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Conserved domains on  [gi|1635577207|ref|NP_001357452|]
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C-type lectin domain family 18 member A precursor [Homo sapiens]

Protein Classification

C-type lectin domain-containing protein( domain architecture ID 10143469)

C-type lectin (CTL)/C-type lectin-like (CTLD) domain-containing protein may bind carbohydrate in a calcium-dependent manner

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 310-434 8.37e-22

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.


:

Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 89.99  E-value: 8.37e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577207 310 CFMVSSEADTYYRARMKCQRKGGVLAQIKSQKVQDILAFYLgrlettnevidSDFETRNFWIGLTYKTAKDSFRWATGEH 389
Cdd:cd00037     2 CYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLL-----------KKSSSSDVWIGLNDLSSEGTWKWSDGSP 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1635577207 390 QA-FTSFAFGQPDNHGFGNCVELQASAAFNWNDQRCKTRNRYICQF 434
Cdd:cd00037    71 LVdYTNWAPGEPNPGGSEDCVVLSSSSDGKWNDVSCSSKLPFICEK 116
CAP_euk cd05380
Eukaryotic CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 ...
 50-183 7.96e-18

Eukaryotic CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain proteins; The CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain is found mainly in eukaryotes. This family includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), glioma pathogenesis-related 1 (GLIPR1), Golgi associated pathogenesis related-1 (GAPR1) proteins, peptidase inhibitor 15 (PI15), peptidase inhibitor 16 (PI16), CRISP LCCL domain containing 1 (CRISPLD1), CRISP LCCL domain containing 2 (CRISPLD2), and allergen 5 from vespid venom.


:

Pssm-ID: 349399  Cd Length: 144  Bit Score: 79.81  E-value: 7.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577207  50 LLLSLHNRLRSWV-------QPPAADMRRLDWSDSLAQLAQARAALCGTPTpslaSGLWRTLQVGWNMQLLPAGLVS--- 119
Cdd:cd05380     3 EILDAHNELRSKVakgklkgLPPAANMPKLKWDCELAKLAQNWAKTCVFAH----SPCRNTGGVGQNLASVSSSGKDlke 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1635577207 120 -FVEVVSLWFAEGQRYSHAAGE-CARNATCTHYTQLVWATSSQLGCGRHLCSAGQAAIEAFVCAYS 183
Cdd:cd05380    79 lIEDAVNAWFDELKDYGFGSNPnNNFNSGIGHFTQMVWAKTTKVGCAVARCPKGGGNKTYVVCNYS 144
 
Name Accession Description Interval E-value
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 310-434 8.37e-22

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 89.99  E-value: 8.37e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577207 310 CFMVSSEADTYYRARMKCQRKGGVLAQIKSQKVQDILAFYLgrlettnevidSDFETRNFWIGLTYKTAKDSFRWATGEH 389
Cdd:cd00037     2 CYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLL-----------KKSSSSDVWIGLNDLSSEGTWKWSDGSP 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1635577207 390 QA-FTSFAFGQPDNHGFGNCVELQASAAFNWNDQRCKTRNRYICQF 434
Cdd:cd00037    71 LVdYTNWAPGEPNPGGSEDCVVLSSSSDGKWNDVSCSSKLPFICEK 116
CAP_euk cd05380
Eukaryotic CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 ...
 50-183 7.96e-18

Eukaryotic CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain proteins; The CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain is found mainly in eukaryotes. This family includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), glioma pathogenesis-related 1 (GLIPR1), Golgi associated pathogenesis related-1 (GAPR1) proteins, peptidase inhibitor 15 (PI15), peptidase inhibitor 16 (PI16), CRISP LCCL domain containing 1 (CRISPLD1), CRISP LCCL domain containing 2 (CRISPLD2), and allergen 5 from vespid venom.


Pssm-ID: 349399  Cd Length: 144  Bit Score: 79.81  E-value: 7.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577207  50 LLLSLHNRLRSWV-------QPPAADMRRLDWSDSLAQLAQARAALCGTPTpslaSGLWRTLQVGWNMQLLPAGLVS--- 119
Cdd:cd05380     3 EILDAHNELRSKVakgklkgLPPAANMPKLKWDCELAKLAQNWAKTCVFAH----SPCRNTGGVGQNLASVSSSGKDlke 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1635577207 120 -FVEVVSLWFAEGQRYSHAAGE-CARNATCTHYTQLVWATSSQLGCGRHLCSAGQAAIEAFVCAYS 183
Cdd:cd05380    79 lIEDAVNAWFDELKDYGFGSNPnNNFNSGIGHFTQMVWAKTTKVGCAVARCPKGGGNKTYVVCNYS 144
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 310-433 3.58e-17

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 77.25  E-value: 3.58e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577207  310 CFMVSSEADTYYRARMKCQRKGGVLAQIKSQKVQDILafylgrlettNEVIDSDFETRNFWIGLTYKTAKDSFRWATG-E 388
Cdd:smart00034  12 CYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFV----------ASLLKNSGSSDYYWIGLSDPDSNGSWQWSDGsG 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1635577207  389 HQAFTSFAFGQPDNHGfGNCVELQASAAFnWNDQRCKTRNRYICQ 433
Cdd:smart00034  82 PVSYSNWAPGEPNNSS-GDCVVLSTSGGK-WNDVSCTSKLPFVCE 124
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 319-434 1.17e-14

Lectin C-type domain; This family includes both long and short form C-type


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 69.81  E-value: 1.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577207 319 TYYRARMKCQRKGGVLAQIKSQKVQDILAFYLGRlettnevidsdfETRNFWIGLTYKTAKDSFRWATGEHQAFTSFAFG 398
Cdd:pfam00059   3 TWDEAREACRKLGGHLVSINSAEELDFLSSTLKK------------SNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPE 70

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1635577207 399 QPDNHGFGNCVELQASAAFnWNDQRCKTRNRYICQF 434
Cdd:pfam00059  71 PNNNGENEDCVELSSSSGK-WNDENCNSKNPFVCEK 105
SCP smart00198
SCP / Tpx-1 / Ag5 / PR-1 / Sc7 family of extracellular domains; Human glioma ...
 51-184 1.98e-13

SCP / Tpx-1 / Ag5 / PR-1 / Sc7 family of extracellular domains; Human glioma pathogenesis-related protein GliPR and the plant pathogenesis-related protein represent functional links between plant defense systems and human immune system. This family has no known function.


Pssm-ID: 214553 [Multi-domain]  Cd Length: 144  Bit Score: 67.41  E-value: 1.98e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577207   51 LLSLHNRLRS------WVQPPAADMRRLDWSDSLAQLAQARAALCGTPTPSLASGLWRTLQVGWNMQLLPagLVSFVEVV 124
Cdd:smart00198   6 ILDAHNKLRSqvaggfLAAPAASNMLKLTWDCELASSAQNWANQCPFGHSTPRPGYGENLAWWSSSTALP--DTYASAAV 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1635577207  125 SLWFAEGQRYSHAAGECA-RNATCTHYTQLVWATSSQLGCGRHLCSAGQAAIEAFVCAYSP 184
Cdd:smart00198  84 QLWYDEFQDYGYSSNTCKdTNGKIGHYTQVVWAKTYKVGCGVANCPDGTKKKTVVVCNYDP 144
CAP pfam00188
Cysteine-rich secretory protein family; This is a large family of cysteine-rich secretory ...
 52-182 1.93e-08

Cysteine-rich secretory protein family; This is a large family of cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins (CAP) that are found in a wide range of organizms, including prokaryotes and non-vertebrate eukaryotes, The nine subfamilies of the mammalian CAP 'super'family include: the human glioma pathogenesis-related 1 (GLIPR1), Golgi associated pathogenesis related-1 (GAPR1) proteins, peptidase inhibitor 15 (PI15), peptidase inhibitor 16 (PI16), cysteine-rich secretory proteins (CRISPs), CRISP LCCL domain containing 1 (CRISPLD1), CRISP LCCL domain containing 2 (CRISPLD2), mannose receptor like and the R3H domain containing like proteins. Members are most often secreted and have an extracellular endocrine or paracrine function and are involved in processes including the regulation of extracellular matrix and branching morphogenesis, potentially as either proteases or protease inhibitors; in ion channel regulation in fertility; as tumour suppressor or pro-oncogenic genes in tissues including the prostate; and in cell-cell adhesion during fertilization. The overall protein structural conservation within the CAP 'super'family results in fundamentally similar functions for the CAP domain in all members, yet the diversity outside of this core region dramatically alters the target specificity and, thus, the biological consequences. The Ca++-chelating function would fit with the various signalling processes (e.g. the CRISP proteins) that members of this family are involved in, and also the sequence and structural evidence of a conserved pocket containing two histidines and a glutamate. It also may explain how Swiss:Q91055 blocks the Ca++ transporting ryanodine receptors.


Pssm-ID: 395136  Cd Length: 117  Bit Score: 52.21  E-value: 1.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577207  52 LSLHNRLRswvqpPAADMRRLDWSDS------LAQLAQARAALCGTPTPSLASGLWRTLQVGWNmqLLPAGLVSFVEVVS 125
Cdd:pfam00188   1 LDLHNEYR-----AAAGLPPLSWDNElaaaaqDHAKYCADNGSHNHRSPYGGNIYARVVAAGYA--LGDAGPDSAEDAVD 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1635577207 126 LWFAEGQRYShaagecarnatCTHYTQLVWATSSQLGCGRHLCSAGQaaIEAFVCAY 182
Cdd:pfam00188  74 GWYDSPGTYN-----------CGHRTNLLWPKSTKVGCAVAKCGDGG--TYYFVCNY 117
 
Name Accession Description Interval E-value
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 310-434 8.37e-22

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 89.99  E-value: 8.37e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577207 310 CFMVSSEADTYYRARMKCQRKGGVLAQIKSQKVQDILAFYLgrlettnevidSDFETRNFWIGLTYKTAKDSFRWATGEH 389
Cdd:cd00037     2 CYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLL-----------KKSSSSDVWIGLNDLSSEGTWKWSDGSP 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1635577207 390 QA-FTSFAFGQPDNHGFGNCVELQASAAFNWNDQRCKTRNRYICQF 434
Cdd:cd00037    71 LVdYTNWAPGEPNPGGSEDCVVLSSSSDGKWNDVSCSSKLPFICEK 116
CAP_euk cd05380
Eukaryotic CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 ...
 50-183 7.96e-18

Eukaryotic CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain proteins; The CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain is found mainly in eukaryotes. This family includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), glioma pathogenesis-related 1 (GLIPR1), Golgi associated pathogenesis related-1 (GAPR1) proteins, peptidase inhibitor 15 (PI15), peptidase inhibitor 16 (PI16), CRISP LCCL domain containing 1 (CRISPLD1), CRISP LCCL domain containing 2 (CRISPLD2), and allergen 5 from vespid venom.


Pssm-ID: 349399  Cd Length: 144  Bit Score: 79.81  E-value: 7.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577207  50 LLLSLHNRLRSWV-------QPPAADMRRLDWSDSLAQLAQARAALCGTPTpslaSGLWRTLQVGWNMQLLPAGLVS--- 119
Cdd:cd05380     3 EILDAHNELRSKVakgklkgLPPAANMPKLKWDCELAKLAQNWAKTCVFAH----SPCRNTGGVGQNLASVSSSGKDlke 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1635577207 120 -FVEVVSLWFAEGQRYSHAAGE-CARNATCTHYTQLVWATSSQLGCGRHLCSAGQAAIEAFVCAYS 183
Cdd:cd05380    79 lIEDAVNAWFDELKDYGFGSNPnNNFNSGIGHFTQMVWAKTTKVGCAVARCPKGGGNKTYVVCNYS 144
CAP_GLIPR1-like cd05385
CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain ...
 52-186 1.65e-17

CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of glioma pathogenesis-related protein 1 and similar proteins; Glioma pathogenesis-related protein 1 (GLIPR1) is also called related to testes-specific, vespid, and pathogenesis protein 1 (RTVP-1). The GLIPR1 gene has been identified as a p53 target gene and was shown to be methylated and down-regulated in prostate cancer. It is a novel broad-spectrum tumor suppressor whose proapoptotic properties are exerted in part through ROS-JNK signaling. GLIPR1 is composed of a signal peptide that directs its secretion, a CAP domain, and a transmembrane domain. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others.


Pssm-ID: 349404  Cd Length: 148  Bit Score: 78.99  E-value: 1.65e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577207  52 LSLHNRLRSWVQPPAADMRRLDWSDSLAQLAQARAALC-GTPTPSL--ASGLWRTLQ-VGWNMQLLPAGLVSFVEVVSLW 127
Cdd:cd05385     7 VRIHNELRSKVSPPAANMRYMSWDKALAKTARAWARKCkFSHNICLkePGKCHPNFTtLGENIWLGSIFSFSVESAITSW 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1635577207 128 FAEGQRYSHAAGECARnaTCTHYTQLVWATSSQLGCGRHLCSAG-------QAAIeaFVCAYSPRG 186
Cdd:cd05385    87 YNEVKDYNFKTNSCSR--VCGHYTQVVWADSYKVGCAVHVCPNGggffsgsSSAI--FVCNYGPAG 148
CAP_PI16_HrTT-1 cd05559
CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain ...
 50-183 2.55e-17

CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of peptidase inhibitor 16 and HrTT-1 protein; Human peptidase inhibitor 16 (PI16) is also called cysteine-rich secretory protein 9 (CRISP-9) or PSP94-binding protein. Mouse PI16 is also called cysteine-rich protease inhibitor. PI16 is predominantly expressed by cardiac fibroblasts and is exposed to the interstitium via a glycophosphatidylinositol (-GPI) membrane anchor. It suppresses the activation of the chemokine chemerin in the myocardium, which may be a part of the cardiac stress response. At high endothelial shear stress, PI16 is an inflammation-regulated inhibitor of matrix metalloproteinase 2 (MMP2). Also included in this subfamily is the HrTT-1 protein, a tail-tip epidermis marker in ascidians. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others.


Pssm-ID: 349405  Cd Length: 134  Bit Score: 78.23  E-value: 2.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577207  50 LLLSLHNRLRSWVQPPAADMRRLDWSDSLAQLAQARAALCgtptpslasgLW----RTLQVGWNMQLLPAGLVSFVEVVS 125
Cdd:cd05559     3 LLVDLHNQYRSQVSPSAANMLKMTWDTELEALAKAYARKC----------IWehnpDRGRVGENLFASTGKPLDVELAVE 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1635577207 126 LWFAEGQRYSHAAGECARNATCTHYTQLVWATSSQLGCGRHLCSAGQ----AAIEAFVCAYS 183
Cdd:cd05559    73 DWHNEKEYYNFETKTCAPGKMCGHYTQVVWANTEKIGCGSYFCETLEgvewENATLLVCNYE 134
CAP_CRISP cd05383
CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain ...
 44-184 3.43e-17

CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of cysteine-rich secretory proteins; Cysteine-rich secretory proteins (CRISPs) are two-domain proteins with an evolutionary diverse and structurally conserved N-terminal CAP domain and a C-terminal cysteine-rich domain, which is comprised of a hinge and an ICR (ion channel regulator) region. CRISPs are involved in response to pathogens, fertilization, and sperm maturation. One member, Tex31 from the venom duct of Conus textile, has been shown to possess proteolytic activity sensitive to serine protease inhibitors. CRISP-1 has been shown to mediate gamete fusion by binding to the egg surface. Other members of the CRISP family secreted in the testis (CRISP2), epididymis (CRISP3-4), or during ejaculation (CRISP3), are also involved in sperm-egg interaction, supporting the existence of a functional redundancy and cooperation between homolog proteins ensuring the success of fertilization. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1) and allergen 5 from vespid venom, among others.


Pssm-ID: 349402  Cd Length: 139  Bit Score: 77.78  E-value: 3.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577207  44 NRKEsflLLSLHNRLRSWVQPPAADMRRLDWSDSLAQLAQARAALCgTPTPSLASGLWRT-LQVGWNMqLLPAGLVSFVE 122
Cdd:cd05383     2 VQQE---IVDLHNALRRSVNPPASNMLKMSWNPEAAENAQRWANRC-NFTHSPPNGRTIPgIRCGENI-FMSSYPASWSE 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1635577207 123 VVSLWFAEGQRYSHAAGECARNATCTHYTQLVWATSSQLGCGRHLCSAGQAAIEAFVCAYSP 184
Cdd:cd05383    77 VIQAWYDEYKDFKYGVGAKPPGSVTGHYTQVVWYSSYLVGCAVAYCPSQGSLKYFYVCQYCP 138
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 310-433 3.58e-17

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 77.25  E-value: 3.58e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577207  310 CFMVSSEADTYYRARMKCQRKGGVLAQIKSQKVQDILafylgrlettNEVIDSDFETRNFWIGLTYKTAKDSFRWATG-E 388
Cdd:smart00034  12 CYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFV----------ASLLKNSGSSDYYWIGLSDPDSNGSWQWSDGsG 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1635577207  389 HQAFTSFAFGQPDNHGfGNCVELQASAAFnWNDQRCKTRNRYICQ 433
Cdd:smart00034  82 PVSYSNWAPGEPNNSS-GDCVVLSTSGGK-WNDVSCTSKLPFVCE 124
CAP_PR-1 cd05381
CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain ...
 107-189 4.37e-17

CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of pathogenesis-related protein 1 (PR-1) family proteins; Members of pathogenesis-related protein 1 (PR-1) family are among the most abundantly produced proteins in plants on pathogen attack. They are considered hallmarks of hypersensitive response/defense pathways and may act as anti-fungal agents or be involved in cell wall loosening.


Pssm-ID: 349400  Cd Length: 136  Bit Score: 77.67  E-value: 4.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577207 107 GWNMQLLPAGLVSFVEVVSLWFAEGQRYSHAAGECARNATCTHYTQLVWATSSQLGCGRHLCSAGQAAIeaFVCAYSPRG 186
Cdd:cd05381    51 GENLFWGSGDNWSPADAVKSWVDEKPYYDYASNTCVGGKMCGHYTQVVWRNSTRLGCARVVCDNNGGTF--VICNYDPPG 128


                  ...
gi 1635577207 187 NWE 189
Cdd:cd05381   129 NYI 131
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 319-434 1.17e-14

Lectin C-type domain; This family includes both long and short form C-type


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 69.81  E-value: 1.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577207 319 TYYRARMKCQRKGGVLAQIKSQKVQDILAFYLGRlettnevidsdfETRNFWIGLTYKTAKDSFRWATGEHQAFTSFAFG 398
Cdd:pfam00059   3 TWDEAREACRKLGGHLVSINSAEELDFLSSTLKK------------SNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPE 70

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1635577207 399 QPDNHGFGNCVELQASAAFnWNDQRCKTRNRYICQF 434
Cdd:pfam00059  71 PNNNGENEDCVELSSSSGK-WNDENCNSKNPFVCEK 105
CAP_R3HDML cd18815
CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain ...
 50-169 4.23e-14

CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of peptidase inhibitor R3HDML; Peptidase inhibitor R3HDML, also called cysteine-rich secretory protein R3HDML, is a putative serine protease inhibitor. The R3HDML gene may be associated with clinical dimensions of schizophrenia. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others.


Pssm-ID: 349409  Cd Length: 146  Bit Score: 69.54  E-value: 4.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577207  50 LLLSLHNRLRSWVQPPAADMRRLDWSDSLAQLAQARAALCgtptpSLASGLWRTLQ-VGWNMQLLPAGLVSFVEVVSLWF 128
Cdd:cd18815     3 ALLDYHNRVRSQVFPPAANMEYMVWDERLAKSAEAWAAQC-----VWEHGPPQLMRyIGQNLSIHSGRYRSIVDLVKSWY 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1635577207 129 AEGQRYSHAAG-EC-------ARNATCTHYTQLVWATSSQLGCGRHLCS 169
Cdd:cd18815    78 DERQHYSFPHPrECnprcpskCSGAVCSHYTQMVWASSNRIGCAVHTCS 126
SCP smart00198
SCP / Tpx-1 / Ag5 / PR-1 / Sc7 family of extracellular domains; Human glioma ...
 51-184 1.98e-13

SCP / Tpx-1 / Ag5 / PR-1 / Sc7 family of extracellular domains; Human glioma pathogenesis-related protein GliPR and the plant pathogenesis-related protein represent functional links between plant defense systems and human immune system. This family has no known function.


Pssm-ID: 214553 [Multi-domain]  Cd Length: 144  Bit Score: 67.41  E-value: 1.98e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577207   51 LLSLHNRLRS------WVQPPAADMRRLDWSDSLAQLAQARAALCGTPTPSLASGLWRTLQVGWNMQLLPagLVSFVEVV 124
Cdd:smart00198   6 ILDAHNKLRSqvaggfLAAPAASNMLKLTWDCELASSAQNWANQCPFGHSTPRPGYGENLAWWSSSTALP--DTYASAAV 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1635577207  125 SLWFAEGQRYSHAAGECA-RNATCTHYTQLVWATSSQLGCGRHLCSAGQAAIEAFVCAYSP 184
Cdd:smart00198  84 QLWYDEFQDYGYSSNTCKdTNGKIGHYTQVVWAKTYKVGCGVANCPDGTKKKTVVVCNYDP 144
CLECT_tetranectin_like cd03596
C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived ...
 304-434 2.17e-13

C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF); CLECT_tetranectin_like: C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. TN binds to plasminogen and stimulates activation of plasminogen, playing a key role in the regulation of proteolytic processes. The TN CTLD binds two calcium ions. Its calcium free form binds to various kringle-like protein ligands. Two residues involved in the coordination of calcium are critical for the binding of TN to the fourth kringle (K4) domain of plasminogen (Plg K4). TN binds the kringle 1-4 form of angiostatin (AST K1-4). AST K1-4 is a fragment of Plg, commonly found in cancer tissues. TN inhibits the binding of Plg and AST K1-4 to the extracellular matrix (EMC) of endothelial cells and counteracts the antiproliferative effects of AST K1-4 on these cells. TN also binds the tenth kringle domain of apolipoprotein (a). In addition, TN binds fibrin and complex polysaccharides in a Ca2+ dependent manner. The binding site for complex sulfated polysaccharides is N-terminal to the CTLD. TN is homotrimeric; N-terminal to the CTLD is an alpha helical domain responsible for trimerization of monomeric units. TN may modulate angiogenesis through interactions with angiostatin and coagulation through interaction with fibrin. TN may play a role in myogenesis and in bone development. Mice having a deletion in the TN gene exhibit a kyphotic spine abnormality. TN is a useful prognostic marker of certain cancer types. CLECSF1 is expressed in cartilage tissue, which is primarily intracellular matrix (ECM), and is a candidate for organizing ECM. SCGF is strongly expressed in bone marrow and is a cytokine for primitive hematopoietic progenitor cells.


Pssm-ID: 153066  Cd Length: 129  Bit Score: 66.64  E-value: 2.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577207 304 LRIDGDCFMVSSEADTYYRARMKCQRKGGVLAQIKSQKVQDILAFYLGRLETTNevidsdfetRNFWIGLTYKTAKDSFR 383
Cdd:cd03596     5 TKIHKKCYLVSEETKHYHEASEDCIARGGTLATPRDSDENDALRDYVKASVPGN---------WEVWLGINDMVAEGKWV 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1635577207 384 WATGehQAFTSFAF-----GQPDNHGFGNCVELQASAAFNWNDQRCKTRNRYICQF 434
Cdd:cd03596    76 DVNG--SPISYFNWereitAQPDGGKRENCVALSSSAQGKWFDEDCRREKPYVCEF 129
CAP cd00168
CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain ...
 51-182 3.33e-13

CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain family; The CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain, also called SCP (sperm-coating glycoprotein), is found in eukaryotes and prokaryotes. This family includes plant pathogenesis-related protein 1 (PR-1), which accumulates after infections with pathogens, and may act as an anti-fungal agent or be involved in cell wall loosening. This family also includes CRISPs (cysteine-rich secretory proteins), which combine the CAP/SCP domain with a C-terminal cysteine rich domain, and allergen 5 from vespid venom. Roles for CRISP, in response to pathogens, fertilization, and sperm maturation have been proposed. One member, Tex31 from the venom duct of Conus textile, has been shown to possess proteolytic activity sensitive to serine protease inhibitors. The human GAPR-1 protein has been reported to dimerize, and such a dimer may form an active site containing a catalytic triad. CAP/SCP has also been proposed to be a Ca++ chelating serine protease. The Ca++-chelating function would fit with various signaling processes that members of this family, such as the CRISPs, are involved in, and is supported by sequence and structural evidence of a conserved pocket containing two histidines and a glutamate. It also may explain how helothermine, a toxic peptide secreted by the beaded lizard, blocks Ca++ transporting ryanodine receptors. Little is known about the biological roles of the bacterial and archaeal CAP/SCP domains.


Pssm-ID: 349397  Cd Length: 128  Bit Score: 66.10  E-value: 3.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577207  51 LLSLHNRLRSWVQPPAADMRRLDWSDSLAQLAQARAALC--GTPTPSLASGLwrtlqvGWNMQLLPAGLvSFVEVVSLWF 128
Cdd:cd00168     4 ILDLHNSYRSSVSPPASNMPLMAWDQELADVAIGYAKDCifSHSSPTSRQLA------GENIAASSYDM-DGVAALQAWH 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1635577207 129 AEGQRYSHAAGECARNATCTHYTQLVWATSSQLGCGRHLCSAGqaaIEAFVCAY 182
Cdd:cd00168    77 NEIKNYNFGTAQPGFNSGTGHYTQMVWEKTTKLGCGVADCSDN---SKFVVCNY 127
CAP_PI15-like cd18812
CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain ...
 51-183 3.61e-13

CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of peptidase inhibitor 15 and similar proteins; This family is composed of peptidase inhibitor 15 (PI15), peptidase inhibitor R3HDML, cysteine-rich secretory protein LCCL domain-containing 1 (CRISPLD1), and cysteine-rich secretory protein LCCL domain-containing 2 (CRISPLD2). PI15 is a serine protease inhibitor which displays weak inhibitory activity against trypsin and may play a role in facial patterning during embryonic development. The PI15 gene is a candidate gene for abdominal aortic internal elastic lamina ruptures in the rat. R3HDML is a putative serine protease inhibitor, whose gene may be associated with clinical dimensions of schizophrenia. CRISPLD1 may play a role in NSCLP (nonsyndromic cleft lip with or without cleft palate) through the interaction with CRISPLD2 and folate pathway genes. plays a role in the etiology of NSCLP and is required for neural crest cell migration and cell viability during craniofacial development. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others.


Pssm-ID: 349406  Cd Length: 146  Bit Score: 66.85  E-value: 3.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577207  51 LLSLHNRLRSWVQPPAADMRRLDWSDSLAQLAQARAALC---GTPTPSLASglwrtlqVGWNMQLLPAGLVSFVEVVSLW 127
Cdd:cd18812     4 ILDYHNKLRGQVYPPAANMEYMVWDKELARSAEAWATQCiweHGPSSLLRS-------IGQNLSAHWGRYRSPVFLVKSW 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577207 128 FAEGQRYSHAA-GEC-------ARNATCTHYTQLVWATSSQLGCGRHLCSA----GQAAIEA--FVCAYS 183
Cdd:cd18812    77 YDEVKDYLFPYpRDCnphcpwrCSGPMCTHYTQMVWATSNRIGCAIHTCSNmnvwGNVWHRAvyLVCNYA 146
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 310-433 1.29e-12

C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR); CLECT_DC-SIGN_like: C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR). This group also contains proteins similar to hepatic asialoglycoprotein receptor (ASGP-R) and langerin in human. These proteins are type II membrane proteins with a CTLD ectodomain. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DC-SIGN is thought to mediate the initial contact between dendritic cells and resting T cells, and may also mediate the rolling of DCs on epithelium. DC-SIGN and DC-SIGNR bind to oligosaccharides present on human tissues, as well as, on pathogens including parasites, bacteria, and viruses. DC-SIGN and DC-SIGNR bind to HIV enhancing viral infection of T cells. DC-SIGN and DC-SIGNR are homotetrameric, and contain four CTLDs stabilized by a coiled coil of alpha helices. The hepatic ASGP-R is an endocytic recycling receptor which binds and internalizes desialylated glycoproteins having a terminal galactose or N-acetylgalactosamine residues on their N-linked carbohydrate chains, via the clathrin-coated pit mediated endocytic pathway, and delivers them to lysosomes for degradation. It has been proposed that glycoproteins bearing terminal Sia (sialic acid) alpha2, 6GalNAc and Sia alpha2, 6Gal are endogenous ligands for ASGP-R and that ASGP-R participates in regulating the relative concentration of serum glycoproteins bearing alpha 2,6-linked Sia. The human ASGP-R is a hetero-oligomer composed of two subunits, both of which are found within this group. Langerin is expressed in a subset of dendritic leukocytes, the Langerhans cells (LC). Langerin induces the formation of Birbeck Granules (BGs) and associates with these BGs following internalization. Langerin binds, in a calcium-dependent manner, to glyco-conjugates containing mannose and related sugars mediating their uptake and degradation. Langerin molecules oligomerize as trimers with three CTLDs held together by a coiled-coil of alpha helices.


Pssm-ID: 153060 [Multi-domain]  Cd Length: 126  Bit Score: 64.63  E-value: 1.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577207 310 CFMVSSEADTYYRARMKCQRKGGVLAQIKSQKVQDILafylgrlettNEVIDSDfetRNFWIGLTYKTAKDSFRWA--TG 387
Cdd:cd03590    12 CYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFI----------SKILSGN---RSYWIGLSDEETEGEWKWVdgTP 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1635577207 388 EHQAFTSFAFGQPDNHGFGN--CVELQASAAfNWNDQRCKTRNRYICQ 433
Cdd:cd03590    79 LNSSKTFWHPGEPNNWGGGGedCAELVYDSG-GWNDVPCNLEYRWICE 125
CAP_CRISPLD2 cd18816
CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain ...
 51-183 5.48e-12

CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of cysteine-rich secretory protein LCCL domain-containing 2; Cysteine-rich secretory protein LCCL domain-containing 2 (CRISPLD2) is also called cysteine-rich secretory protein 11 (CRSIP-11), LCCL domain-containing cysteine-rich secretory protein 2 (LCRISP2), or CAP and LCCL domain containing protein 2 (CAPLD2). It plays a role in the etiology of NSCLP (non-syndromic cleft lip with or without cleft palate). It is required for neural crest cell migration and cell viability during craniofacial development. The CRISPLD2 gene has been identified a glucocorticoid responsive gene that modulates cytokine function in airway smooth muscle cells. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others.


Pssm-ID: 349410  Cd Length: 146  Bit Score: 63.46  E-value: 5.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577207  51 LLSLHNRLRSWVQPPAADMRRLDWSDSLAQLAQARAALC---GTPTPSLASgLWRTLQVGWNMQLLPAGLVSfvevvsLW 127
Cdd:cd18816     4 ILQLHNKLRGQVYPSASNMEYMTWDDELERSAEAWAQQCiweHGPTSLLPS-IGQNLAVHWGRYRSPAFHVQ------SW 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577207 128 FAEGQRYSHA-AGEC-------ARNATCTHYTQLVWATSSQLGCGRHLCSA----GQAAIEA--FVCAYS 183
Cdd:cd18816    77 YDEVKDYTYPyPHECnpwcperCSGPMCTHYTQIVWATTNKVGCAVNVCRRmnvwGEIWENAvyLVCNYS 146
CAP_PRY1-like cd05384
CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain ...
 113-189 1.14e-10

CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of pathogen-related yeast 1 (PRY1) protein and similar fungal proteins; PRY1, also called pathogenesis-related protein 1, is a yeast protein that is up-regulated in core ESCRT mutants. It is a secreted protein required for efficient export of lipids such as acetylated sterols, and acts in detoxification of hydrophobic compounds. This PRY1-like group also contains fruiting body proteins SC7/14 from Schizophyllum commune. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others.


Pssm-ID: 349403  Cd Length: 129  Bit Score: 58.88  E-value: 1.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577207 113 LPAGLVSFVEVVSLWFAEGQRY-------SHAAGecarnatctHYTQLVWATSSQLGCGRHLCSAGQAAIeaFVCAYSPR 185
Cdd:cd05384    56 LALGYSSGAAAVDAWYDEISDYdysnpgfSESTG---------HFTQLVWKSTTQVGCAYKDCGGAWGLY--IVCEYDPA 124


                  ....
gi 1635577207 186 GNWE 189
Cdd:cd05384   125 GNVI 128
CAP_CRISPLD1 cd18813
CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain ...
 50-183 1.94e-10

CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of cysteine-rich secretory protein LCCL domain-containing 1; Cysteine-rich secretory protein LCCL domain-containing 1 (CRISPLD1) is also called cysteine-rich secretory protein 10 (CRISP-10), CocoaCrisp, LCCL domain-containing cysteine-rich secretory protein 1 (LCRISP1), or CAP and LCCL domain containing protein 1 (CAPLD1). CRISPLD1 is clearly distinct from CRISPs because they do not contain the 10 absolutely conserved cysteines or the ICR (ion channel regulator) domain of the CRISPs. It may play a role in NSCLP (nonsyndromic cleft lip with or without cleft palate) through the interaction with CRISPLD2 and folate pathway genes. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others.


Pssm-ID: 349407  Cd Length: 146  Bit Score: 58.86  E-value: 1.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577207  50 LLLSLHNRLRSWVQPPAADMRRLDWSDSLAQLAQARAALC--GTPTPSLASGLWRTLQVGWNMQLLPAGLVSfvevvsLW 127
Cdd:cd18813     3 LILDLHNKLRGQVYPPASNMEYMTWDVELERSAEAWAETClwEHGPAHLLPSIGQNLGAHWGRYRPPTFHVQ------AW 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577207 128 FAEGQRYSHA-AGEC-------ARNATCTHYTQLVWATSSQLGCGRHLCSA----GQAAIEA--FVCAYS 183
Cdd:cd18813    77 YDEVRDFSYPyPQECnpycpfrCSGPVCTHYTQVVWATSNRIGCAINLCHNmnvwGQIWPKAiyLVCNYS 146
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 307-434 3.10e-10

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2); CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro.


Pssm-ID: 153064 [Multi-domain]  Cd Length: 129  Bit Score: 57.77  E-value: 3.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577207 307 DGDCFMVSSEADTYYRARMKCQR--KGGVLAQIKSQKVQDILAFYlgrlettneVIDSDFETRNFWIGLTYKTAKDSFRW 384
Cdd:cd03594     9 KGNCYGYFRQPLSWSDAELFCQKygPGAHLASIHSPAEAAAIASL---------ISSYQKAYQPVWIGLHDPQQSRGWEW 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1635577207 385 ATGEHQAFTSFAFGQPDNHGfGNCVELQASAAF-NWNDQRCKTRNRYICQF 434
Cdd:cd03594    80 SDGSKLDYRSWDRNPPYARG-GYCAELSRSTGFlKWNDANCEERNPFICKY 129
CAP_PI15 cd18814
CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain ...
 51-168 3.46e-10

CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of peptidase inhibitor 15; Peptidase inhibitor 15 (PI15) is also called 25 kDa trypsin inhibitor (p25TI), cysteine-rich secretory protein 8 (CRISP-8), or SugarCrisp. It is a serine protease inhibitor which displays weak inhibitory activity against trypsin and may play a role in facial patterning during embryonic development. The PI15 gene is a candidate gene for abdominal aortic internal elastic lamina ruptures in the rat. PI15 may also participate in the regulation of drug resistance in ovarian cancer and serve as a potential target in targeted therapies. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others.


Pssm-ID: 349408  Cd Length: 146  Bit Score: 58.09  E-value: 3.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577207  51 LLSLHNRLRSWVQPPAADMRRLDWSDSLAQLAQARAALC-GTPTPSLasgLWRTLqvGWNMQLLPAGLVSFVEVVSLWFA 129
Cdd:cd18814     4 ILDYHNQVRGKVFPPAANMEYMVWDENLAKSAEAWAATCiWDHGPSY---LLRFL--GQNLSVRTGRYRSILQLVKPWYD 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1635577207 130 EGQRYSHA-AGEC-------ARNATCTHYTQLVWATSSQLGCGRHLC 168
Cdd:cd18814    79 EVKDYAFPyPQDCnprcplrCYGPMCTHYTQMVWATSNRIGCAIHTC 125
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 310-433 5.25e-09

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.


Pssm-ID: 153063  Cd Length: 116  Bit Score: 53.88  E-value: 5.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577207 310 CFMVSSEADTYYRARMKCQRKGGVLAQIKSQKVQDILAFYLGRlettnevidsdfetRNFWIGLTYKTAKDSFRWatgEH 389
Cdd:cd03593    12 CYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGS--------------SSYWIGLSREKSEKPWKW---ID 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1635577207 390 QAFTSFAFGQPDNHGFGNCVELQASAAFNwndQRCKTRNRYICQ 433
Cdd:cd03593    75 GSPLNNLFNIRGSTKSGNCAYLSSTGIYS---EDCSTKKRWICE 115
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
 311-434 7.01e-09

C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1); CLECT_collectin_like: C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CTLDs of these collectins bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, or apoptotic cells) and mediate functions associated with killing and phagocytosis. MBPs recognize high mannose oligosaccharides in a calcium dependent manner, bind to a broad range of pathogens, and trigger cell killing by activating the complement pathway. MBP also acts directly as an opsonin. SP-A and SP-D in addition to functioning as host defense components, are components of pulmonary surfactant which play a role in surfactant homeostasis. Pulmonary surfactant is a phospholipid-protein complex which reduces the surface tension within the lungs. SP-A binds the major surfactant lipid: dipalmitoylphosphatidylcholine (DPPC). SP-D binds two minor components of surfactant that contain sugar moieties: glucosylceramide and phosphatidylinositol (PI). MBP and SP-A, -D monomers are homotrimers with an N-terminal collagen region and three CTLDs. Multiple homotrimeric units associate to form supramolecular complexes. MBL deficiency results in an increased susceptibility to a large number of different infections and to inflammatory disease, such as rheumatoid arthritis.


Pssm-ID: 153061 [Multi-domain]  Cd Length: 114  Bit Score: 53.45  E-value: 7.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577207 311 FMVSSEADTYYRARMKCQRKGGVLAQIKSqkvqdilafylgrlETTNEVIDS---DFETRNFwIGLTYKTAKDSFRWATG 387
Cdd:cd03591     4 FVTNGEEKNFDDAQKLCSEAGGTLAMPRN--------------AAENAAIASyvkKGNTYAF-IGITDLETEGQFVYLDG 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1635577207 388 EHQAFTSFAFGQPDNHGFG-NCVELQASAafNWNDQRCKTRNRYICQF 434
Cdd:cd03591    69 GPLTYTNWKPGEPNNAGGGeDCVEMYTSG--KWNDVACNLTRLFVCEF 114
CLECT_chondrolectin_like cd03595
C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins ...
 310-434 7.06e-09

C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin; CLECT_chondrolectin_like: C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. CHODL is predominantly expressed in muscle cells and is associated with T-cell maturation. Various alternatively spliced isoforms have been of CHODL have been identified. The transmembrane form of CHODL is localized in the ER-Golgi apparatus. Layilin is widely expressed in different cell types. The extracellular CTLD of layilin binds hyaluronan (HA), a major constituent of the extracellular matrix (ECM). The cytoplasmic tail of layilin binds various members of the band 4.1/ERM superfamily (talin, radixin, and merlin). The ERM proteins are cytoskeleton-membrane linker molecules which link actin to receptors in the plasma membrane. Layilin co-localizes in with talin in membrane ruffles and may mediate signals from the ECM to the cell cytoskeleton.


Pssm-ID: 153065  Cd Length: 149  Bit Score: 54.51  E-value: 7.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577207 310 CFMVSSEADTYYR-----ARMKCQRKGGVLAQIKSQKVQDILAFYLGRLETTneviDSDFetrnfWIGL--------TYK 376
Cdd:cd03595    12 CYKIAYFQDSRRRlnfeeARQACREDGGELLSIESENEQKLIERFIQTLRAS----DGDF-----WIGLrrssqynvTSS 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1635577207 377 TAKDSFRWATGEHQAFTSFAFGQPdNHGFGNCVEL--QASAA--------FNWNDQRCKTRNRYICQF 434
Cdd:cd03595    83 ACSSLYYWLDGSISTFRNWYVDEP-SCGSEVCVVMyhQPSAPagqggpylFQWNDDNCNMKNNFICKY 149
CAP pfam00188
Cysteine-rich secretory protein family; This is a large family of cysteine-rich secretory ...
 52-182 1.93e-08

Cysteine-rich secretory protein family; This is a large family of cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins (CAP) that are found in a wide range of organizms, including prokaryotes and non-vertebrate eukaryotes, The nine subfamilies of the mammalian CAP 'super'family include: the human glioma pathogenesis-related 1 (GLIPR1), Golgi associated pathogenesis related-1 (GAPR1) proteins, peptidase inhibitor 15 (PI15), peptidase inhibitor 16 (PI16), cysteine-rich secretory proteins (CRISPs), CRISP LCCL domain containing 1 (CRISPLD1), CRISP LCCL domain containing 2 (CRISPLD2), mannose receptor like and the R3H domain containing like proteins. Members are most often secreted and have an extracellular endocrine or paracrine function and are involved in processes including the regulation of extracellular matrix and branching morphogenesis, potentially as either proteases or protease inhibitors; in ion channel regulation in fertility; as tumour suppressor or pro-oncogenic genes in tissues including the prostate; and in cell-cell adhesion during fertilization. The overall protein structural conservation within the CAP 'super'family results in fundamentally similar functions for the CAP domain in all members, yet the diversity outside of this core region dramatically alters the target specificity and, thus, the biological consequences. The Ca++-chelating function would fit with the various signalling processes (e.g. the CRISP proteins) that members of this family are involved in, and also the sequence and structural evidence of a conserved pocket containing two histidines and a glutamate. It also may explain how Swiss:Q91055 blocks the Ca++ transporting ryanodine receptors.


Pssm-ID: 395136  Cd Length: 117  Bit Score: 52.21  E-value: 1.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577207  52 LSLHNRLRswvqpPAADMRRLDWSDS------LAQLAQARAALCGTPTPSLASGLWRTLQVGWNmqLLPAGLVSFVEVVS 125
Cdd:pfam00188   1 LDLHNEYR-----AAAGLPPLSWDNElaaaaqDHAKYCADNGSHNHRSPYGGNIYARVVAAGYA--LGDAGPDSAEDAVD 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1635577207 126 LWFAEGQRYShaagecarnatCTHYTQLVWATSSQLGCGRHLCSAGQaaIEAFVCAY 182
Cdd:pfam00188  74 GWYDSPGTYN-----------CGHRTNLLWPKSTKVGCAVAKCGDGG--TYYFVCNY 117
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 308-432 4.44e-07

C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina; CLECT_CEL-1_like: C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CEL-1 CTLD binds three calcium ions and has a high specificity for N-acteylgalactosamine (GalNAc). CEL-1 exhibits strong cytotoxicity which is inhibited by GalNAc. This protein may play a role as a toxin defending against predation. Echinoidin is found in the coelomic fluid of the sea urchin and is specific for GalBeta1-3GalNAc. Echinoidin has a cell adhesive activity towards human cancer cells which is not mediated through the CTLD. Both CEL-1 and Echinoidin are multimeric proteins comprised of multiple dimers linked by disulfide bonds.


Pssm-ID: 153059  Cd Length: 137  Bit Score: 48.89  E-value: 4.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577207 308 GDCFMVSSEADTYYRARMKCQ-----RKGGVLAQIKSQKVQDILAFYLgrlettnEVIDSDFETRNFWIGLTYKTAKDSF 382
Cdd:cd03589    10 GYCYRFFGDRLTWEEAELRCRsfsipGLIAHLVSIHSQEENDFVYDLF-------ESSRGPDTPYGLWIGLHDRTSEGPF 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1635577207 383 RWATGEHQAFTSFAFGQPDNH-GFGNCVEL--QASAAFNWNDQRCKTRNRYIC 432
Cdd:cd03589    83 EWTDGSPVDFTKWAGGQPDNYgGNEDCVQMwrRGDAGQSWNDMPCDAVFPYIC 135
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
 308-434 3.55e-06

C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH); CLECT_EMBP_like: C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Eosinophils and basophils carry out various functions in allergic, parasitic, and inflammatory diseases. EMBP is stored in eosinophil crystalloid granules and is released upon degranulation. EMBP is also expressed in basophils. The proform of EMBP is expressed in placental X cells and breast tissue and increases significantly during human pregnancy. EMBP has cytotoxic properties and damages bacteria and mammalian cells, in vitro, as well as, helminth parasites. EMBP deposition has been observed in the inflamed tissue of allergy patients in a variety of diseases including asthma, atopic dermatitis, and rhinitis. In addition to its cytotoxic functions, EMBP activates cells and stimulates cytokine production. EMBP has been shown to bind the proteoglycan heparin. The binding site is similar to the carbohydrate binding site of other classical CTLD, such as mannose-binding protein (MBP1), however, heparin binding to EMBP is calcium ion independent. MBPH has reduced potency in cytotoxic and cytostimulatory assays compared with EMBP.


Pssm-ID: 153068  Cd Length: 117  Bit Score: 45.90  E-value: 3.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577207 308 GDCFMVSSEADTYYRARMKCQR-KGGVLAQIKSQKVQDILAFYLGRLETTNevidsdfetrnFWIG--LTYKTAKDSFRW 384
Cdd:cd03598     1 GRCYRFVKSPRTFRDAQVICRRcYRGNLASIHSFAFNYRVQRLVSTLNQAQ-----------VWIGgiITGKGRCRRFSW 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1635577207 385 ATGEHQAFTSFAFGQPDNhGFGNCVELQASAAFnWNDQRCKTRNRYICQF 434
Cdd:cd03598    70 VDGSVWNYAYWAPGQPGN-RRGHCVELCTRGGH-WRRAHCKLRRPFICSY 117
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
 311-433 4.52e-06

C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels); CLECT_selectins_like: C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. P- E- and L-sels are cell adhesion receptors that mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. L- sel is expressed constitutively on most leukocytes. P-sel is stored in the Weibel-Palade bodies of endothelial cells and in the alpha granules of platlets. E- sels are present on endothelial cells. Following platelet and/or endothelial cell activation P- sel is rapidly translocated to the cell surface and E-sel expression is induced. The initial step in leukocyte migration involves interactions of selectins with fucosylated, sialylated, and sulfated carbohydrate moieties on target ligands displayed on glycoprotein scaffolds on endothelial cells and leucocytes. A major ligand of P- E- and L-sels is PSGL-1 (P-sel glycoprotein ligand). Interactions of E- and P- sels with tumor cells may promote extravasation of cancer cells. Regulation of L-sel and P-sel function includes proteolytic shedding of the most extracellular portion (containing the CTLD) from the cell surface. Increased levels of the soluble form of P-sel in the plasma have been found in a number of diseases including coronary disease and diabetes. E- and P- sel also play roles in the development of synovial inflammation in inflammatory arthritis. Platelet P-sel, but not endothelial P-sel, plays a role in the inflammatory response and neointimal formation after arterial injury. Selectins may also function as signal-transducing receptors.


Pssm-ID: 153062  Cd Length: 115  Bit Score: 45.44  E-value: 4.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577207 311 FMVSSEADTYYRARMKCQRKGGVLAQIKSQKVqdilafylgrlettNEVIDSDFETRN---FWIGLtyKTAKDSFRW--A 385
Cdd:cd03592     3 YHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEE--------------NALLNGFALKYNlgyYWIDG--NDINNEGTWvdT 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1635577207 386 TGEHQAFTSFAFGQPDNHGFGNCVELQASAAFNWNDQRCKTRNRYICQ 433
Cdd:cd03592    67 DKKELEYKNWAPGEPNNGRNENCLEIYIKDNGKWNDEPCSKKKSAICY 114
CLECT_thrombomodulin_like cd03600
C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, ...
 306-435 6.65e-06

C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR; CLECT_thrombomodulin_like: C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In these thrombomodulin-like proteins the residues involved in coordinating Ca2+ in the classical MBP-A CTLD are not conserved. TM exerts anti-fibrinolytic and anti-inflammatory activity. TM also regulates blood coagulation in the anticoagulant protein C pathway. In this pathway, the procoagulant properties of thrombin (T) are lost when it binds TM. TM also plays a key role in tumor biology. It is expressed on endothelial cells and on several type of tumor cell including squamous cell carcinoma. Loss of TM expression correlates with advanced stage and poor prognosis. Loss of function of TM function may be associated with arterial or venous thrombosis and with late fetal loss. Soluble molecules of TM retaining the CTLD are detected in human plasma and urine where higher levels indicate injury and/or enhanced turnover of the endothelium. C1qR is expressed on endothelial cells and stem cells. It is also expressed on monocots and neutrophils, where it is subject to ectodomain shedding. Soluble forms of C1qR retaining the CTLD is detected in human plasma. C1qR modulates the phagocytosis of apoptotic cells in vivo. C1qR-deficient mice are defective in clearance of apoptotic cells in vivo. The cytoplasmic tail of C1qR, C-terminal to the CTLD of CD93, contains a PDZ binding domain which interacts with the PDZ domain-containing adaptor protein, GIPC. The juxtamembrane region of this tail interacts with the ezrin/radixin/moesin family. Endosialin functions in the growth and progression of abdominal tumors and is expressed in the stroma of several tumors.


Pssm-ID: 153070  Cd Length: 141  Bit Score: 45.50  E-value: 6.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577207 306 IDGDCFMVSSEADTYYRARMKCQRKGGVLAQIKSQKVQDILAFYLGRLETTNEVIDsdfetRNFWIGLTYKTAKDS---- 381
Cdd:cd03600     2 VSDACYTLHPQKLTFLEAQRSCIELGGNLATVRSGEEADVVSLLLAAGPGRHGRGS-----LRLWIGLQREPRQCSdpsl 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1635577207 382 ----FRWATG-EHQAFTSFAFGQPDNHGFGNCVELQASAA----FNWNDQRCKTR-NRYICQFA 435
Cdd:cd03600    77 plrgFSWVTGdQDTDFSNWLQEPAGTCTSPRCVALSAAGStpdnLKWKDGPCSARaDGYLCKFS 140
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 308-433 4.54e-05

C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins; CLECT_CSPGs: C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins (CSPGs) in human and chicken aggrecan, frog brevican, and zebra fish dermacan. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Xenopus brevican is expressed in the notochord and the brain during early embryogenesis. Zebra fish dermacan is expressed in dermal bones and may play a role in dermal bone development. CSPGs do contain LINK domain(s) which bind HA. These LINK domains are considered by one classification system to be a variety of CTLD, but are omitted from this hierarchical classification based on insignificant sequence similarity.


Pssm-ID: 153058  Cd Length: 124  Bit Score: 42.95  E-value: 4.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635577207 308 GDCFMVSSEADTYYRARMKCQRKGGVLAQIKSQKVQDilafYLGRLEttnevidSDFEtrnfWIGLTYKTAKDSFRWATG 387
Cdd:cd03588    10 GHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQE----FVNNNA-------QDYQ----WIGLNDRTIEGDFRWSDG 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1635577207 388 EHQAFTSFAFGQPDNHGFG--NCVELQASAAFNWNDQRCKTRNRYICQ 433
Cdd:cd03588    75 HPLQFENWRPNQPDNFFATgeDCVVMIWHEEGEWNDVPCNYHLPFTCK 122
CAP_GAPR1-like cd05382
CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain ...
 122-188 7.68e-05

CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of Golgi-associated plant pathogenesis-related protein 1 and similar proteins; Golgi-associated plant pathogenesis related protein 1 (GAPR1), also called Golgi-associated PR-1 protein or glioma pathogenesis-related protein 2 (GLIPR-2), forms amyloid-like fibrils in the presence of liposomes containing acidic phospholipids. It has been identified in mice as an up-regulated protein in kidney fibrosis, and is involved in epithelial to mesenchymal transition and in generating a pool of myofibroblasts contributing to fibrosis. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others.


Pssm-ID: 349401  Cd Length: 132  Bit Score: 42.20  E-value: 7.68e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1635577207 122 EVVSLWFAEGQRY-------SHAAGecarnatctHYTQLVWATSSQLGCGRhlcsAGQAAIEAFVCA-YSPRGNW 188
Cdd:cd05382    71 EAVDSWYNEIKNYnfnkpgfQSGTG---------HFTQVVWKSSTELGVGV----AKSKDGCVYVVArYSPAGNV 132
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
 331-407 4.82e-03

A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_VCBS: A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Bacterial CTLDs within this group are functionally uncharacterized. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.


Pssm-ID: 153073 [Multi-domain]  Cd Length: 118  Bit Score: 37.02  E-value: 4.82e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1635577207 331 GGVLAQIKSQKVQDILafylGRLETTNEvidsdfetrNFWIGLTYKTAKDSFRWATGEHQAFTSFAFGQPDNHGFGN 407
Cdd:cd03603    23 GGHLVTINSAEENDWL----LSNFGGYG---------ASWIGASDAATEGTWKWSDGEESTYTNWGSGEPHNNGGGN 86
 
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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