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Conserved domains on  [gi|188528609|ref|NP_003006|]
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secreted frizzled-related protein 5 precursor [Homo sapiens]

Protein Classification

CRD_SFRP5 and NTR_Sfrp1_like domain-containing protein( domain architecture ID 10165218)

CRD_SFRP5 and NTR_Sfrp1_like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CRD_SFRP5 cd07444
Cysteine-rich domain of the secreted frizzled-related protein 5 (SFRP5), a regulator of Wnt ...
 47-173 3.86e-91

Cysteine-rich domain of the secreted frizzled-related protein 5 (SFRP5), a regulator of Wnt activity; The cysteine-rich domain (CRD) is an essential part of the secreted frizzled-related Protein 5 (SFRP5), which regulates the activity of Wnt proteins, key players in a number of fundamental cellular processes such as embryogenesis and postnatal development. SFRPs antagonize the activation of Wnt signaling by binding to the CRD domains of frizzled (Fz) proteins, thereby preventing Wnt proteins from binding to these receptors. SFRPs are also known to have functions unrelated to Wnt, as enhancers of procollagen cleavage by the TLD proteinases. SFRPs and Fz proteins both contain CRD domains, but SFRPs lack the seven-pass transmembrane domain which is an integral part of Fzs.


:

Pssm-ID: 143553  Cd Length: 127  Bit Score: 267.20  E-value: 3.86e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528609  47 YSKPPQCLDIPADLPLCHTVGYKRMRLPNLLEHESLAEVKQQASSWLPLLAKRCHSDTQVFLCSLFAPVCLDRPIYPCRS 126
Cdd:cd07444    1 YSKQPQCVDIPADLPLCHNVGYKRMRLPNLLEHESMAEVKQQASSWVPLLAKRCHADTQVFLCSLFAPVCLDRPIYPCRS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 188528609 127 LCEAVRAGCAPLMEAYGFPWPEMLHCHKFPLDNDLCIAVQFGHLPAT 173
Cdd:cd07444   81 LCEAVRDSCAPVMESYGFPWPEMLHCHKFPLDNDLCIAVQFGHLQAT 127
NTR_Sfrp1_like cd03580
NTR domain, Secreted frizzled-related protein (Sfrp) 1-like subfamily; composed of proteins ...
 178-303 1.88e-54

NTR domain, Secreted frizzled-related protein (Sfrp) 1-like subfamily; composed of proteins similar to human Sfrp1, Sfrp2 and Sfrp5. Sfrps are soluble proteins containing an NTR domain C-terminal to a cysteine-rich Frizzled domain. They show diverse functions and are thought to work in Wnt signaling indirectly, as modulators or antagonists by binding Wnt ligands, and directly, via the Wnt receptor, Frizzled. They participate in regulating the patterning along the anteroposterior axis in vertebrates. Human Sfrp1 has been found frequently to be downregulated in breast cancer and is associated with disease progression and poor prognosis.


:

Pssm-ID: 239635  Cd Length: 126  Bit Score: 173.63  E-value: 1.88e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528609 178 TKICAQCEMEH-SADGLMEQMCSSDFVVKMRIKEIKIENGDRKLIGAQKKKKLLKPGPLkRKDTKRLVLHMKNGAGCPCP 256
Cdd:cd03580    1 PKVCPPCENEEeSAKTLLDNFCASDFALKVKIKEISYENGDRKVIGEKKKEILKQGPLK-KKDLKKLVLWLKNGANCPCP 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 188528609 257 QLDSLAGSFLVMGRKVDGQLLLMAVYRWDKKNKEMKFAVKFMFSYPC 303
Cdd:cd03580   80 QLDNLNGVYLVMGRKVDGKLLLTSIYKWQKKNKEFKRAVRKWKKHKC 126
 
Name Accession Description Interval E-value
CRD_SFRP5 cd07444
Cysteine-rich domain of the secreted frizzled-related protein 5 (SFRP5), a regulator of Wnt ...
 47-173 3.86e-91

Cysteine-rich domain of the secreted frizzled-related protein 5 (SFRP5), a regulator of Wnt activity; The cysteine-rich domain (CRD) is an essential part of the secreted frizzled-related Protein 5 (SFRP5), which regulates the activity of Wnt proteins, key players in a number of fundamental cellular processes such as embryogenesis and postnatal development. SFRPs antagonize the activation of Wnt signaling by binding to the CRD domains of frizzled (Fz) proteins, thereby preventing Wnt proteins from binding to these receptors. SFRPs are also known to have functions unrelated to Wnt, as enhancers of procollagen cleavage by the TLD proteinases. SFRPs and Fz proteins both contain CRD domains, but SFRPs lack the seven-pass transmembrane domain which is an integral part of Fzs.


Pssm-ID: 143553  Cd Length: 127  Bit Score: 267.20  E-value: 3.86e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528609  47 YSKPPQCLDIPADLPLCHTVGYKRMRLPNLLEHESLAEVKQQASSWLPLLAKRCHSDTQVFLCSLFAPVCLDRPIYPCRS 126
Cdd:cd07444    1 YSKQPQCVDIPADLPLCHNVGYKRMRLPNLLEHESMAEVKQQASSWVPLLAKRCHADTQVFLCSLFAPVCLDRPIYPCRS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 188528609 127 LCEAVRAGCAPLMEAYGFPWPEMLHCHKFPLDNDLCIAVQFGHLPAT 173
Cdd:cd07444   81 LCEAVRDSCAPVMESYGFPWPEMLHCHKFPLDNDLCIAVQFGHLQAT 127
NTR_Sfrp1_like cd03580
NTR domain, Secreted frizzled-related protein (Sfrp) 1-like subfamily; composed of proteins ...
 178-303 1.88e-54

NTR domain, Secreted frizzled-related protein (Sfrp) 1-like subfamily; composed of proteins similar to human Sfrp1, Sfrp2 and Sfrp5. Sfrps are soluble proteins containing an NTR domain C-terminal to a cysteine-rich Frizzled domain. They show diverse functions and are thought to work in Wnt signaling indirectly, as modulators or antagonists by binding Wnt ligands, and directly, via the Wnt receptor, Frizzled. They participate in regulating the patterning along the anteroposterior axis in vertebrates. Human Sfrp1 has been found frequently to be downregulated in breast cancer and is associated with disease progression and poor prognosis.


Pssm-ID: 239635  Cd Length: 126  Bit Score: 173.63  E-value: 1.88e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528609 178 TKICAQCEMEH-SADGLMEQMCSSDFVVKMRIKEIKIENGDRKLIGAQKKKKLLKPGPLkRKDTKRLVLHMKNGAGCPCP 256
Cdd:cd03580    1 PKVCPPCENEEeSAKTLLDNFCASDFALKVKIKEISYENGDRKVIGEKKKEILKQGPLK-KKDLKKLVLWLKNGANCPCP 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 188528609 257 QLDSLAGSFLVMGRKVDGQLLLMAVYRWDKKNKEMKFAVKFMFSYPC 303
Cdd:cd03580   80 QLDNLNGVYLVMGRKVDGKLLLTSIYKWQKKNKEFKRAVRKWKKHKC 126
FRI smart00063
Frizzled; Drosophila melanogaster frizzled mediates signalling that polarises a precursor cell ...
 56-164 1.54e-47

Frizzled; Drosophila melanogaster frizzled mediates signalling that polarises a precursor cell along the anteroposterior axis. Homologues of the N-terminal region of frizzled exist either as transmembrane or secreted molecules. Frizzled homologues are reported to be receptors for the Wnt growth factors. (Not yet in MEDLINE: the FRI domain occurs in several receptor tyrosine kinases [Xu, Y.K. and Nusse, Curr. Biol. 8 R405-R406 (1998); Masiakowski, P. and Yanopoulos, G.D., Curr. Biol. 8, R407 (1998)].


Pssm-ID: 214498  Cd Length: 113  Bit Score: 155.55  E-value: 1.54e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528609    56 IPADLPLCHTVGYKRMRLPNLLEHESLAEVKQQASSWLPLLAKRCHSDTQVFLCSLFAPVCLDR--PIYPCRSLCEAVRA 133
Cdd:smart00063   2 EPITIPLCKDLGYNLTSMPNLLGHTTQEEAGLELEQFHPLLNVQCSPDLRFFLCSVYAPICTEDlrPILPCRSLCEAARE 81

                           90       100       110
                   ....*....|....*....|....*....|.
gi 188528609   134 GCAPLMEAYGFPWPEMLHCHKFPLDNDLCIA 164
Cdd:smart00063  82 GCEPLMEKFGFPWPEFLRCDRFPVQEELCMD 112
Fz pfam01392
Fz domain; Also known as the CRD (cysteine rich domain), the C6 box in MuSK receptor. This ...
 53-156 1.46e-30

Fz domain; Also known as the CRD (cysteine rich domain), the C6 box in MuSK receptor. This domain of unknown function has been independently identified by several groups. The domain contains 10 conserved cysteines.


Pssm-ID: 460190  Cd Length: 116  Bit Score: 111.51  E-value: 1.46e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528609   53 CLDIpaDLPLCHTVGYKRMRLPNLLEHESLAEVKQQA-----SSWLPLLAKRCHSDTQVFLCSLFAPVC-----LDRPIY 122
Cdd:pfam01392   1 CEPI--TLPMCLGLGYNATVFPNLLGHQTQEEAELSLaylvlSEFEPLVDLSCSPSLRLFLCSLYFPPCtlgpsPKPVCP 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 188528609  123 PCRSLCEAVRAGCAPLME--AYGFPWPEMLHCHKFP 156
Cdd:pfam01392  79 PCRSLCEEVRYGCEPLLEeaKFGFSWPEFLDCDSLP 114
NTR pfam01759
UNC-6/NTR/C345C module; Sequence similarity between netrin UNC-6 and C345C complement protein ...
 195-292 1.01e-09

UNC-6/NTR/C345C module; Sequence similarity between netrin UNC-6 and C345C complement protein family members, and hence the existence of the UNC-6 module, was first reported in. Subsequently, many additional members of the family were identified on the basis of sequence similarity between the C-terminal domains of netrins, complement proteins C3, C4, C5, secreted frizzled-related proteins, and type I pro-collagen C-proteinase enhancer proteins (PCOLCEs), which are homologous with the N-terminal domains of tissue inhibitors of metalloproteinases (TIMPs). The TIMPs are classified as a separate family in Pfam (pfam00965). This expanded domain family has been named as the NTR module.


Pssm-ID: 396359  Cd Length: 106  Bit Score: 55.04  E-value: 1.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528609  195 EQMCS-SDFVVKMRIKEIKIENGDRKLI---------GAQkkkkllkpgplkRKDTKRLVLHMKNGAgCPCPQLDsLAGS 264
Cdd:pfam01759   1 KKACKgSDYVYKVKVLSVEEEGSFDKYTvkvkevlkeGTD------------KIQRGKVRLFLKRGD-CRCPQLR-LGKE 66

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 188528609  265 FLVMGRKVD-----------GQLLLMAVYRWDKKNKEMK 292
Cdd:pfam01759  67 YLIMGKVGDlegrgryvldkNSWVEPWPTKWECKLRELQ 105
C345C smart00643
Netrin C-terminal Domain;
194-289 1.58e-09

Netrin C-terminal Domain;


Pssm-ID: 214759  Cd Length: 114  Bit Score: 54.68  E-value: 1.58e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528609   194 MEQMCSS--DFVVKMRIKEIKIENGDRKLI---------GaqkkkkllkpgpLKRKDTKRLVLHMKNG-AGCPCPQLDSL 261
Cdd:smart00643   1 LEKACKSdvDYVYKVKVLSVEEEGGFDKYTvkileviksG------------TDELVRGKNKLRVFISrASCRCPLLLKL 68

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 188528609   262 AGSFLVMGRKVD-------GQLLLMA---VYRWDKKNK 289
Cdd:smart00643  69 GKSYLIMGKSGDlwdakgrGQYVLGKnswVEEWPTEEE 106
 
Name Accession Description Interval E-value
CRD_SFRP5 cd07444
Cysteine-rich domain of the secreted frizzled-related protein 5 (SFRP5), a regulator of Wnt ...
 47-173 3.86e-91

Cysteine-rich domain of the secreted frizzled-related protein 5 (SFRP5), a regulator of Wnt activity; The cysteine-rich domain (CRD) is an essential part of the secreted frizzled-related Protein 5 (SFRP5), which regulates the activity of Wnt proteins, key players in a number of fundamental cellular processes such as embryogenesis and postnatal development. SFRPs antagonize the activation of Wnt signaling by binding to the CRD domains of frizzled (Fz) proteins, thereby preventing Wnt proteins from binding to these receptors. SFRPs are also known to have functions unrelated to Wnt, as enhancers of procollagen cleavage by the TLD proteinases. SFRPs and Fz proteins both contain CRD domains, but SFRPs lack the seven-pass transmembrane domain which is an integral part of Fzs.


Pssm-ID: 143553  Cd Length: 127  Bit Score: 267.20  E-value: 3.86e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528609  47 YSKPPQCLDIPADLPLCHTVGYKRMRLPNLLEHESLAEVKQQASSWLPLLAKRCHSDTQVFLCSLFAPVCLDRPIYPCRS 126
Cdd:cd07444    1 YSKQPQCVDIPADLPLCHNVGYKRMRLPNLLEHESMAEVKQQASSWVPLLAKRCHADTQVFLCSLFAPVCLDRPIYPCRS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 188528609 127 LCEAVRAGCAPLMEAYGFPWPEMLHCHKFPLDNDLCIAVQFGHLPAT 173
Cdd:cd07444   81 LCEAVRDSCAPVMESYGFPWPEMLHCHKFPLDNDLCIAVQFGHLQAT 127
CRD_SFRP1 cd07443
Cysteine-rich domain of the secreted frizzled-related protein 1 (SFRP1), a regulator of Wnt ...
 47-165 1.95e-67

Cysteine-rich domain of the secreted frizzled-related protein 1 (SFRP1), a regulator of Wnt activity; The cysteine-rich domain (CRD) is an essential part of the secreted frizzled-related protein 1 (SFRP1), which regulates the activity of Wnt proteins, key players in a number of fundamental cellular processes such as embryogenesis and postnatal development. SFRPs antagonize the activation of Wnt signaling by binding to the CRDs domains of frizzled (Fz) proteins, thereby preventing Wnt proteins from binding to these receptors. SFRPs are also known to have functions unrelated to Wnt, as enhancers of procollagen cleavage by the TLD proteinases. SFRPs and Fz proteins both contain CRD domains, but SFRPs lack the seven-pass transmembrane domain which is an integral part of Fzs. SFRP1 is expressed in many tissues and is involved in the regulation of Wnt signaling in osteoblasts, leading to enhanced trabecular bone formation in adults; it has also been shown to control the growth of retinal ganglion cell axons and the elongation of the antero-posterior axis.


Pssm-ID: 143552  Cd Length: 124  Bit Score: 206.67  E-value: 1.95e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528609  47 YSKPPQCLDIPADLPLCHTVGYKRMRLPNLLEHESLAEVKQQASSWLPLLAKRCHSDTQVFLCSLFAPVCLDRPIYPCRS 126
Cdd:cd07443    1 YTKPPQCVDIPADLRLCHNVGYKKMVLPNLLDHETMAEVKQQASSWVPLLNKNCHKGTQVFLCSLFAPVCLDRPVYPCRW 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 188528609 127 LCEAVRAGCAPLMEAYGFPWPEMLHCHKFPLDnDLCIAV 165
Cdd:cd07443   81 LCEAVRDSCEPVMQFFGFYWPEMLKCDKFPEG-EVCIAM 118
CRD_crescent cd07453
Cysteine-rich domain of the crescent protein; The cysteine-rich domain (CRD) is an essential ...
 53-187 3.42e-63

Cysteine-rich domain of the crescent protein; The cysteine-rich domain (CRD) is an essential part of the crescent protein, a member of the secreted frizzled-related protein (SFRP) family, which regulates convergent extension movements (CEMs) during gastrulation and neurulation. Xenopus laevis crescent efficiently forms inhibitory complexes with Wnt5a and Wnt11, but this effect is cancelled in the presence of another member of the SFRP family, Frzb1. A potential role for Crescent in head formation is to regulate a non-canonical Wnt pathway positively in the adjacent posterior mesoderm, and negatively in the overlying anterior neuroectoderm.


Pssm-ID: 143562 [Multi-domain]  Cd Length: 135  Bit Score: 196.32  E-value: 3.42e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528609  53 CLDIPADLPLCHTVGYKRMRLPNLLEHESLAEVKQQASSWLPLLAKRCHSDTQVFLCSLFAPVCLDRPIYPCRSLCEAVR 132
Cdd:cd07453    3 CMRIPKSMALCYDIGYSEMRIPNLLEHETMAEVIQQSSSWLPLLARECHPDARIFLCSLFAPICWDRPIYPCRSLCEAVR 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 188528609 133 AGCAPLMEAYGFPWPEMLHCHKFPLDNDLCIAVQFghLPATAPPVTKICAQCEME 187
Cdd:cd07453   83 SSCAPLMACYGYPWPEILHCDKFPVDHDLCISPQF--IDTLSPERVKPRASCEDC 135
CRD_SFRP2 cd07446
Cysteine-rich domain of the secreted frizzled-related protein 2 (SFRP2), a regulator of Wnt ...
 49-163 1.68e-56

Cysteine-rich domain of the secreted frizzled-related protein 2 (SFRP2), a regulator of Wnt activity; The cysteine-rich-domain (CRD) is an essential part of the secreted frizzled related protein 2 (SFRP2), which regulates the activity of Wnt proteins, key players in a number of fundamental cellular processes such as embryogenesis and postnatal development. SFRPs antagonize the activation of Wnt signaling by binding to CRD domains of frizzled (Fz) proteins, thereby preventing Wnt proteins from binding to these receptors. SFRPs and Fz proteins both contain CRD domains, but SFRPs lack the seven-pass transmembrane domain which is an integral part of Fzs. As a Wnt antagonist, SFRP2 regulates Nkx2.2 expression in the ventral spinal cord and anteroposterior axis elongation. SFRP2 also has a Wnt-independent function as an enhancer of procollagen cleavage by the TLD proteinases. SFRP2 binds both procollagen and TLD, thus facilitating the enzymatic reaction by bringing together the proteinase and its substrate.


Pssm-ID: 143555  Cd Length: 128  Bit Score: 178.95  E-value: 1.68e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528609  49 KPPQCLDIPADLPLCHTVGYKRMRLPNLLEHESLAEVKQQASSWLPLLAKRCHSDTQVFLCSLFAPVC---LDRPIYPCR 125
Cdd:cd07446    1 KKSNCKPIPANMLLCHGIEYTNMRLPNLLGHETMKEVLQQAGSWIPLVQKQCHPDTKKFLCSLFAPVClddLDEAIQPCR 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 188528609 126 SLCEAVRAGCAPLMEAYGFPWPEMLHCHKFPLDNDLCI 163
Cdd:cd07446   81 SLCEAVKDGCAPVMSAFGFPWPDMLDCTRFPLDNDLCI 118
NTR_Sfrp1_like cd03580
NTR domain, Secreted frizzled-related protein (Sfrp) 1-like subfamily; composed of proteins ...
 178-303 1.88e-54

NTR domain, Secreted frizzled-related protein (Sfrp) 1-like subfamily; composed of proteins similar to human Sfrp1, Sfrp2 and Sfrp5. Sfrps are soluble proteins containing an NTR domain C-terminal to a cysteine-rich Frizzled domain. They show diverse functions and are thought to work in Wnt signaling indirectly, as modulators or antagonists by binding Wnt ligands, and directly, via the Wnt receptor, Frizzled. They participate in regulating the patterning along the anteroposterior axis in vertebrates. Human Sfrp1 has been found frequently to be downregulated in breast cancer and is associated with disease progression and poor prognosis.


Pssm-ID: 239635  Cd Length: 126  Bit Score: 173.63  E-value: 1.88e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528609 178 TKICAQCEMEH-SADGLMEQMCSSDFVVKMRIKEIKIENGDRKLIGAQKKKKLLKPGPLkRKDTKRLVLHMKNGAGCPCP 256
Cdd:cd03580    1 PKVCPPCENEEeSAKTLLDNFCASDFALKVKIKEISYENGDRKVIGEKKKEILKQGPLK-KKDLKKLVLWLKNGANCPCP 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 188528609 257 QLDSLAGSFLVMGRKVDGQLLLMAVYRWDKKNKEMKFAVKFMFSYPC 303
Cdd:cd03580   80 QLDNLNGVYLVMGRKVDGKLLLTSIYKWQKKNKEFKRAVRKWKKHKC 126
FRI smart00063
Frizzled; Drosophila melanogaster frizzled mediates signalling that polarises a precursor cell ...
 56-164 1.54e-47

Frizzled; Drosophila melanogaster frizzled mediates signalling that polarises a precursor cell along the anteroposterior axis. Homologues of the N-terminal region of frizzled exist either as transmembrane or secreted molecules. Frizzled homologues are reported to be receptors for the Wnt growth factors. (Not yet in MEDLINE: the FRI domain occurs in several receptor tyrosine kinases [Xu, Y.K. and Nusse, Curr. Biol. 8 R405-R406 (1998); Masiakowski, P. and Yanopoulos, G.D., Curr. Biol. 8, R407 (1998)].


Pssm-ID: 214498  Cd Length: 113  Bit Score: 155.55  E-value: 1.54e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528609    56 IPADLPLCHTVGYKRMRLPNLLEHESLAEVKQQASSWLPLLAKRCHSDTQVFLCSLFAPVCLDR--PIYPCRSLCEAVRA 133
Cdd:smart00063   2 EPITIPLCKDLGYNLTSMPNLLGHTTQEEAGLELEQFHPLLNVQCSPDLRFFLCSVYAPICTEDlrPILPCRSLCEAARE 81

                           90       100       110
                   ....*....|....*....|....*....|.
gi 188528609   134 GCAPLMEAYGFPWPEMLHCHKFPLDNDLCIA 164
Cdd:smart00063  82 GCEPLMEKFGFPWPEFLRCDRFPVQEELCMD 112
CRD_FZ cd07066
CRD_domain cysteine-rich domain, also known as Fz (frizzled) domain; CRD_FZ is an essential ...
 52-166 4.47e-40

CRD_domain cysteine-rich domain, also known as Fz (frizzled) domain; CRD_FZ is an essential component of a number of cell surface receptors, which are involved in multiple signal transduction pathways, particularly in modulating the activity of the Wnt proteins, which play a fundamental role in the early development of metazoans. CRD is also found in secreted frizzled related proteins (SFRPs), which lack the transmembrane segment found in the frizzled protein. The CRD domain is also present in the alpha-1 chain of mouse type XVIII collagen, in carboxypeptidase Z, several receptor tyrosine kinases, and the mosaic transmembrane serine protease corin. The CRD domain is well conserved in metazoans - 10 frizzled proteins have been identified in mammals, 4 in Drosophila and 3 in Caenorhabditis elegans. CRD domains have also been identified in multiple tandem copies in a Dictyostelium discoideum protein. Very little is known about the mechanism by which CRD domains interact with their ligands. The domain contains 10 conserved cysteines.


Pssm-ID: 143549  Cd Length: 119  Bit Score: 136.48  E-value: 4.47e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528609  52 QCLDIPadLPLCHTVGYKRMRLPNLLEHESLAEVKQQASSWLPLLAKRCHSDTQVFLCSLFAPVCL---DRPIYPCRSLC 128
Cdd:cd07066    1 KCEPIP--LPLCRGLPYNTTRFPNLLGHESQEEAEQELESFTPLVNSGCHPDLRFFLCSLYFPECTpdgDRPIPPCRSLC 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 188528609 129 EAVRAGCAPLMEAYGFPWPEMLHCHKFPLDN--DLCIAVQ 166
Cdd:cd07066   79 EEVRDSCEPLMLAFGFPWPEPLDCDRFPDSNeeGLCISPP 118
CRD_sizzled cd07452
Cysteine-rich domain of the sizzled protein; The cysteine-rich domain (CRD) is an essential ...
 52-164 1.74e-38

Cysteine-rich domain of the sizzled protein; The cysteine-rich domain (CRD) is an essential part of the sizzled protein, which regulates bone morphogenetic protein (Bmp) signaling by stabilizing chordin, and plays a critical role in the patterning of vertebrate and invertebrate embryos. Sizzled also functions in the ventral region as a Wnt inhibitor and modulates canonical Wnt signaling. Sizzled proteins belong to the secreted frizzled-related protein family (SFRP), and have be identified in the genomes of birds, fishes and frogs, but not mammals.


Pssm-ID: 143561  Cd Length: 141  Bit Score: 133.08  E-value: 1.74e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528609  52 QCLDIPADLPLCHTVGYKRMRLPNLLEHESLAEVKQQASSWLPLLAKRCHSDTQVFLCSLFAPVCLDRPIYPCRSLCEAV 131
Cdd:cd07452    8 KCVPIPPEMSMCQDVGYSEMRLPNLLGHTSMAEVVPKSADWQTLLHTGCHPHARTFLCSLFAPVCLDTFIQPCRSMCVAV 87

                         90       100       110
                 ....*....|....*....|....*....|...
gi 188528609 132 RAGCAPLMEAYGFPWPEMLHCHKFPLDNDLCIA 164
Cdd:cd07452   88 RDSCAPVLACHGHSWPESLDCDRFPAGEDMCLA 120
CRD_FZ4 cd07448
Cysteine-rich Wnt-binding domain of the frizzled 4 (Fz4) receptor; The cysteine-rich domain ...
 57-160 4.48e-33

Cysteine-rich Wnt-binding domain of the frizzled 4 (Fz4) receptor; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 4 (Fz4) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and the Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Frizzled 4 (Fz4) activates the Ca(2+)/calmodulin-dependent protein kinase II and protein kinase C of the Wnt/Ca(2+) signaling pathway during retinal angiogenesis. Mutations in Fz4 lead to familial exudative vitreoretinopathy (FEVR), a hereditary ocular disorder characterized by failure of the peripheral retinal vascularization. In addition, the interplay between Fz4 and norrin as a receptor-ligand pair plays an important role in vascular development in the retina and inner ear in a Wnt-independent manner.


Pssm-ID: 143557  Cd Length: 126  Bit Score: 118.72  E-value: 4.48e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528609  57 PADLPLCHTVGYKRMRLPNLLEHESLAEVKQQASSWLPLLAKRCHSDTQVFLCSLFAPVC---LDRPIYPCRSLCEAVRA 133
Cdd:cd07448    6 PIRIEMCQGLGYNVTRMPNLVGHELQTDAELQLQTFTPLIQYGCSSQLKFFLCSVYVPMCtekVPVPIGPCRPLCLSVKK 85

                         90       100
                 ....*....|....*....|....*..
gi 188528609 134 GCAPLMEAYGFPWPEMLHCHKFPLDND 160
Cdd:cd07448   86 RCLPVLKEFGFPWPEALNCSKFPPQNN 112
CRD_FZ1_like cd07458
Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 1; The cysteine-rich ...
 57-164 3.95e-31

Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 1; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 1 (Fz1), frizzled 2 (Fz2), and frizzled 7 (Fz7) receptors, and similar proteins. This domain is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. The CRD domain is well conserved in metazoans - 10 frizzled proteins have been identified in mammals, 4 in Drosophila and 3 in Caenorhabditis elegans. Very little is known about the mechanism by which CRD domains interact with their ligands. The domain contains 10 conserved cysteines.


Pssm-ID: 143567  Cd Length: 119  Bit Score: 113.28  E-value: 3.95e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528609  57 PADLPLCHTVGYKRMRLPNLLEHESLAEVKQQASSWLPLLAKRCHSDTQVFLCSLFAPVC--LDRPIYPCRSLCEAVRAG 134
Cdd:cd07458    5 PITIPLCTDIPYNMTIFPNLLGHTKQEDAGLEVHQFYPLVKVQCSPDLKFFLCSVYAPVCtvLERPIPPCRSLCESARQG 84

                         90       100       110
                 ....*....|....*....|....*....|..
gi 188528609 135 CAPLMEAYGFPWPEMLHCHKFPLDN--DLCIA 164
Cdd:cd07458   85 CEALMNKFGFQWPESLDCEKFPVHGagDLCVG 116
Fz pfam01392
Fz domain; Also known as the CRD (cysteine rich domain), the C6 box in MuSK receptor. This ...
 53-156 1.46e-30

Fz domain; Also known as the CRD (cysteine rich domain), the C6 box in MuSK receptor. This domain of unknown function has been independently identified by several groups. The domain contains 10 conserved cysteines.


Pssm-ID: 460190  Cd Length: 116  Bit Score: 111.51  E-value: 1.46e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528609   53 CLDIpaDLPLCHTVGYKRMRLPNLLEHESLAEVKQQA-----SSWLPLLAKRCHSDTQVFLCSLFAPVC-----LDRPIY 122
Cdd:pfam01392   1 CEPI--TLPMCLGLGYNATVFPNLLGHQTQEEAELSLaylvlSEFEPLVDLSCSPSLRLFLCSLYFPPCtlgpsPKPVCP 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 188528609  123 PCRSLCEAVRAGCAPLME--AYGFPWPEMLHCHKFP 156
Cdd:pfam01392  79 PCRSLCEEVRYGCEPLLEeaKFGFSWPEFLDCDSLP 114
CRD_FZ8 cd07461
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 8 (Fz8) receptor; The cysteine-rich ...
 49-156 2.99e-30

Cysteine-rich Wnt-binding domain (CRD) of the frizzled 8 (Fz8) receptor; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 8 (Fz8) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Xenopus Fz8 is important in Wnt/beta-catenin signaling pathways controlling the transcriptional activation of target genes Siamois and Xnr3 in the animal caps of late blastula.


Pssm-ID: 143570  Cd Length: 125  Bit Score: 111.23  E-value: 2.99e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528609  49 KPPQCLDIPadLPLCHTVGYKRMRLPNLLEHESLAEVKQQASSWLPLLAKRCHSDTQVFLCSLFAPVCLD---RPIYPCR 125
Cdd:cd07461    1 KELQCQEIT--VPLCKGIGYNYTYMPNQFNHDTQDEAGLEVHQFWPLVEIQCSPDLKFFLCSMYTPICLEdykKPLPPCR 78

                         90       100       110
                 ....*....|....*....|....*....|.
gi 188528609 126 SLCEAVRAGCAPLMEAYGFPWPEMLHCHKFP 156
Cdd:cd07461   79 SVCERAKAGCAPLMRQYGFPWPDRMRCDLLP 109
CRD_FZ9_like cd07457
Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 9; The cysteine-rich ...
 57-164 4.15e-30

Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 9; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 9 (Fz9) and frizzled 10 (Fz10) receptors, and similar proteins. This domain is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. The CRD domain is well conserved in metazoans - 10 frizzled proteins have been identified in mammals, 4 in Drosophila and 3 in Caenorhabditis elegans. Very little is known about the mechanism by which CRD domains interact with their ligands. The domain contains 10 conserved cysteines.


Pssm-ID: 143566  Cd Length: 121  Bit Score: 110.66  E-value: 4.15e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528609  57 PADLPLCHTVGYKRMRLPNLLEHESLAEVKQQASSWLPLLAKRCHSDTQVFLCSLFAPVCLDR---PIYPCRSLCEAVRA 133
Cdd:cd07457    5 RITIPMCQGIGYNMTRMPNLLGHESQSEAAISIHEFAPLVQYGCAEHLRFFLCSLYAPMCTEQvsiPIPACRSMCEQARD 84

                         90       100       110
                 ....*....|....*....|....*....|....
gi 188528609 134 GCAPLMEAYGFPWPEMLHCHKFPLDND---LCIA 164
Cdd:cd07457   85 KCSPIMEQFSFSWPDSLDCDRLPRKNDpkdLCME 118
CRD_FZ5_like cd07456
Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 5; The cysteine-rich ...
 53-164 4.22e-30

Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 5; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 5 (Fz5) and frizzled 8 (Fz8) receptors, and similar proteins. This domain is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. The CRD domain is well conserved in metazoans - 10 frizzled proteins have been identified in mammals, 4 in Drosophila and 3 in Caenorhabditis elegans. Very little is known about the mechanism by which CRD domains interact with their ligands. The domain contains 10 conserved cysteines.


Pssm-ID: 143565  Cd Length: 120  Bit Score: 110.57  E-value: 4.22e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528609  53 CLDIpaDLPLCHTVGYKRMRLPNLLEHESLAEVKQQASSWLPLLAKRCHSDTQVFLCSLFAPVCL---DRPIYPCRSLCE 129
Cdd:cd07456    2 CEEI--TIPMCKGIGYNMTYMPNQFNHDTQEEAGLEVHQFWPLVEIQCSPDLKFFLCSMYTPICLedyDKPLPPCRSVCE 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 188528609 130 AVRAGCAPLMEAYGFPWPEMLHCHKFPL---DNDLCIA 164
Cdd:cd07456   80 RARDGCAPIMRQYGFAWPERMSCDALPEggdPDNLCMD 117
CRD_FZ9 cd07463
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 9 (Fz9) receptor; The cysteine-rich ...
 57-163 1.14e-29

Cysteine-rich Wnt-binding domain (CRD) of the frizzled 9 (Fz9) receptor; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 9 (Fz9) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Fz9 may play a signaling role in lymphoid development and maturation, particularly at points where B cells undergo self-renewal prior to further differentiation.


Pssm-ID: 143572  Cd Length: 127  Bit Score: 109.73  E-value: 1.14e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528609  57 PADLPLCHTVGYKRMRLPNLLEHESLAEVKQQASSWLPLLAKRCHSDTQVFLCSLFAPVCLDR---PIYPCRSLCEAVRA 133
Cdd:cd07463    7 PVVIPMCRGIGYNLTRMPNFLGHDSQREAAIKLNEFAPLVEYGCHVHLRFFLCSLYAPMCTDQvstSIPACRPMCEQARQ 86

                         90       100       110
                 ....*....|....*....|....*....|...
gi 188528609 134 GCAPLMEAYGFPWPEMLHCHKFPLDND---LCI 163
Cdd:cd07463   87 KCSPIMEQFNFGWPESLDCSRLPTRNDpnaLCM 119
CRD_FZ5 cd07460
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 5 (Fz5) receptor.proteins; The ...
 49-163 9.00e-29

Cysteine-rich Wnt-binding domain (CRD) of the frizzled 5 (Fz5) receptor.proteins; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 5 (Fz5) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Fz5 plays critical regulating roles in the yolk sac and placental angiogenesis, in the maturation of the Paneth cell phenotype, in governing the neural potential of progenitors in the developing retina, and in neuronal survival in the parafascicular nucleus.


Pssm-ID: 143569 [Multi-domain]  Cd Length: 127  Bit Score: 107.41  E-value: 9.00e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528609  49 KPPQCLDIpaDLPLCHTVGYKRMRLPNLLEHESLAEVKQQASSWLPLLAKRCHSDTQVFLCSLFAPVCLD---RPIYPCR 125
Cdd:cd07460    1 KALVCQEI--TVPMCKGIGYNLTYMPNQFNHDTQDEAGLEVHQFWPLVEIQCSPDLRFFLCSMYTPICLPdyrKPLPPCR 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 188528609 126 SLCEAVRAGCAPLMEAYGFPWPEMLHCHKFPLDND---LCI 163
Cdd:cd07460   79 SVCERAKAGCSPLMRQYGFAWPERMNCDRLPVLGDpetLCM 119
CRD_FZ10 cd07462
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 10 (Fz10) receptor; The cysteine-rich ...
 57-163 5.39e-28

Cysteine-rich Wnt-binding domain (CRD) of the frizzled 10 (Fz10) receptor; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 10 (Fz10) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. The cellular functon of Fz10 is unknown.


Pssm-ID: 143571  Cd Length: 127  Bit Score: 105.49  E-value: 5.39e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528609  57 PADLPLCHTVGYKRMRLPNLLEHESLAEVKQQASSWLPLLAKRCHSDTQVFLCSLFAPVCLDR---PIYPCRSLCEAVRA 133
Cdd:cd07462    7 PIEIPMCKDIGYNMTRMPNLMGHENQREAAIQLHEFAPLVEYGCHSHLKFFLCSLYAPMCTEQvstPIPACRVMCEQARL 86

                         90       100       110
                 ....*....|....*....|....*....|...
gi 188528609 134 GCAPLMEAYGFPWPEMLHCHKFPLDND---LCI 163
Cdd:cd07462   87 KCSPIMEQFNFKWPDSLDCSKLPNKNDpnyLCM 119
CRD_FZ7 cd07466
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 7 (Fz7) receptor; The cysteine-rich ...
 57-157 1.89e-25

Cysteine-rich Wnt-binding domain (CRD) of the frizzled 7 (Fz7) receptor; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 7 (Fz7) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Xenopus Fz7 is important in Wnt/beta-catenin signaling pathways controlling the transcriptional activation of target genes Siamois and Xnr3 in the animal caps of late blastula.


Pssm-ID: 143575 [Multi-domain]  Cd Length: 125  Bit Score: 98.62  E-value: 1.89e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528609  57 PADLPLCHTVGYKRMRLPNLLEHESLAEVKQQASSWLPLLAKRCHSDTQVFLCSLFAPVC--LDRPIYPCRSLCEAVRAG 134
Cdd:cd07466    7 PISIPLCTDIAYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSPELKFFLCSMYAPVCtvLEQAIPPCRSLCERARQG 86

                         90       100
                 ....*....|....*....|...
gi 188528609 135 CAPLMEAYGFPWPEMLHCHKFPL 157
Cdd:cd07466   87 CEALMNKFGFQWPERLRCENFPV 109
CRD_FZ1 cd07465
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 1 (Fz1) receptor; The cysteine-rich ...
 57-164 5.04e-25

Cysteine-rich Wnt-binding domain (CRD) of the frizzled 1 (Fz1) receptor; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 1 (Fz1) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata.


Pssm-ID: 143574  Cd Length: 127  Bit Score: 97.43  E-value: 5.04e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528609  57 PADLPLCHTVGYKRMRLPNLLEHESLAEVKQQASSWLPLLAKRCHSDTQVFLCSLFAPVC--LDRPIYPCRSLCEAVRAG 134
Cdd:cd07465    7 PISIPLCTDIAYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSAELKFFLCSMYAPVCtvLEQALPPCRSLCERARQG 86

                         90       100       110
                 ....*....|....*....|....*....|..
gi 188528609 135 CAPLMEAYGFPWPEMLHCHKFPLD--NDLCIA 164
Cdd:cd07465   87 CEALMNKFGFQWPDTLRCEKFPVHgaGELCVG 118
CRD_FZ2 cd07464
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 2 (Fz2) receptor; The cysteine-rich ...
 57-156 1.24e-24

Cysteine-rich Wnt-binding domain (CRD) of the frizzled 2 (Fz2) receptor; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 2 (Fz2) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Fz2 is involved in the Wnt/beta-catenin signaling pathway and in the activation of protein kinase C and calcium/calmodulin-dependent protein kinase (CaM kinase).


Pssm-ID: 143573  Cd Length: 127  Bit Score: 96.31  E-value: 1.24e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528609  57 PADLPLCHTVGYKRMRLPNLLEHESLAEVKQQASSWLPLLAKRCHSDTQVFLCSLFAPVC--LDRPIYPCRSLCEAVRAG 134
Cdd:cd07464    7 PISIPLCTDIAYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSLELRFFLCSMYAPVCtvLEQAIPPCRSICERARQG 86

                         90       100
                 ....*....|....*....|..
gi 188528609 135 CAPLMEAYGFPWPEMLHCHKFP 156
Cdd:cd07464   87 CEALMNKFGFQWPERLRCENFP 108
CRD_SFRP3 cd07441
Cysteine-rich domain of the secreted frizzled-related protein 3 (SFRP3, alias FRZB), a Wnt ...
 57-164 1.17e-21

Cysteine-rich domain of the secreted frizzled-related protein 3 (SFRP3, alias FRZB), a Wnt antagonist; The cysteine-rich domain (CRD) is an essential part of the secreted frizzled-related protein 3 (SFRP3, alias FRZB), which plays important roles in embryogenesis and postnatal development as an antagonist of Wnt proteins, key players in a number of fundamental cellular processes. SFRPs antagonize the activation of Wnt signaling by binding to the CRD domains of frizzled proteins (Fz), thereby preventing Wnt proteins from binding to these receptors. SFRPs are also known to have functions unrelated to Wnt, as enhancers of procollagen cleavage by the TLD proteinases. SFRPs and Fz proteins both contain CRD domains, but SFRPs lack the seven-pass transmembrane domain which is an integral part of Fzs. SFRP3 regulates Wnt signaling activity in bone development and homeostasis. It is also involved in the control of planar cell polarity.


Pssm-ID: 143550  Cd Length: 126  Bit Score: 88.57  E-value: 1.17e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528609  57 PADLPLCHTVGYKRMRLPNLLEHESLAEVKQQASSWLPLLAKRCHSDTQVFLCSLFAPVCL----DRPIYPCRSLCEAVR 132
Cdd:cd07441    6 PVRIPMCKSMPWNMTKMPNHLHHSTQANAVLAIEQFEGLLGTQCSPDLLFFLCAMYAPICTidfqHEPIKPCKSVCERAR 85

                         90       100       110
                 ....*....|....*....|....*....|...
gi 188528609 133 AGCAPLMEAYGFPWPEMLHCHKFPL-DNDLCIA 164
Cdd:cd07441   86 AGCEPVLIRYRHTWPESLACEELPVyDRGVCIS 118
CRD_FZ3 cd07449
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 3 (Fz3) receptor; The cysteine-rich ...
 57-156 1.72e-20

Cysteine-rich Wnt-binding domain (CRD) of the frizzled 3 (Fz3) receptor; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 3 (Fz3) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Fz3 plays a vital role in the anterior-posterior guidance of commissural axons. Knockout mice without Fz3 show defects in fiber tracts in the rostral CNS.


Pssm-ID: 143558 [Multi-domain]  Cd Length: 127  Bit Score: 85.45  E-value: 1.72e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528609  57 PADLPLCHTVGYKRMRLPNLLEHESLAEVKQQASSWLPLLAKRCHSDTQVFLCSLFAPVCLD--RPIYPCRSLCEAVRAG 134
Cdd:cd07449    7 PITLRMCQDLPYNTTFMPNLLNHYDQQTAALAMEPFHPMVNLECSRDFRPFLCALYAPVCMEygRVTLPCRRLCQRAYSE 86

                         90       100
                 ....*....|....*....|..
gi 188528609 135 CAPLMEAYGFPWPEMLHCHKFP 156
Cdd:cd07449   87 CSKLMEMFGVPWPEDMECSRFP 108
CRD_LIN_17 cd07454
Cysteine-rich domain (CRD) of LIN_17; A cysteine-rich domain (CRD) is an essential component ...
 56-163 3.65e-20

Cysteine-rich domain (CRD) of LIN_17; A cysteine-rich domain (CRD) is an essential component of a number of cell surface receptors, which are involved in multiple signal transduction pathways, particularly in modulating the activity of the Wnt proteins, which play a fundamental role in the early development of metazoans. CRD is also found in secreted frizzled related proteins (SFRPs), which lack the transmembrane segment found in the frizzled protein. The CRD domain is also present in the alpha-1 chain of mouse type XVIII collagen, in carboxypeptidase Z, several receptor tyrosine kinases, and the mosaic transmembrane serine protease corin. The CRD domain is well conserved in metazoans - 10 frizzled proteins have been identified in mammals, 4 in Drosophila and 3 in Caenorhabditis elegans. CRD domains have also been identified in multiple tandem copies in a Dictyostelium discoideum protein. Very little is known about the mechanism by which CRD domains interact with their ligands. The domain contains 10 conserved cysteines. The protein lin-17 is involved in cell type specification during Caenorhabditis elegans vulval development.


Pssm-ID: 143563  Cd Length: 124  Bit Score: 84.45  E-value: 3.65e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528609  56 IPADLPLCHTVGYKRMRLPNLLEHESLAEVKQQASSWLPLLAKRCHSDTQVFLCSLFAPVCLDR---PIYPCRSLCEAVR 132
Cdd:cd07454    6 IPIDIELCKDLPYNYTYFPNTILHNDQHTLQTHTEHFKPLMKTKCHPHIHFFICSVFAPMCPIGmpqAVTSCKSVCEQVK 85

                         90       100       110
                 ....*....|....*....|....*....|.
gi 188528609 133 AGCAPLMEAYGFPWPEMLHCHKFPLDNDLCI 163
Cdd:cd07454   86 ADCFSILEEFGIGWPEPLNCAQFPDPPELCM 116
CRD_SFRP4 cd07442
Cysteine-rich domain of the secreted frizzled-related protein 4 (SFRP4), a Wnt antagonist; The ...
 60-164 1.11e-19

Cysteine-rich domain of the secreted frizzled-related protein 4 (SFRP4), a Wnt antagonist; The cysteine-rich domain (CRD) is an essential part of the secreted frizzled-related Protein 4 (SFRP4), which regulates the activity of Wnt proteins, key players in a number of fundamental cellular processes such as embryogenesis and postnatal development. SFRPs antagonize the activation of Wnt signaling by binding to the CRDs domains of frizzled (Fz) proteins, thereby preventing Wnt proteins from binding to these receptors. SFRPs are also known to have functions unrelated to Wnt, as enhancers of procollagen cleavage by the TLD proteinases. SFRPs and Fz proteins both contain CRD domains, but SFRPs lack the seven-pass transmembrane domain which is an integral part of Fzs.


Pssm-ID: 143551  Cd Length: 127  Bit Score: 83.15  E-value: 1.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528609  60 LPLCHTVGYKRMRLPNLLEHESLAEVKQQASSWLPLLAKRCHSDTQVFLCSLFAPVC----LDRPIYPCRSLCEAVRAGC 135
Cdd:cd07442   10 IPMCRHMPWNITRMPNHLHHSTQENAVLAIEQYEELVDTGCSPVLPFFLCAMYAPICtlefLYDPIKPCRSVCQRARDGC 89

                         90       100       110
                 ....*....|....*....|....*....|
gi 188528609 136 APLMEAYGFPWPEMLHCHKFPL-DNDLCIA 164
Cdd:cd07442   90 EPIMRRYNHSWPESLACDDLPVyDRGVCIS 119
CRD_Collagen_XVIII cd07455
Cysteine-rich domain of the variant 3 of collagen XVIII (V3C18 ); The cysteine-rich domain ...
 50-167 3.97e-18

Cysteine-rich domain of the variant 3 of collagen XVIII (V3C18 ); The cysteine-rich domain (CRD) is an essential part of the variant 3 of collagen XVIII (V3C18), which regulates major cellular functions such as the differential epithelial morphogenesis of early lung and kidney development. V3C18 is a 170 kD protein, which is proteolotically processed into the CRD-containing 50 kD glucoprotein precursor that binds Wnt3a through its CRD domain and suppresses the Wnt3a-induced stabilization of beta catenin. Full-length V3C18 is unable to inhibit Wnt signaling.


Pssm-ID: 143564  Cd Length: 123  Bit Score: 78.70  E-value: 3.97e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528609  50 PPQCLDIPADLPLCHTVGYKRMRLPNLLEHESLAEVKQQASSWLPLLAKRCHSDTQVFLCSLFAPVCLDRPIY---PCRS 126
Cdd:cd07455    2 RPRCLPVPSSLPFCSRLGIRSFWLPNFLNHTSVEEVRAVLAEWAWLLESGCHPSLEWFFCLLLVPSCGGGPPPpppPCRQ 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 188528609 127 LCEAVRAGCAPLMEAYGFPwpemLHCHKFPLDND-LCIAVQF 167
Cdd:cd07455   82 FCEVLQDSCWNLLEGGRLP----VACASLPEQEDgYCVLIGP 119
CRD_FZ6 cd07450
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 6 (Fz6) receptor; The cysteine-rich ...
 57-175 1.27e-15

Cysteine-rich Wnt-binding domain (CRD) of the frizzled 6 (Fz6) receptor; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 6 (Fz6) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Frizzled 6 (Fz6) is expressed in the skin and hair follicles and controls hair patterning in mammals using a Fz-dependent tissue polarity system, which is similar to the one that patterns the Drosophila cuticle.


Pssm-ID: 143559 [Multi-domain]  Cd Length: 127  Bit Score: 72.11  E-value: 1.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528609  57 PADLPLCHTVGYKRMRLPNLLEHESLAEVKQQASSWLPLLAKRCHSDTQVFLCSLFAPVCLDR--PIYPCRSLCEAVRAG 134
Cdd:cd07450    7 PITVPRCLKMPYNMTFFPNLMGHYDQDIAAVEMEPFLPLANLRCSPNVHTFLCQAFVPTCTEQihVVRPCRELCEKVYSD 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 188528609 135 CAPLMEAYGFPWPEMLHCHKFPLDNDLCIAVQFGHLPATAP 175
Cdd:cd07450   87 CKKLIDTFGISWPEELECDRLQYCDETVPDTADPHTEFSSP 127
CRD_Carboxypeptidase_Z cd07447
Cysteine-rich domain of carboxypeptidase Z, a member of the carboxypeptidase E family; The ...
 51-155 4.41e-15

Cysteine-rich domain of carboxypeptidase Z, a member of the carboxypeptidase E family; The cysteine-rich-domain (CRD) is an essential part of carboxypeptidase Z, a member of the carboxypeptidase E family of metallocarboxypeptidases. This is a group of Zn-dependent enzymes implicated in the intra- and extracellular processing of proteins. Carboxypeptidase Z removes C-terminal basic amino acid residues from its substrates, particularly arginine. The CRD acts as a ligand-binding domain for Wnts involved in developmental processes. CPZ binds and may process Wnt-4, CPZ has also been found to enhance the induction of the homeobox gene Cdx1. During vertebrate embryogenesis, the CRD of CPZ upregulates Pax3, a Wnt reporter gene essential for patterning of somites and limb development.


Pssm-ID: 143556  Cd Length: 128  Bit Score: 70.55  E-value: 4.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528609  51 PQCLDIpaDLPLCHTVGYKRMRLPNLLEHESLAEVKQQASSWL-----PLLAKRCHSDTQVFLCSLFAPVCL-DRPIYPC 124
Cdd:cd07447    2 ATCTDL--LLSYCSDVSYTQTTFPNLLGHRSREVTEAGAEYLLlsvlhGLLGGECNPDIRLLGCSVLAPRCEnDKVIKPC 79

                         90       100       110
                 ....*....|....*....|....*....|.
gi 188528609 125 RSLCEAVRAGCAPLMEAYGFPWPEMLHCHKF 155
Cdd:cd07447   80 RSTCEALRKRCSHAFDAIQMAWPYFLDCDRF 110
CRD_corin_2 cd07888
One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ...
 57-163 3.34e-13

One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ; The cysteine-rich domain (CRD) is an essential component of corin, a type II transmembrane serine protease which functions as the convertase of the pro-atrial natriuretic peptide (pro-ANP) in the heart. Corin contains two CRDs in its extracellular region, which play an important role in recognition of the physiological substrate, pro-ANP. This model characterizes the second (C-terminal) CRD.


Pssm-ID: 143579 [Multi-domain]  Cd Length: 122  Bit Score: 65.42  E-value: 3.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528609  57 PADLPLCHTVGYKRMRLPNLLEHESLAE--VKQQASSWLPLLAKRCHSDTQVFLCSLFAPVC---LDRPIYPCRSLCEAV 131
Cdd:cd07888    4 PITLELCMNLPYNTTRYPNYLGHRTQKEasISWESSLFPALVQTNCYKYLMFFACTILVPKCdpvTQQRIPPCRSLCRNS 83

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 188528609 132 RAGCAPLMEAYGFPWPEMLHCHKFP---LDNDLCI 163
Cdd:cd07888   84 KERCESVLGIVGLQWPEDTDCAQFPeenSDNQTCL 118
NTR_like cd03523
NTR_like domain; a beta barrel with an oligosaccharide/oligonucleotide-binding fold found in ...
 198-292 1.68e-10

NTR_like domain; a beta barrel with an oligosaccharide/oligonucleotide-binding fold found in netrins, complement proteins, tissue inhibitors of metalloproteases (TIMP), and procollagen C-proteinase enhancers (PCOLCE), amongst others. In netrins, the domain plays a role in controlling axon branching in neural development, while the common function of these modules in TIMPs appears to be binding to metzincins. A subset of this family is also known as the C345C domain because it occurs as a C-terminal domain in complement C3, C4 and C5. In C5, the domain interacts with various partners during the formation of the membrane attack complex.


Pssm-ID: 239600  Cd Length: 105  Bit Score: 57.09  E-value: 1.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528609 198 CSSDFVVKMRIKEIKIENGDRKligAQKKKKLLKPGPLKRKDTKRLVLHMKNGAGCPCPQLDSLAGSFLVMGRKVD--GQ 275
Cdd:cd03523    4 CKSDYVVRAKIKEIKEENDDVK---YEVKIIKIYKTGKAKADKADLRFYYTAPACCPCHPILNPGREYLIMGKEEDsqGG 80

                         90       100
                 ....*....|....*....|
gi 188528609 276 LLLM---AVYRWDKKNKEMK 292
Cdd:cd03523   81 LVLDplsFVEPWSPLSLRQD 100
NTR pfam01759
UNC-6/NTR/C345C module; Sequence similarity between netrin UNC-6 and C345C complement protein ...
 195-292 1.01e-09

UNC-6/NTR/C345C module; Sequence similarity between netrin UNC-6 and C345C complement protein family members, and hence the existence of the UNC-6 module, was first reported in. Subsequently, many additional members of the family were identified on the basis of sequence similarity between the C-terminal domains of netrins, complement proteins C3, C4, C5, secreted frizzled-related proteins, and type I pro-collagen C-proteinase enhancer proteins (PCOLCEs), which are homologous with the N-terminal domains of tissue inhibitors of metalloproteinases (TIMPs). The TIMPs are classified as a separate family in Pfam (pfam00965). This expanded domain family has been named as the NTR module.


Pssm-ID: 396359  Cd Length: 106  Bit Score: 55.04  E-value: 1.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528609  195 EQMCS-SDFVVKMRIKEIKIENGDRKLI---------GAQkkkkllkpgplkRKDTKRLVLHMKNGAgCPCPQLDsLAGS 264
Cdd:pfam01759   1 KKACKgSDYVYKVKVLSVEEEGSFDKYTvkvkevlkeGTD------------KIQRGKVRLFLKRGD-CRCPQLR-LGKE 66

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 188528609  265 FLVMGRKVD-----------GQLLLMAVYRWDKKNKEMK 292
Cdd:pfam01759  67 YLIMGKVGDlegrgryvldkNSWVEPWPTKWECKLRELQ 105
C345C smart00643
Netrin C-terminal Domain;
194-289 1.58e-09

Netrin C-terminal Domain;


Pssm-ID: 214759  Cd Length: 114  Bit Score: 54.68  E-value: 1.58e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528609   194 MEQMCSS--DFVVKMRIKEIKIENGDRKLI---------GaqkkkkllkpgpLKRKDTKRLVLHMKNG-AGCPCPQLDSL 261
Cdd:smart00643   1 LEKACKSdvDYVYKVKVLSVEEEGGFDKYTvkileviksG------------TDELVRGKNKLRVFISrASCRCPLLLKL 68

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 188528609   262 AGSFLVMGRKVD-------GQLLLMA---VYRWDKKNK 289
Cdd:smart00643  69 GKSYLIMGKSGDlwdakgrGQYVLGKnswVEEWPTEEE 106
CRD_corin_1 cd07445
One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ...
 100-155 3.88e-08

One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ; The cysteine-rich domain (CRD) is an essential component of corin, a type II transmembrane serine protease which functions as the convertase of the pro-atrial natriuretic peptide (pro-ANP) in the heart. Corin contains two CRDs in its extracellular region, which play an important role in recognition of the physiological substrate, pro-ANP. This model characterizes the first (N-terminal) CRD.


Pssm-ID: 143554  Cd Length: 130  Bit Score: 51.09  E-value: 3.88e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 188528609 100 CHSDTQVFLCSLFAPVCL----DRP-IYPCRSLCEAVRAGCAPLMEAYGFPWPEMLHCHKF 155
Cdd:cd07445   49 CYQHIMLFGCSLALPECIsdgdDRHgLLPCRSFCEAAKEGCEPVLGMVNASWPDFLRCSQF 109
CRD_SMO cd07451
Cysteine-rich domain of the smoothened receptor (Smo) integral membrane protein; The ...
 78-162 1.83e-07

Cysteine-rich domain of the smoothened receptor (Smo) integral membrane protein; The cysteine-rich domain (CRD) is part of the smoothened receptor (Smo), an integral membrane protein and one of the key players in the Hedgehog (Hh) signaling pathway, critical for development, cell growth and migration, as well as stem cell maintenance. The CRD of Smo is conserved in vertebrates and can also be identified in invertebrates. The precise function of the CRD in Smo is unknown. Mutations in the Drosophila CRD disrupt Smo activity in vivo, while deletion of the CRD in mammalian cells does not seem to affect the activity of overexpressed Smo.


Pssm-ID: 143560  Cd Length: 132  Bit Score: 49.29  E-value: 1.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188528609  78 EHESLAEVKQQASSWLPL-LAKRCHSDTQVFLCSLFAPVCLDRPIY-PCRSLCEAVRAGCAPLMEAYGfpWPEMLHCHKF 155
Cdd:cd07451   30 DSTTQEEVQEKLHLWSGLrNVPKCWAVIQPLLCALYMPKCENGKVElPSQEMCQATRGPCKIVENERG--WPDFLRCDND 107


                 ....*..
gi 188528609 156 PLDNDLC 162
Cdd:cd07451  108 RFPPRGC 114
 
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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