ASPIC and UnbV; This conserved sequence is found associated with pfam00515 in several paralogous proteins in Rhodopirellula baltica. It is also found associated with pfam01839 in several eukaryotic integrin-like proteins (e.g. human ASPIC) and in several other bacterial proteins.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1974316035 469 GAKVVLFTrHSGAHLRIIDGGSGYLCEMEPVAHFGLGQ-DEPSSLEVTWPDGK 520
Cdd:pfam07593   1 GARVTVTT-AGGRQYREVTGGRGYLSSSDPRLHFGLGDaTTIDSLEVRWPDGK 52

FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related proteins in which form a 7-fold repeat that adopts a beta-propeller fold. This repeat contains a putative calcium-binding site. These repeats are found in multiple proteins from eukaryotes and bacteria and mediate diverse biological processes at both molecular and cellular levels, such as cell-cell interactions, host-pathogen recognition or innate immune responses.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1974316035 308 DFNRDGKVDLIYGNWNGPhRLYLQVNAGgriRFRDIATPKLSMPSPVRTVIAADFDNDQELEVFF 372
Cdd:pfam13517   1 DLDGDGKLDLVVANDGGL-RLYLNNGDG---TFTFITSVSLGGGGGGLSVAVGDLDGDGRLDLLV 61

FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related proteins in which form a 7-fold repeat that adopts a beta-propeller fold. This repeat contains a putative calcium-binding site. These repeats are found in multiple proteins from eukaryotes and bacteria and mediate diverse biological processes at both molecular and cellular levels, such as cell-cell interactions, host-pathogen recognition or innate immune responses.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1974316035  73 DVDQDGDFEVIVAGYNGPNLVLKYDKARGRLlnlaVDEHSSPyyalrdRQGNAIGVAACDIDGDGWEEIYF 143
Cdd:pfam13517   1 DLDGDGKLDLVVANDGGLRLYLNNGDGTFTF----ITSVSLG------GGGGGLSVAVGDLDGDGRLDLLV 61

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)].

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974316035  678 IPADLQLCHNVGYKRMRLPNLLEHDSMPEIKQQANSWVPLLAKRCHSDTQIFLCSLFTPVCLDQ--PIYPCRSLCEVVRD 755
Cdd:smart00063   2 EPITIPLCKDLGYNLTSMPNLLGHTTQEEAGLELEQFHPLLNVQCSPDLRFFLCSVYAPICTEDlrPILPCRSLCEAARE 81

                           90       100       110
                   ....*....|....*....|....*....|
gi 1974316035  756 SCAPVMESYGFPWPDMLNCNKFPFDNDLCI 785
Cdd:smart00063  82 GCEPLMEKFGFPWPEFLRCDRFPVQEELCM 111

ASPIC and UnbV; This conserved sequence is found associated with pfam00515 in several paralogous proteins in Rhodopirellula baltica. It is also found associated with pfam01839 in several eukaryotic integrin-like proteins (e.g. human ASPIC) and in several other bacterial proteins.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1974316035 469 GAKVVLFTrHSGAHLRIIDGGSGYLCEMEPVAHFGLGQ-DEPSSLEVTWPDGK 520
Cdd:pfam07593   1 GARVTVTT-AGGRQYREVTGGRGYLSSSDPRLHFGLGDaTTIDSLEVRWPDGK 52

FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related proteins in which form a 7-fold repeat that adopts a beta-propeller fold. This repeat contains a putative calcium-binding site. These repeats are found in multiple proteins from eukaryotes and bacteria and mediate diverse biological processes at both molecular and cellular levels, such as cell-cell interactions, host-pathogen recognition or innate immune responses.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1974316035 308 DFNRDGKVDLIYGNWNGPhRLYLQVNAGgriRFRDIATPKLSMPSPVRTVIAADFDNDQELEVFF 372
Cdd:pfam13517   1 DLDGDGKLDLVVANDGGL-RLYLNNGDG---TFTFITSVSLGGGGGGLSVAVGDLDGDGRLDLLV 61

Calcium-binding EGF-like domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1974316035  569 DMDECAEFPfVCPRGrPICINTYGGYRCrsnkRCNRGFepnEDGTACV 616
Cdd:smart00179   1 DIDECASGN-PCQNG-GTCVNTVGSYRC----ECPPGY---TDGRNCE 39

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

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1974316035 569 DMDECAEFPfVCPRGrPICINTYGGYRCrsnkRCNRGFEpnedGTACV 616
Cdd:cd00054     1 DIDECASGN-PCQNG-GTCVNTVGSYRC----SCPPGYT----GRNCE 38

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974316035 669 YTKQSQCVDIPADLQLCHNVGYKRMRLPNLLEHDSMPEIKQQANSWVPLLAKRCHSDTQIFLCSLFTPVCLDQPIYPCRS 748
Cdd:cd07443     1 YTKPPQCVDIPADLRLCHNVGYKKMVLPNLLDHETMAEVKQQASSWVPLLNKNCHKGTQVFLCSLFAPVCLDRPVYPCRW 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1974316035 749 LCEVVRDSCAPVMESYGFPWPDMLNCNKFPFDnDLCITVQFGN 791
Cdd:cd07443    81 LCEAVRDSCEPVMQFFGFYWPEMLKCDKFPEG-EVCIAMTPPN 122

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974316035 673 SQCVDIPADLQLCHNVGYKRMRLPNLLEHDSMPEIKQQANSWVPLLAKRCHSDTQIFLCSLFTPVCLDQPIYPCRSLCEV 752
Cdd:cd07453     1 SPCMRIPKSMALCYDIGYSEMRIPNLLEHETMAEVIQQSSSWLPLLARECHPDARIFLCSLFAPICWDRPIYPCRSLCEA 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1974316035 753 VRDSCAPVMESYGFPWPDMLNCNKFPFDNDLCITVQFGN 791
Cdd:cd07453    81 VRSSCAPLMACYGYPWPEILHCDKFPVDHDLCISPQFID 119

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974316035 674 QCVDIPadLQLCHNVGYKRMRLPNLLEHDSMPEIKQQANSWVPLLAKRCHSDTQIFLCSLFTPVCLDQ---PIYPCRSLC 750
Cdd:cd07066     1 KCEPIP--LPLCRGLPYNTTRFPNLLGHESQEEAEQELESFTPLVNSGCHPDLRFFLCSLYFPECTPDgdrPIPPCRSLC 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1974316035 751 EVVRDSCAPVMESYGFPWPDMLNCNKFPFDN--DLCITVQ 788
Cdd:cd07066    79 EEVRDSCEPLMLAFGFPWPEPLDCDRFPDSNeeGLCISPP 118

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974316035 679 PADLQLCHNVGYKRMRLPNLLEHDSMPEIKQQANSWVPLLAKRCHSDTQIFLCSLFTPVC---LDQPIYPCRSLCEVVRD 755
Cdd:cd07448     6 PIRIEMCQGLGYNVTRMPNLVGHELQTDAELQLQTFTPLIQYGCSSQLKFFLCSVYVPMCtekVPVPIGPCRPLCLSVKK 85

                          90       100
                  ....*....|....*....|....*..
gi 1974316035 756 SCAPVMESYGFPWPDMLNCNKFPFDND 782
Cdd:cd07448    86 RCLPVLKEFGFPWPEALNCSKFPPQNN 112

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974316035 674 QCVDIPadlqLCHNVGYKRMRLPNLLEHDSMPEIKQQANSWVPLLAKRCHSDTQIFLCSLFTPVCLDQ---PIYPCRSLC 750
Cdd:cd07463     6 QPVVIP----MCRGIGYNLTRMPNFLGHDSQREAAIKLNEFAPLVEYGCHVHLRFFLCSLYAPMCTDQvstSIPACRPMC 81

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1974316035 751 EVVRDSCAPVMESYGFPWPDMLNCNKFPFDND---LCI 785
Cdd:cd07463    82 EQARQKCSPIMEQFNFGWPESLDCSRLPTRNDpnaLCM 119

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974316035 671 KQSQCVDIPadLQLCHNVGYKRMRLPNLLEHDSMPEIKQQANSWVPLLAKRCHSDTQIFLCSLFTPVCLD---QPIYPCR 747
Cdd:cd07461     1 KELQCQEIT--VPLCKGIGYNYTYMPNQFNHDTQDEAGLEVHQFWPLVEIQCSPDLKFFLCSMYTPICLEdykKPLPPCR 78

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1974316035 748 SLCEVVRDSCAPVMESYGFPWPDMLNCNKFP 778
Cdd:cd07461    79 SVCERAKAGCAPLMRQYGFPWPDRMRCDLLP 109

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974316035 679 PADLQLCHNVGYKRMRLPNLLEHDSMPEIKQQANSWVPLLAKRCHSDTQIFLCSLFTPVC--LDQPIYPCRSLCEVVRDS 756
Cdd:cd07458     5 PITIPLCTDIPYNMTIFPNLLGHTKQEDAGLEVHQFYPLVKVQCSPDLKFFLCSVYAPVCtvLERPIPPCRSLCESARQG 84

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1974316035 757 CAPVMESYGFPWPDMLNCNKFPFDN--DLCI 785
Cdd:cd07458    85 CEALMNKFGFQWPESLDCEKFPVHGagDLCV 115

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974316035 684 LCHNVGYKRMRLPNLLEHDSMPEIKQQANSWVPLLAKRCHSDTQIFLCSLFTPVCLD---QPIYPCRSLCEVVRDSCAPV 760
Cdd:cd07460    12 MCKGIGYNLTYMPNQFNHDTQDEAGLEVHQFWPLVEIQCSPDLRFFLCSMYTPICLPdyrKPLPPCRSVCERAKAGCSPL 91

                          90       100
                  ....*....|....*....|....*...
gi 1974316035 761 MESYGFPWPDMLNCNKFPFDND---LCI 785
Cdd:cd07460    92 MRQYGFAWPERMNCDRLPVLGDpetLCM 119

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974316035 679 PADLQLCHNVGYKRMRLPNLLEHDSMPEIKQQANSWVPLLAKRCHSDTQIFLCSLFTPVC--LDQPIYPCRSLCEVVRDS 756
Cdd:cd07466     7 PISIPLCTDIAYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSPELKFFLCSMYAPVCtvLEQAIPPCRSLCERARQG 86

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1974316035 757 CAPVMESYGFPWPDMLNCNKFPFD--NDLCITVQFGNN 792
Cdd:cd07466    87 CEALMNKFGFQWPERLRCENFPVHgaGEICVGQNTSDA 124

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974316035 678 IPADLQLCHNVGYKRMRLPNLLEHDSMPEIKQQANSWVPLLAKRCHSDTQIFLCSLFTPVCLDQ---PIYPCRSLCEVVR 754
Cdd:cd07454     6 IPIDIELCKDLPYNYTYFPNTILHNDQHTLQTHTEHFKPLMKTKCHPHIHFFICSVFAPMCPIGmpqAVTSCKSVCEQVK 85

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1974316035 755 DSCAPVMESYGFPWPDMLNCNKFPFDNDLCI 785
Cdd:cd07454    86 ADCFSILEEFGIGWPEPLNCAQFPDPPELCM 116

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974316035 674 QCVDIPadlqLCHNVGYKRMRLPNLLEHDSMPEIKQQANSWVPLLAKRCHSDTQIFLCSLFTPVC----LDQPIYPCRSL 749
Cdd:cd07442     6 EAVRIP----MCRHMPWNITRMPNHLHHSTQENAVLAIEQYEELVDTGCSPVLPFFLCAMYAPICtlefLYDPIKPCRSV 81

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1974316035 750 CEVVRDSCAPVMESYGFPWPDMLNCNKFP-FDNDLCIT 786
Cdd:cd07442    82 CQRARDGCEPIMRRYNHSWPESLACDDLPvYDRGVCIS 119

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974316035 679 PADLQLCHNVGYKRMRLPNLLEHDSMPE--IKQQANSWVPLLAKRCHSDTQIFLCSLFTPVC---LDQPIYPCRSLCEVV 753
Cdd:cd07888     4 PITLELCMNLPYNTTRYPNYLGHRTQKEasISWESSLFPALVQTNCYKYLMFFACTILVPKCdpvTQQRIPPCRSLCRNS 83

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1974316035 754 RDSCAPVMESYGFPWPDMLNCNKFP---FDNDLCIT 786
Cdd:cd07888    84 KERCESVLGIVGLQWPEDTDCAQFPeenSDNQTCLL 119

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974316035 679 PADLQLCHNVGYKRMRLPNLLEHDSMPEIKQQANSWVPLLAKRCHSDTQIFLCSLFTPVCLDQ--PIYPCRSLCEVVRDS 756
Cdd:cd07450     7 PITVPRCLKMPYNMTFFPNLMGHYDQDIAAVEMEPFLPLANLRCSPNVHTFLCQAFVPTCTEQihVVRPCRELCEKVYSD 86

                          90       100
                  ....*....|....*....|..
gi 1974316035 757 CAPVMESYGFPWPDMLNCNKFP 778
Cdd:cd07450    87 CKKLIDTFGISWPEELECDRLQ 108

ASPIC and UnbV; This conserved sequence is found associated with pfam00515 in several paralogous proteins in Rhodopirellula baltica. It is also found associated with pfam01839 in several eukaryotic integrin-like proteins (e.g. human ASPIC) and in several other bacterial proteins.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1974316035 469 GAKVVLFTrHSGAHLRIIDGGSGYLCEMEPVAHFGLGQ-DEPSSLEVTWPDGK 520
Cdd:pfam07593   1 GARVTVTT-AGGRQYREVTGGRGYLSSSDPRLHFGLGDaTTIDSLEVRWPDGK 52

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1974316035 722 CHSDTQIFLCSLFTPVCLDQP-----IYPCRSLCEVVRDSCAPVMESYGFPWPDMLNCNKF 777
Cdd:cd07445    49 CYQHIMLFGCSLALPECISDGddrhgLLPCRSFCEAAKEGCEPVLGMVNASWPDFLRCSQF 109

FG-GAP-like repeat; This entry represents a repeat found in alpha integrins and related proteins in which form a 7-fold repeat that adopts a beta-propeller fold. This repeat contains a putative calcium-binding site. These repeats are found in multiple proteins from eukaryotes and bacteria and mediate diverse biological processes at both molecular and cellular levels, such as cell-cell interactions, host-pathogen recognition or innate immune responses.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1974316035 308 DFNRDGKVDLIYGNWNGPhRLYLQVNAGgriRFRDIATPKLSMPSPVRTVIAADFDNDQELEVFF 372
Cdd:pfam13517   1 DLDGDGKLDLVVANDGGL-RLYLNNGDG---TFTFITSVSLGGGGGGLSVAVGDLDGDGRLDLLV 61

Calcium-binding EGF-like domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1974316035  569 DMDECAEFPfVCPRGrPICINTYGGYRCrsnkRCNRGFepnEDGTACV 616
Cdd:smart00179   1 DIDECASGN-PCQNG-GTCVNTVGSYRC----ECPPGY---TDGRNCE 39

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

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1974316035 569 DMDECAEFPfVCPRGrPICINTYGGYRCrsnkRCNRGFEpnedGTACV 616
Cdd:cd00054     1 DIDECASGN-PCQNG-GTCVNTVGSYRC----SCPPGYT----GRNCE 38