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Conserved domains on  [gi|157822425|ref|NP_001101607|]
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membrane frizzled-related protein [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 307-419 5.10e-39

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


:

Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 138.70  E-value: 5.10e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425 307 CGGNLT-ELSGVFSTPNYPQHYPHQQLCTWYIKVPVGYRIRLEFHNFSLEEQTECKFDYVEVYEaSNSGTFSSLGRFCGA 385
Cdd:cd00041    1 CGGTLTaSTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYD-GPSTSSPLLGRFCGS 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 157822425 386 EPPSHLVSSQHQLTVIFKTDLGISSGGFLATYQA 419
Cdd:cd00041   80 TLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 150-258 1.05e-31

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


:

Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 118.67  E-value: 1.05e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425 150 CGGLLPGP-SGFFSSPNYPDLYPPHSHCVWHIQVATGQTIQLKIQVLSTESMLACLFDRLEI--SPAPTGPLL-RMCGKT 225
Cdd:cd00041    1 CGGTLTAStSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIydGPSTSSPLLgRFCGST 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 157822425 226 PPATVNTNTSHLRVSFVSDNDVEGSGFQAWYQA 258
Cdd:cd00041   81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CRD_FZ cd07066
CRD_domain cysteine-rich domain, also known as Fz (frizzled) domain; CRD_FZ is an essential ...
 476-590 4.31e-24

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: 97.58  E-value: 4.31e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425 476 TCEPVQVEMCLGLSYNTTAFPNIwVGLATQMEVTDILRGYKSLTSLPCYQTFRRFLCGLLEPRCTSLG-TILPPCRSVCQ 554
Cdd:cd07066    1 KCEPIPLPLCRGLPYNTTRFPNL-LGHESQEEAEQELESFTPLVNSGCHPDLRFFLCSLYFPECTPDGdRPIPPCRSLCE 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 157822425 555 EAEQQCQSSLALLGIPWP--FNCNRLPVPASLEACSQP 590
Cdd:cd07066   80 EVRDSCEPLMLAFGFPWPepLDCDRFPDSNEEGLCISP 117
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 266-300 2.07e-08

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


:

Pssm-ID: 238060  Cd Length: 35  Bit Score: 50.28  E-value: 2.07e-08
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 157822425 266 CTHYEFHCDLLLCLKQDSVCDGIKDCIDGSDEANC 300
Cdd:cd00112    1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
 
Name Accession Description Interval E-value
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 307-419 5.10e-39

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 138.70  E-value: 5.10e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425 307 CGGNLT-ELSGVFSTPNYPQHYPHQQLCTWYIKVPVGYRIRLEFHNFSLEEQTECKFDYVEVYEaSNSGTFSSLGRFCGA 385
Cdd:cd00041    1 CGGTLTaSTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYD-GPSTSSPLLGRFCGS 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 157822425 386 EPPSHLVSSQHQLTVIFKTDLGISSGGFLATYQA 419
Cdd:cd00041   80 TLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CUB pfam00431
CUB domain;
307-417 4.94e-36

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 130.49  E-value: 4.94e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425  307 CGGNLTELSGVFSTPNYPQHYPHQQLCTWYIKVPVGYRIRLEFHNFSLEEQTECKFDYVEVYEaSNSGTFSSLGRFCGAE 386
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRD-GPSASSPLLGRFCGSG 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 157822425  387 PPSHLVSSQHQLTVIFKTDLGISSGGFLATY 417
Cdd:pfam00431  80 IPEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 316-417 1.96e-33

Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.


Pssm-ID: 214483 [Multi-domain]  Cd Length: 102  Bit Score: 122.88  E-value: 1.96e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425   316 GVFSTPNYPQHYPHQQLCTWYIKVPVGYRIRLEFHNFSLEEQTECKFDYVEVYEaSNSGTFSSLGRFCGAEPPSHLVSSQ 395
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYD-GPSASSPLLGRFCGSEAPPPVISSS 79

                           90       100
                   ....*....|....*....|...
gi 157822425   396 H-QLTVIFKTDLGISSGGFLATY 417
Cdd:smart00042  80 SnSLTLTFVSDSSVQKRGFSARY 102
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 150-258 1.05e-31

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 118.67  E-value: 1.05e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425 150 CGGLLPGP-SGFFSSPNYPDLYPPHSHCVWHIQVATGQTIQLKIQVLSTESMLACLFDRLEI--SPAPTGPLL-RMCGKT 225
Cdd:cd00041    1 CGGTLTAStSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIydGPSTSSPLLgRFCGST 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 157822425 226 PPATVNTNTSHLRVSFVSDNDVEGSGFQAWYQA 258
Cdd:cd00041   81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 159-256 1.04e-28

Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.


Pssm-ID: 214483 [Multi-domain]  Cd Length: 102  Bit Score: 109.79  E-value: 1.04e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425   159 GFFSSPNYPDLYPPHSHCVWHIQVATGQTIQLKIQVLSTESMLACLFDRLEI--SPAPTGPLL-RMCGKTPPATVNT-NT 234
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIydGPSASSPLLgRFCGSEAPPPVISsSS 80

                           90       100
                   ....*....|....*....|..
gi 157822425   235 SHLRVSFVSDNDVEGSGFQAWY 256
Cdd:smart00042  81 NSLTLTFVSDSSVQKRGFSARY 102
CUB pfam00431
CUB domain;
150-256 9.46e-28

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 107.38  E-value: 9.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425  150 CGGLLPGPSGFFSSPNYPDLYPPHSHCVWHIQVATGQTIQLKIQVLSTESMLACLFDRLEI--SPAPTGPLL-RMCGKTP 226
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIrdGPSASSPLLgRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 157822425  227 PATVNTNTSHLRVSFVSDNDVEGSGFQAWY 256
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CRD_FZ cd07066
CRD_domain cysteine-rich domain, also known as Fz (frizzled) domain; CRD_FZ is an essential ...
 476-590 4.31e-24

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: 97.58  E-value: 4.31e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425 476 TCEPVQVEMCLGLSYNTTAFPNIwVGLATQMEVTDILRGYKSLTSLPCYQTFRRFLCGLLEPRCTSLG-TILPPCRSVCQ 554
Cdd:cd07066    1 KCEPIPLPLCRGLPYNTTRFPNL-LGHESQEEAEQELESFTPLVNSGCHPDLRFFLCSLYFPECTPDGdRPIPPCRSLCE 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 157822425 555 EAEQQCQSSLALLGIPWP--FNCNRLPVPASLEACSQP 590
Cdd:cd07066   80 EVRDSCEPLMLAFGFPWPepLDCDRFPDSNEEGLCISP 117
Fz pfam01392
Fz domain; Also known as the CRD (cysteine rich domain), the C6 box in MuSK receptor. This ...
 477-581 1.41e-22

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: 93.02  E-value: 1.41e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425  477 CEPVQVEMCLGLSYNTTAFPNiWVGLATQMEVTD-----ILRGYKSLTSLPCYQTFRRFLCGLLEPRCTSLG---TILPP 548
Cdd:pfam01392   1 CEPITLPMCLGLGYNATVFPN-LLGHQTQEEAELslaylVLSEFEPLVDLSCSPSLRLFLCSLYFPPCTLGPspkPVCPP 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 157822425  549 CRSVCQEAEQQCQSSLALL--GIPWP--FNCNRLPVP 581
Cdd:pfam01392  80 CRSLCEEVRYGCEPLLEEAkfGFSWPefLDCDSLPAD 116
FRI smart00063
Frizzled; Drosophila melanogaster frizzled mediates signalling that polarises a precursor cell ...
 477-581 1.22e-20

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: 87.37  E-value: 1.22e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425   477 CEPVQVEMCLGLSYNTTAFPNIwVGLATQMEVTDILRGYKSLTSLPCYQTFRRFLCGLLEPRCTSLGTILPPCRSVCQEA 556
Cdd:smart00063   1 CEPITIPLCKDLGYNLTSMPNL-LGHTTQEEAGLELEQFHPLLNVQCSPDLRFFLCSVYAPICTEDLRPILPCRSLCEAA 79

                           90       100
                   ....*....|....*....|....*..
gi 157822425   557 EQQCQSSLALLGIPWP--FNCNRLPVP 581
Cdd:smart00063  80 REGCEPLMEKFGFPWPefLRCDRFPVQ 106
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 266-300 2.07e-08

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 50.28  E-value: 2.07e-08
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 157822425 266 CTHYEFHCDLLLCLKQDSVCDGIKDCIDGSDEANC 300
Cdd:cd00112    1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 266-297 3.38e-06

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 43.78  E-value: 3.38e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 157822425   266 CTHYEFHCDLLLCLKQDSVCDGIKDCIDGSDE 297
Cdd:smart00192   2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
266-300 4.06e-06

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 43.78  E-value: 4.06e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 157822425  266 CTHYEFHCDLLLCLKQDSVCDGIKDCIDGSDEANC 300
Cdd:pfam00057   3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
 
Name Accession Description Interval E-value
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 307-419 5.10e-39

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 138.70  E-value: 5.10e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425 307 CGGNLT-ELSGVFSTPNYPQHYPHQQLCTWYIKVPVGYRIRLEFHNFSLEEQTECKFDYVEVYEaSNSGTFSSLGRFCGA 385
Cdd:cd00041    1 CGGTLTaSTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIYD-GPSTSSPLLGRFCGS 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 157822425 386 EPPSHLVSSQHQLTVIFKTDLGISSGGFLATYQA 419
Cdd:cd00041   80 TLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CUB pfam00431
CUB domain;
307-417 4.94e-36

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 130.49  E-value: 4.94e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425  307 CGGNLTELSGVFSTPNYPQHYPHQQLCTWYIKVPVGYRIRLEFHNFSLEEQTECKFDYVEVYEaSNSGTFSSLGRFCGAE 386
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIRD-GPSASSPLLGRFCGSG 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 157822425  387 PPSHLVSSQHQLTVIFKTDLGISSGGFLATY 417
Cdd:pfam00431  80 IPEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 316-417 1.96e-33

Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.


Pssm-ID: 214483 [Multi-domain]  Cd Length: 102  Bit Score: 122.88  E-value: 1.96e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425   316 GVFSTPNYPQHYPHQQLCTWYIKVPVGYRIRLEFHNFSLEEQTECKFDYVEVYEaSNSGTFSSLGRFCGAEPPSHLVSSQ 395
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIYD-GPSASSPLLGRFCGSEAPPPVISSS 79

                           90       100
                   ....*....|....*....|...
gi 157822425   396 H-QLTVIFKTDLGISSGGFLATY 417
Cdd:smart00042  80 SnSLTLTFVSDSSVQKRGFSARY 102
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 150-258 1.05e-31

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 118.67  E-value: 1.05e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425 150 CGGLLPGP-SGFFSSPNYPDLYPPHSHCVWHIQVATGQTIQLKIQVLSTESMLACLFDRLEI--SPAPTGPLL-RMCGKT 225
Cdd:cd00041    1 CGGTLTAStSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSPNCSYDYLEIydGPSTSSPLLgRFCGST 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 157822425 226 PPATVNTNTSHLRVSFVSDNDVEGSGFQAWYQA 258
Cdd:cd00041   81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 159-256 1.04e-28

Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.


Pssm-ID: 214483 [Multi-domain]  Cd Length: 102  Bit Score: 109.79  E-value: 1.04e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425   159 GFFSSPNYPDLYPPHSHCVWHIQVATGQTIQLKIQVLSTESMLACLFDRLEI--SPAPTGPLL-RMCGKTPPATVNT-NT 234
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDNCEYDYVEIydGPSASSPLLgRFCGSEAPPPVISsSS 80

                           90       100
                   ....*....|....*....|..
gi 157822425   235 SHLRVSFVSDNDVEGSGFQAWY 256
Cdd:smart00042  81 NSLTLTFVSDSSVQKRGFSARY 102
CUB pfam00431
CUB domain;
150-256 9.46e-28

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 107.38  E-value: 9.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425  150 CGGLLPGPSGFFSSPNYPDLYPPHSHCVWHIQVATGQTIQLKIQVLSTESMLACLFDRLEI--SPAPTGPLL-RMCGKTP 226
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGYDYVEIrdGPSASSPLLgRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 157822425  227 PATVNTNTSHLRVSFVSDNDVEGSGFQAWY 256
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CRD_FZ cd07066
CRD_domain cysteine-rich domain, also known as Fz (frizzled) domain; CRD_FZ is an essential ...
 476-590 4.31e-24

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: 97.58  E-value: 4.31e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425 476 TCEPVQVEMCLGLSYNTTAFPNIwVGLATQMEVTDILRGYKSLTSLPCYQTFRRFLCGLLEPRCTSLG-TILPPCRSVCQ 554
Cdd:cd07066    1 KCEPIPLPLCRGLPYNTTRFPNL-LGHESQEEAEQELESFTPLVNSGCHPDLRFFLCSLYFPECTPDGdRPIPPCRSLCE 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 157822425 555 EAEQQCQSSLALLGIPWP--FNCNRLPVPASLEACSQP 590
Cdd:cd07066   80 EVRDSCEPLMLAFGFPWPepLDCDRFPDSNEEGLCISP 117
Fz pfam01392
Fz domain; Also known as the CRD (cysteine rich domain), the C6 box in MuSK receptor. This ...
 477-581 1.41e-22

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: 93.02  E-value: 1.41e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425  477 CEPVQVEMCLGLSYNTTAFPNiWVGLATQMEVTD-----ILRGYKSLTSLPCYQTFRRFLCGLLEPRCTSLG---TILPP 548
Cdd:pfam01392   1 CEPITLPMCLGLGYNATVFPN-LLGHQTQEEAELslaylVLSEFEPLVDLSCSPSLRLFLCSLYFPPCTLGPspkPVCPP 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 157822425  549 CRSVCQEAEQQCQSSLALL--GIPWP--FNCNRLPVP 581
Cdd:pfam01392  80 CRSLCEEVRYGCEPLLEEAkfGFSWPefLDCDSLPAD 116
FRI smart00063
Frizzled; Drosophila melanogaster frizzled mediates signalling that polarises a precursor cell ...
 477-581 1.22e-20

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: 87.37  E-value: 1.22e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425   477 CEPVQVEMCLGLSYNTTAFPNIwVGLATQMEVTDILRGYKSLTSLPCYQTFRRFLCGLLEPRCTSLGTILPPCRSVCQEA 556
Cdd:smart00063   1 CEPITIPLCKDLGYNLTSMPNL-LGHTTQEEAGLELEQFHPLLNVQCSPDLRFFLCSVYAPICTEDLRPILPCRSLCEAA 79

                           90       100
                   ....*....|....*....|....*..
gi 157822425   557 EQQCQSSLALLGIPWP--FNCNRLPVP 581
Cdd:smart00063  80 REGCEPLMEKFGFPWPefLRCDRFPVQ 106
CRD_FZ3 cd07449
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 3 (Fz3) receptor; The cysteine-rich ...
 475-579 1.89e-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: 87.37  E-value: 1.89e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425 475 LTCEPVQVEMCLGLSYNTTAFPNIwVGLATQMEVTDILRGYKSLTSLPCYQTFRRFLCGLLEPRCTSLGTILPPCRSVCQ 554
Cdd:cd07449    3 FSCEPITLRMCQDLPYNTTFMPNL-LNHYDQQTAALAMEPFHPMVNLECSRDFRPFLCALYAPVCMEYGRVTLPCRRLCQ 81

                         90       100
                 ....*....|....*....|....*..
gi 157822425 555 EAEQQCQSSLALLGIPWP--FNCNRLP 579
Cdd:cd07449   82 RAYSECSKLMEMFGVPWPedMECSRFP 108
CRD_FZ1_like cd07458
Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 1; The cysteine-rich ...
 477-587 1.13e-19

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: 84.77  E-value: 1.13e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425 477 CEPVQVEMCLGLSYNTTAFPNIwVGLATQMEVTDILRGYKSLTSLPCYQTFRRFLCGLLEPRCTSLGTILPPCRSVCQEA 556
Cdd:cd07458    3 CEPITIPLCTDIPYNMTIFPNL-LGHTKQEDAGLEVHQFYPLVKVQCSPDLKFFLCSVYAPVCTVLERPIPPCRSLCESA 81

                         90       100       110
                 ....*....|....*....|....*....|...
gi 157822425 557 EQQCQSSLALLGIPWPFN--CNRLPVPASLEAC 587
Cdd:cd07458   82 RQGCEALMNKFGFQWPESldCEKFPVHGAGDLC 114
CRD_FZ4 cd07448
Cysteine-rich Wnt-binding domain of the frizzled 4 (Fz4) receptor; The cysteine-rich domain ...
 474-580 4.14e-18

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: 80.58  E-value: 4.14e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425 474 DLTCEPVQVEMCLGLSYNTTAFPNIwVGLATQMEVTDILRGYKSLTSLPCYQTFRRFLCGLLEPRCT-SLGTILPPCRSV 552
Cdd:cd07448    1 DRRCEPIRIEMCQGLGYNVTRMPNL-VGHELQTDAELQLQTFTPLIQYGCSSQLKFFLCSVYVPMCTeKVPVPIGPCRPL 79

                         90       100       110
                 ....*....|....*....|....*....|
gi 157822425 553 CQEAEQQCQSSLALLGIPWP--FNCNRLPV 580
Cdd:cd07448   80 CLSVKKRCLPVLKEFGFPWPeaLNCSKFPP 109
CRD_corin_2 cd07888
One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ...
 477-579 1.00e-17

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: 79.29  E-value: 1.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425 477 CEPVQVEMCLGLSYNTTAFPNiWVGLATQMEVTDILRG--YKSLTSLPCYQTFRRFLCGLLEPRC-TSLGTILPPCRSVC 553
Cdd:cd07888    2 CEPITLELCMNLPYNTTRYPN-YLGHRTQKEASISWESslFPALVQTNCYKYLMFFACTILVPKCdPVTQQRIPPCRSLC 80

                         90       100
                 ....*....|....*....|....*...
gi 157822425 554 QEAEQQCQSSLALLGIPWP--FNCNRLP 579
Cdd:cd07888   81 RNSKERCESVLGIVGLQWPedTDCAQFP 108
CRD_FZ9 cd07463
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 9 (Fz9) receptor; The cysteine-rich ...
 477-579 1.10e-16

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: 76.60  E-value: 1.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425 477 CEPVQVEMCLGLSYNTTAFPNIwVGLATQMEVTDILRGYKSLTSLPCYQTFRRFLCGLLEPRCT-SLGTILPPCRSVCQE 555
Cdd:cd07463    5 CQPVVIPMCRGIGYNLTRMPNF-LGHDSQREAAIKLNEFAPLVEYGCHVHLRFFLCSLYAPMCTdQVSTSIPACRPMCEQ 83

                         90       100
                 ....*....|....*....|....*.
gi 157822425 556 AEQQCQSSLALLGIPWP--FNCNRLP 579
Cdd:cd07463   84 ARQKCSPIMEQFNFGWPesLDCSRLP 109
CRD_FZ9_like cd07457
Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 9; The cysteine-rich ...
 477-579 1.15e-16

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: 76.38  E-value: 1.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425 477 CEPVQVEMCLGLSYNTTAFPNIwVGLATQMEVTDILRGYKSLTSLPCYQTFRRFLCGLLEPRCTS-LGTILPPCRSVCQE 555
Cdd:cd07457    3 CERITIPMCQGIGYNMTRMPNL-LGHESQSEAAISIHEFAPLVQYGCAEHLRFFLCSLYAPMCTEqVSIPIPACRSMCEQ 81

                         90       100
                 ....*....|....*....|....*.
gi 157822425 556 AEQQCQSSLALLGIPWP--FNCNRLP 579
Cdd:cd07457   82 ARDKCSPIMEQFSFSWPdsLDCDRLP 107
CRD_FZ7 cd07466
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 7 (Fz7) receptor; The cysteine-rich ...
 477-587 1.61e-16

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: 75.89  E-value: 1.61e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425 477 CEPVQVEMCLGLSYNTTAFPNIwVGLATQMEVTDILRGYKSLTSLPCYQTFRRFLCGLLEPRCTSLGTILPPCRSVCQEA 556
Cdd:cd07466    5 CQPISIPLCTDIAYNQTIMPNL-LGHTNQEDAGLEVHQFYPLVKVQCSPELKFFLCSMYAPVCTVLEQAIPPCRSLCERA 83

                         90       100       110
                 ....*....|....*....|....*....|...
gi 157822425 557 EQQCQSSLALLGIPWP--FNCNRLPVPASLEAC 587
Cdd:cd07466   84 RQGCEALMNKFGFQWPerLRCENFPVHGAGEIC 116
CRD_FZ2 cd07464
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 2 (Fz2) receptor; The cysteine-rich ...
 477-587 1.09e-15

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: 73.58  E-value: 1.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425 477 CEPVQVEMCLGLSYNTTAFPNIwVGLATQMEVTDILRGYKSLTSLPCYQTFRRFLCGLLEPRCTSLGTILPPCRSVCQEA 556
Cdd:cd07464    5 CQPISIPLCTDIAYNQTIMPNL-LGHTNQEDAGLEVHQFYPLVKVQCSLELRFFLCSMYAPVCTVLEQAIPPCRSICERA 83

                         90       100       110
                 ....*....|....*....|....*....|...
gi 157822425 557 EQQCQSSLALLGIPWP--FNCNRLPVPASLEAC 587
Cdd:cd07464   84 RQGCEALMNKFGFQWPerLRCENFPRHGAEQIC 116
CRD_FZ1 cd07465
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 1 (Fz1) receptor; The cysteine-rich ...
 477-587 1.78e-15

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: 73.16  E-value: 1.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425 477 CEPVQVEMCLGLSYNTTAFPNIwVGLATQMEVTDILRGYKSLTSLPCYQTFRRFLCGLLEPRCTSLGTILPPCRSVCQEA 556
Cdd:cd07465    5 CQPISIPLCTDIAYNQTIMPNL-LGHTNQEDAGLEVHQFYPLVKVQCSAELKFFLCSMYAPVCTVLEQALPPCRSLCERA 83

                         90       100       110
                 ....*....|....*....|....*....|...
gi 157822425 557 EQQCQSSLALLGIPWP--FNCNRLPVPASLEAC 587
Cdd:cd07465   84 RQGCEALMNKFGFQWPdtLRCEKFPVHGAGELC 116
CRD_FZ5 cd07460
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 5 (Fz5) receptor.proteins; The ...
 475-580 3.21e-15

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: 72.36  E-value: 3.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425 475 LTCEPVQVEMCLGLSYNTTAFPNIWvGLATQMEVTDILRGYKSLTSLPCYQTFRRFLCGLLEPRCTS-LGTILPPCRSVC 553
Cdd:cd07460    3 LVCQEITVPMCKGIGYNLTYMPNQF-NHDTQDEAGLEVHQFWPLVEIQCSPDLRFFLCSMYTPICLPdYRKPLPPCRSVC 81

                         90       100
                 ....*....|....*....|....*....
gi 157822425 554 QEAEQQCQSSLALLGIPWP--FNCNRLPV 580
Cdd:cd07460   82 ERAKAGCSPLMRQYGFAWPerMNCDRLPV 110
CRD_FZ10 cd07462
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 10 (Fz10) receptor; The cysteine-rich ...
 477-579 5.90e-15

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: 71.59  E-value: 5.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425 477 CEPVQVEMCLGLSYNTTAFPNIwVGLATQMEVTDILRGYKSLTSLPCYQTFRRFLCGLLEPRCT-SLGTILPPCRSVCQE 555
Cdd:cd07462    5 CQPIEIPMCKDIGYNMTRMPNL-MGHENQREAAIQLHEFAPLVEYGCHSHLKFFLCSLYAPMCTeQVSTPIPACRVMCEQ 83

                         90       100
                 ....*....|....*....|....*.
gi 157822425 556 AEQQCQSSLALLGIPWP--FNCNRLP 579
Cdd:cd07462   84 ARLKCSPIMEQFNFKWPdsLDCSKLP 109
CRD_FZ5_like cd07456
Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 5; The cysteine-rich ...
 477-579 1.29e-14

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: 70.50  E-value: 1.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425 477 CEPVQVEMCLGLSYNTTAFPNIWvGLATQMEVTDILRGYKSLTSLPCYQTFRRFLCGLLEPRC-TSLGTILPPCRSVCQE 555
Cdd:cd07456    2 CEEITIPMCKGIGYNMTYMPNQF-NHDTQEEAGLEVHQFWPLVEIQCSPDLKFFLCSMYTPIClEDYDKPLPPCRSVCER 80

                         90       100
                 ....*....|....*....|....*.
gi 157822425 556 AEQQCQSSLALLGIPWP--FNCNRLP 579
Cdd:cd07456   81 ARDGCAPIMRQYGFAWPerMSCDALP 106
CRD_FZ8 cd07461
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 8 (Fz8) receptor; The cysteine-rich ...
 474-580 1.52e-14

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: 70.40  E-value: 1.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425 474 DLTCEPVQVEMCLGLSYNTTAFPNIWvGLATQMEVTDILRGYKSLTSLPCYQTFRRFLCGLLEPRC-TSLGTILPPCRSV 552
Cdd:cd07461    2 ELQCQEITVPLCKGIGYNYTYMPNQF-NHDTQDEAGLEVHQFWPLVEIQCSPDLKFFLCSMYTPIClEDYKKPLPPCRSV 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 157822425 553 CQEAEQQCQSSLALLGIPWP--FNCNRLPV 580
Cdd:cd07461   81 CERAKAGCAPLMRQYGFPWPdrMRCDLLPE 110
CRD_FZ6 cd07450
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 6 (Fz6) receptor; The cysteine-rich ...
 476-579 8.09e-14

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: 68.25  E-value: 8.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425 476 TCEPVQVEMCLGLSYNTTAFPNIWVGL-----ATQMEvtdilrGYKSLTSLPCYQTFRRFLCGLLEPRCTSLGTILPPCR 550
Cdd:cd07450    4 TCEPITVPRCLKMPYNMTFFPNLMGHYdqdiaAVEME------PFLPLANLRCSPNVHTFLCQAFVPTCTEQIHVVRPCR 77

                         90       100       110
                 ....*....|....*....|....*....|.
gi 157822425 551 SVCQEAEQQCQSSLALLGIPWP--FNCNRLP 579
Cdd:cd07450   78 ELCEKVYSDCKKLIDTFGISWPeeLECDRLQ 108
CRD_SFRP4 cd07442
Cysteine-rich domain of the secreted frizzled-related protein 4 (SFRP4), a Wnt antagonist; The ...
 477-580 4.76e-12

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: 63.51  E-value: 4.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425 477 CEPVQVEMCLGLSYNTTAFPNiWVGLATQMEVTDILRGYKSLTSLPCYQTFRRFLCGLLEPRCT--SLGTILPPCRSVCQ 554
Cdd:cd07442    5 CEAVRIPMCRHMPWNITRMPN-HLHHSTQENAVLAIEQYEELVDTGCSPVLPFFLCAMYAPICTleFLYDPIKPCRSVCQ 83

                         90       100
                 ....*....|....*....|....*...
gi 157822425 555 EAEQQCQSSLALLGIPWP--FNCNRLPV 580
Cdd:cd07442   84 RARDGCEPIMRRYNHSWPesLACDDLPV 111
CRD_SFRP2 cd07446
Cysteine-rich domain of the secreted frizzled-related protein 2 (SFRP2), a regulator of Wnt ...
 479-579 5.29e-12

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: 63.39  E-value: 5.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425 479 PVQVEMCLGLSYNTTAFPNIwVGLATQMEVTDILRGYKSLTSLPCYQTFRRFLCGLLEPRCTS-LGTILPPCRSVCQEAE 557
Cdd:cd07446    9 PANMLLCHGIEYTNMRLPNL-LGHETMKEVLQQAGSWIPLVQKQCHPDTKKFLCSLFAPVCLDdLDEAIQPCRSLCEAVK 87

                         90       100
                 ....*....|....*....|....
gi 157822425 558 QQCQSSLALLGIPWP--FNCNRLP 579
Cdd:cd07446   88 DGCAPVMSAFGFPWPdmLDCTRFP 111
CRD_LIN_17 cd07454
Cysteine-rich domain (CRD) of LIN_17; A cysteine-rich domain (CRD) is an essential component ...
 477-590 5.97e-12

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: 62.88  E-value: 5.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425 477 CEPVQVEMCLGLSYNTTAFPNIWVGLATQMEVTDIlRGYKSLTSLPCYQTFRRFLCGLLEPRC-TSLGTILPPCRSVCQE 555
Cdd:cd07454    5 CIPIDIELCKDLPYNYTYFPNTILHNDQHTLQTHT-EHFKPLMKTKCHPHIHFFICSVFAPMCpIGMPQAVTSCKSVCEQ 83

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 157822425 556 AEQQCQSSLALLGIPWP--FNCNRLPVPASLeaCSQP 590
Cdd:cd07454   84 VKADCFSILEEFGIGWPepLNCAQFPDPPEL--CMKP 118
CRD_SFRP3 cd07441
Cysteine-rich domain of the secreted frizzled-related protein 3 (SFRP3, alias FRZB), a Wnt ...
 476-580 1.57e-10

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: 58.91  E-value: 1.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425 476 TCEPVQVEMCLGLSYNTTAFPNiWVGLATQMEVTDILRGYKSLTSLPCYQTFRRFLCGLLEPRCTSLGTILP--PCRSVC 553
Cdd:cd07441    3 SCEPVRIPMCKSMPWNMTKMPN-HLHHSTQANAVLAIEQFEGLLGTQCSPDLLFFLCAMYAPICTIDFQHEPikPCKSVC 81

                         90       100
                 ....*....|....*....|....*....
gi 157822425 554 QEAEQQCQSSLALLGIPWP--FNCNRLPV 580
Cdd:cd07441   82 ERARAGCEPVLIRYRHTWPesLACEELPV 110
CRD_sizzled cd07452
Cysteine-rich domain of the sizzled protein; The cysteine-rich domain (CRD) is an essential ...
 479-579 1.85e-08

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: 53.35  E-value: 1.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425 479 PVQVEMCLGLSYNTTAFPNIwVGLATQMEVTDILRGYKSLTSLPCYQTFRRFLCGLLEPRCtsLGTILPPCRSVCQEAEQ 558
Cdd:cd07452   13 PPEMSMCQDVGYSEMRLPNL-LGHTSMAEVVPKSADWQTLLHTGCHPHARTFLCSLFAPVC--LDTFIQPCRSMCVAVRD 89

                         90       100
                 ....*....|....*....|...
gi 157822425 559 QCQSSLALLGIPWP--FNCNRLP 579
Cdd:cd07452   90 SCAPVLACHGHSWPesLDCDRFP 112
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 266-300 2.07e-08

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 50.28  E-value: 2.07e-08
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 157822425 266 CTHYEFHCDLLLCLKQDSVCDGIKDCIDGSDEANC 300
Cdd:cd00112    1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
CRD_Carboxypeptidase_Z cd07447
Cysteine-rich domain of carboxypeptidase Z, a member of the carboxypeptidase E family; The ...
 476-590 9.68e-08

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: 50.91  E-value: 9.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425 476 TCEPVQVEMCLGLSYNTTAFPNIwVGLATQmEVTDILRGYKSLTSL------PCYQTFRRFLCGLLEPRCTSlGTILPPC 549
Cdd:cd07447    3 TCTDLLLSYCSDVSYTQTTFPNL-LGHRSR-EVTEAGAEYLLLSVLhgllggECNPDIRLLGCSVLAPRCEN-DKVIKPC 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 157822425 550 RSVCQEAEQQCQSSLALLGIPWPF--NCNRLPVpASLEACSQP 590
Cdd:cd07447   80 RSTCEALRKRCSHAFDAIQMAWPYflDCDRFFA-GEQEGCYDP 121
CRD_corin_1 cd07445
One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ...
 476-572 1.06e-07

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: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425 476 TCEPVQVEMCLGLSYNTTAFPNIWVglATQMEVTDILRGYKSLTSLPCYQTFRRFLCGLLEPRCTSLG---TILPPCRSV 552
Cdd:cd07445    4 ACMNITHSQCQMLPYHSTLKPSLLS--VKNMEMEKFLKFFSYLHRLSCYQHIMLFGCSLALPECISDGddrHGLLPCRSF 81

                         90       100
                 ....*....|....*....|
gi 157822425 553 CQEAEQQCQSSLALLGIPWP 572
Cdd:cd07445   82 CEAAKEGCEPVLGMVNASWP 101
CRD_SFRP5 cd07444
Cysteine-rich domain of the secreted frizzled-related protein 5 (SFRP5), a regulator of Wnt ...
 479-584 3.89e-07

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: 49.17  E-value: 3.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425 479 PVQVEMCLGLSYNTTAFPNIwVGLATQMEVTDILRGYKSLTSLPCYQTFRRFLCGLLEPRCtsLGTILPPCRSVCQEAEQ 558
Cdd:cd07444   11 PADLPLCHNVGYKRMRLPNL-LEHESMAEVKQQASSWVPLLAKRCHADTQVFLCSLFAPVC--LDRPIYPCRSLCEAVRD 87

                         90       100
                 ....*....|....*....|....*...
gi 157822425 559 QCQSSLALLGIPWP--FNCNRLPVPASL 584
Cdd:cd07444   88 SCAPVMESYGFPWPemLHCHKFPLDNDL 115
CRD_crescent cd07453
Cysteine-rich domain of the crescent protein; The cysteine-rich domain (CRD) is an essential ...
 479-580 4.48e-07

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: 49.17  E-value: 4.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425 479 PVQVEMCLGLSYNTTAFPNIwVGLATQMEVTDILRGYKSLTSLPCYQTFRRFLCGLLEPRCtsLGTILPPCRSVCQEAEQ 558
Cdd:cd07453    7 PKSMALCYDIGYSEMRIPNL-LEHETMAEVIQQSSSWLPLLARECHPDARIFLCSLFAPIC--WDRPIYPCRSLCEAVRS 83

                         90       100
                 ....*....|....*....|....
gi 157822425 559 QCQSSLALLGIPWP--FNCNRLPV 580
Cdd:cd07453   84 SCAPLMACYGYPWPeiLHCDKFPV 107
CRD_SMO cd07451
Cysteine-rich domain of the smoothened receptor (Smo) integral membrane protein; The ...
 476-584 6.90e-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: 48.52  E-value: 6.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425 476 TCEPVQVEMCLG--LSYNTTAFpNIWVGLATQMEVTDILRGYKSLTSLP-CYQTFRRFLCGLLEPRCTSlGTILPPCRSV 552
Cdd:cd07451    4 KCEPLKNTTCLGskLPYTYTSL-DLVPDSTTQEEVQEKLHLWSGLRNVPkCWAVIQPLLCALYMPKCEN-GKVELPSQEM 81

                         90       100       110
                 ....*....|....*....|....*....|..
gi 157822425 553 CQEAEQQCQSSLALLGIPWPFNCNRLPVPASL 584
Cdd:cd07451   82 CQATRGPCKIVENERGWPDFLRCDNDRFPPRG 113
CRD_SFRP1 cd07443
Cysteine-rich domain of the secreted frizzled-related protein 1 (SFRP1), a regulator of Wnt ...
 479-579 2.44e-06

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: 46.82  E-value: 2.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822425 479 PVQVEMCLGLSYNTTAFPNIwVGLATQMEVTDILRGYKSLTSLPCYQTFRRFLCGLLEPRCtsLGTILPPCRSVCQEAEQ 558
Cdd:cd07443   11 PADLRLCHNVGYKKMVLPNL-LDHETMAEVKQQASSWVPLLNKNCHKGTQVFLCSLFAPVC--LDRPVYPCRWLCEAVRD 87

                         90       100
                 ....*....|....*....|...
gi 157822425 559 QCQSSLALLGIPWP--FNCNRLP 579
Cdd:cd07443   88 SCEPVMQFFGFYWPemLKCDKFP 110
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 266-297 3.38e-06

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 43.78  E-value: 3.38e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 157822425   266 CTHYEFHCDLLLCLKQDSVCDGIKDCIDGSDE 297
Cdd:smart00192   2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
266-300 4.06e-06

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 43.78  E-value: 4.06e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 157822425  266 CTHYEFHCDLLLCLKQDSVCDGIKDCIDGSDEANC 300
Cdd:pfam00057   3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
CRD_Collagen_XVIII cd07455
Cysteine-rich domain of the variant 3 of collagen XVIII (V3C18 ); The cysteine-rich domain ...
 507-579 7.28e-05

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: 42.50  E-value: 7.28e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157822425 507 EVTDILRGYKSLTSLPCYQTFRRFLCGLLEPRCTSLG-TILPPCRSVCQEAEQQCQSSLAllGIPWPFNCNRLP 579
Cdd:cd07455   36 EVRAVLAEWAWLLESGCHPSLEWFFCLLLVPSCGGGPpPPPPPCRQFCEVLQDSCWNLLE--GGRLPVACASLP 107
 
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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