proteins. The WNT pathway plays a critical role in many developmental processes, such as cell-fate determination, cell proliferation, neural patterning, stem cell renewal, tissue homeostasis and repair, and tumorigenesis, among many others.


Pssm-ID: 320161  Cd Length: 321  Bit Score: 41.47  E-value: 5.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365651 2594 THNQLlCTVVAILLHYFFLSTFAWLLVQGLHLYRMQVePR----NVDRGAMRFyHALGWGVPAVLLGLAVGLDP-EGYGN 2668
Cdd:cd15033    90 SHNKA-CTMLFMVLYFFTMAGSVWWVILTITWFLAAV-PKwgseAIEKKALLF-HASAWGIPGTLTIILLAMNKiEGDNI 166

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 564365651 2669 PDFCWISIHE--PLIWSFAGPIVLVIVMnGIMFLLA 2702
Cdd:cd15033   167 SGVCFVGLYDvdALRYFVLAPLCLDVVV-GVSLLLA 201
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 1940-1971 6.76e-03

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 36.30  E-value: 6.76e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 564365651 1940 PCA-SGPCPPHANCKDLWQTFSCTCWPGYYGPG 1971
Cdd:cd00053     1 ECAaSNPCSNGGTCVNTPGSYRCVCPPGYTGDR 33
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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