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Conserved domains on  [gi|170295827|ref|NP_001116228|]
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atrial natriuretic peptide-converting enzyme isoform 2 [Mus musculus]

Protein Classification

CRD_corin_2 and Tryp_SPc domain-containing protein( domain architecture ID 10868866)

protein containing domains CRD_corin_1, CRD_corin_2, SR, and Tryp_SPc

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 803-1034 7.60e-83

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


:

Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 268.38  E-value: 7.60e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  803 ILGGRTSRPGRWPWQCSLQSEPSGHICGCVLIAKKWVLTVAHCFEGREDADvWKVVFGINNLDHPSGFMQTRFVKTILLH 882
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSN-YTVRLGSHDLSSNEGGGQVIKVKKVIVH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  883 PRYSRAVVDYDISVVELSDDINETSYVRPVCLPSPEEYLEPDTYCYITGWGHMGNKM--PFKLQEGEVRIIPLEQCQS-Y 959
Cdd:cd00190    80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGplPDVLQEVNVPIVSNAECKRaY 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 170295827  960 FDMKTITNRMICAGYESGTVDSCMGDSGGPLVCERPgGQWTLFGLTSWGSVCfSKVLGPGVYSNVSYFVGWIERQ 1034
Cdd:cd00190   160 SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGC-ARPNYPGVYTRVSSYLDWIQKT 232
CRD_corin_2 cd07888
One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ...
 456-577 4.61e-81

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: 259.18  E-value: 4.61e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  456 QCEPITLELCMNLPYNHTHYPNYLGHRTQKEASISWESSLFPALVQTNCYKYLMFFACTILVPKCDVNTGQRIPPCRLLC 535
Cdd:cd07888     1 QCEPITLELCMNLPYNTTRYPNYLGHRTQKEASISWESSLFPALVQTNCYKYLMFFACTILVPKCDPVTQQRIPPCRSLC 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 170295827  536 EHSKERCESVLGIVGLQWPEDTDCNQFPEESSDNQTCLLPNE 577
Cdd:cd07888    81 RNSKERCESVLGIVGLQWPEDTDCAQFPEENSDNQTCLLPDE 122
CRD_corin_1 cd07445
One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ...
 136-265 2.44e-76

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: 246.38  E-value: 2.44e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  136 NTSTCMNITHSQCQILPYHSTLAPLLPIVKNMDMEKFLKFFTYLHRLSCYQHILLFGCSLAFPECVVDGDDRHGLLPCRS 215
Cdd:cd07445     1 NTSACMNITHSQCQMLPYHSTLKPSLLSVKNMEMEKFLKFFSYLHRLSCYQHIMLFGCSLALPECISDGDDRHGLLPCRS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 170295827  216 FCEAAKEGCESVLGMVNSSWPDSLRCSQFRDHTETNSSVRKSCFSLQQEH 265
Cdd:cd07445    81 FCEAAKEGCEPVLGMVNASWPDFLRCSQFRNNTETAVENRALCFSPQQER 130
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 692-787 3.36e-11

Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR domains that contain 6 conserved cysteines. May bind bacterial antigens in the protein MARCO.


:

Pssm-ID: 214555 [Multi-domain]  Cd Length: 101  Bit Score: 60.82  E-value: 3.36e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827    692 VTLSKNGNSSS-LLTVHKSAKEHHVCADGWRETLSQLACKQMGLGEPSVTKL--IPGQEGQQWLRLYPNWENLNGStLQE 768
Cdd:smart00202    1 VRLVGGGSPCEgRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGsaYFGPGSGPIWLDNVRCSGTEAS-LSD 79

                            90       100
                    ....*....|....*....|..
gi 170295827    769 LL---VYRHSCPSRSEISLLCS 787
Cdd:smart00202   80 CPhsgWGSHNCSHGEDAGVVCS 101
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
582-616 8.23e-09

Low-density lipoprotein receptor domain class A;


:

Pssm-ID: 395011  Cd Length: 37  Bit Score: 51.87  E-value: 8.23e-09
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 170295827   582 CSPSHFKCRSGRCVLGSRRCDGQADCDDDSDEENC 616
Cdd:pfam00057    3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 657-691 9.44e-09

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: 51.82  E-value: 9.44e-09
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 170295827  657 CQDNELECANHECVPRDLWCDGWVDCSDSSDEWGC 691
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
349-379 1.25e-08

Low-density lipoprotein receptor domain class A;


:

Pssm-ID: 395011  Cd Length: 37  Bit Score: 51.48  E-value: 1.25e-08
                           10        20        30
                   ....*....|....*....|....*....|.
gi 170295827   349 EHRCGDGRCIAAEWVCDGDHDCVDKSDEVNC 379
Cdd:pfam00057    7 EFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 308-342 2.80e-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: 2.80e-08
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 170295827  308 CSKDLFHCGTGKCLHYSLLCDGYDDCGDLSDEQNC 342
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 389-416 5.44e-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: 49.51  E-value: 5.44e-08
                          10        20
                  ....*....|....*....|....*...
gi 170295827  389 CRSGQCIPSTFQCDGDEDCKDGSDEENC 416
Cdd:cd00112     8 CANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 271-306 2.32e-07

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: 47.97  E-value: 2.32e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 170295827  271 CGGGEsFLCTSGLCVPKKLQCNGYNDCDDWSDEAHC 306
Cdd:cd00112     1 CPPNE-FRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 629-654 2.45e-03

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: 36.42  E-value: 2.45e-03
                          10        20
                  ....*....|....*....|....*.
gi 170295827  629 NKQCLKHTLICDGFPDCPDSMDEKNC 654
Cdd:cd00112    10 NGRCIPSSWVCDGEDDCGDGSDEENC 35
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 803-1034 7.60e-83

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 268.38  E-value: 7.60e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  803 ILGGRTSRPGRWPWQCSLQSEPSGHICGCVLIAKKWVLTVAHCFEGREDADvWKVVFGINNLDHPSGFMQTRFVKTILLH 882
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSN-YTVRLGSHDLSSNEGGGQVIKVKKVIVH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  883 PRYSRAVVDYDISVVELSDDINETSYVRPVCLPSPEEYLEPDTYCYITGWGHMGNKM--PFKLQEGEVRIIPLEQCQS-Y 959
Cdd:cd00190    80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGplPDVLQEVNVPIVSNAECKRaY 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 170295827  960 FDMKTITNRMICAGYESGTVDSCMGDSGGPLVCERPgGQWTLFGLTSWGSVCfSKVLGPGVYSNVSYFVGWIERQ 1034
Cdd:cd00190   160 SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGC-ARPNYPGVYTRVSSYLDWIQKT 232
CRD_corin_2 cd07888
One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ...
 456-577 4.61e-81

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: 259.18  E-value: 4.61e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  456 QCEPITLELCMNLPYNHTHYPNYLGHRTQKEASISWESSLFPALVQTNCYKYLMFFACTILVPKCDVNTGQRIPPCRLLC 535
Cdd:cd07888     1 QCEPITLELCMNLPYNTTRYPNYLGHRTQKEASISWESSLFPALVQTNCYKYLMFFACTILVPKCDPVTQQRIPPCRSLC 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 170295827  536 EHSKERCESVLGIVGLQWPEDTDCNQFPEESSDNQTCLLPNE 577
Cdd:cd07888    81 RNSKERCESVLGIVGLQWPEDTDCAQFPEENSDNQTCLLPDE 122
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 802-1031 1.28e-79

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 259.15  E-value: 1.28e-79
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827    802 RILGGRTSRPGRWPWQCSLQSEPSGHICGCVLIAKKWVLTVAHCFEGReDADVWKVVFGINNLDHPsGFMQTRFVKTILL 881
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSG-EEGQVIKVSKVII 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827    882 HPRYSRAVVDYDISVVELSDDINETSYVRPVCLPSPEEYLEPDTYCYITGWGHMGN---KMPFKLQEGEVRIIPLEQCQS 958
Cdd:smart00020   79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEgagSLPDTLQEVNVPIVSNATCRR 158

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 170295827    959 -YFDMKTITNRMICAGYESGTVDSCMGDSGGPLVCErpGGQWTLFGLTSWGSVCfSKVLGPGVYSNVSYFVGWI 1031
Cdd:smart00020  159 aYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGC-ARPGKPGVYTRVSSYLDWI 229
CRD_corin_1 cd07445
One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ...
 136-265 2.44e-76

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: 246.38  E-value: 2.44e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  136 NTSTCMNITHSQCQILPYHSTLAPLLPIVKNMDMEKFLKFFTYLHRLSCYQHILLFGCSLAFPECVVDGDDRHGLLPCRS 215
Cdd:cd07445     1 NTSACMNITHSQCQMLPYHSTLKPSLLSVKNMEMEKFLKFFSYLHRLSCYQHIMLFGCSLALPECISDGDDRHGLLPCRS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 170295827  216 FCEAAKEGCESVLGMVNSSWPDSLRCSQFRDHTETNSSVRKSCFSLQQEH 265
Cdd:cd07445    81 FCEAAKEGCEPVLGMVNASWPDFLRCSQFRNNTETAVENRALCFSPQQER 130
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 795-1035 4.79e-64

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 217.59  E-value: 4.79e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  795 PAARMNKRILGGRTSRPGRWPWQCSLQSE--PSGHICGCVLIAKKWVLTVAHCFEGREDADVwKVVFGINNLDHPSGfmQ 872
Cdd:COG5640    23 PAADAAPAIVGGTPATVGEYPWMVALQSSngPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDL-RVVIGSTDLSTSGG--T 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  873 TRFVKTILLHPRYSRAVVDYDISVVELSDDINETSYVRpvcLPSPEEYLEPDTYCYITGWGHMGN---KMPFKLQEGEVR 949
Cdd:COG5640   100 VVKVARIVVHPDYDPATPGNDIALLKLATPVPGVAPAP---LATSADAAAPGTPATVAGWGRTSEgpgSQSGTLRKADVP 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  950 IIPLEQCQSYFDMktITNRMICAGYESGTVDSCMGDSGGPLVcERPGGQWTLFGLTSWG-SVCFSKvlGPGVYSNVSYFV 1028
Cdd:COG5640   177 VVSDATCAAYGGF--DGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGgGPCAAG--YPGVYTRVSAYR 251


                  ....*..
gi 170295827 1029 GWIERQI 1035
Cdd:COG5640   252 DWIKSTA 258
Trypsin pfam00089
Trypsin;
803-1031 2.76e-63

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 213.84  E-value: 2.76e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827   803 ILGGRTSRPGRWPWQCSLQSEPSGHICGCVLIAKKWVLTVAHCFEGREDadvWKVVFGINNLDHPSGFMQTRFVKTILLH 882
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASD---VKVVLGAHNIVLREGGEQKFDVEKIIVH 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827   883 PRYSRAVVDYDISVVELSDDINETSYVRPVCLPSPEEYLEPDTYCYITGWGHMG-NKMPFKLQEGEVRIIPLEQCQSYFD 961
Cdd:pfam00089   78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKtLGPSDTLQEVTVPVVSRETCRSAYG 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827   962 mKTITNRMICAGYesGTVDSCMGDSGGPLVCERPggqwTLFGLTSWGSVCfSKVLGPGVYSNVSYFVGWI 1031
Cdd:pfam00089  158 -GTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGC-ASGNYPGVYTPVSSYLDWI 219
Fz pfam01392
Fz domain; Also known as the CRD (cysteine rich domain), the C6 box in MuSK receptor. This ...
 457-564 2.45e-31

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: 118.83  E-value: 2.45e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827   457 CEPITLELCMNLPYNHTHYPNYLGHRTQKEASISWES---SLFPALVQTNCYKYLMFFACTILVPKCDVNTGQR--IPPC 531
Cdd:pfam01392    1 CEPITLPMCLGLGYNATVFPNLLGHQTQEEAELSLAYlvlSEFEPLVDLSCSPSLRLFLCSLYFPPCTLGPSPKpvCPPC 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 170295827   532 RLLCEHSKERCESVLGIV--GLQWPEDTDCNQFPE 564
Cdd:pfam01392   81 RSLCEEVRYGCEPLLEEAkfGFSWPEFLDCDSLPA 115
FRI smart00063
Frizzled; Drosophila melanogaster frizzled mediates signalling that polarises a precursor cell ...
 457-565 1.44e-27

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: 107.78  E-value: 1.44e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827    457 CEPITLELCMNLPYNHTHYPNYLGHRTQKEASIswESSLFPALVQTNCYKYLMFFACTILVPKCDvNTGQRIPPCRLLCE 536
Cdd:smart00063    1 CEPITIPLCKDLGYNLTSMPNLLGHTTQEEAGL--ELEQFHPLLNVQCSPDLRFFLCSVYAPICT-EDLRPILPCRSLCE 77

                            90       100
                    ....*....|....*....|....*....
gi 170295827    537 HSKERCESVLGIVGLQWPEDTDCNQFPEE 565
Cdd:smart00063   78 AAREGCEPLMEKFGFPWPEFLRCDRFPVQ 106
Fz pfam01392
Fz domain; Also known as the CRD (cysteine rich domain), the C6 box in MuSK receptor. This ...
 140-247 1.92e-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: 93.40  E-value: 1.92e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827   140 CMNITHSQCQILPYHSTLAPLLPIVKNMDMEKFLKFFTYLH------RLSCYQHILLFGCSLAFPECVVDGDDRHGLLPC 213
Cdd:pfam01392    1 CEPITLPMCLGLGYNATVFPNLLGHQTQEEAELSLAYLVLSefeplvDLSCSPSLRLFLCSLYFPPCTLGPSPKPVCPPC 80

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 170295827   214 RSFCEAAKEGCESVLGMVNS--SWPDSLRCSQFRDH 247
Cdd:pfam01392   81 RSLCEEVRYGCEPLLEEAKFgfSWPEFLDCDSLPAD 116
FRI smart00063
Frizzled; Drosophila melanogaster frizzled mediates signalling that polarises a precursor cell ...
 140-249 7.95e-14

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: 68.88  E-value: 7.95e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827    140 CMNITHSQCQILPYHSTLAPLLPIVKNM-DMEKFLKFFTYLHRLSCYQHILLFGCSLAFPECvvdGDDRHGLLPCRSFCE 218
Cdd:smart00063    1 CEPITIPLCKDLGYNLTSMPNLLGHTTQeEAGLELEQFHPLLNVQCSPDLRFFLCSVYAPIC---TEDLRPILPCRSLCE 77

                            90       100       110
                    ....*....|....*....|....*....|.
gi 170295827    219 AAKEGCESVLGMVNSSWPDSLRCSQFRDHTE 249
Cdd:smart00063   78 AAREGCEPLMEKFGFPWPEFLRCDRFPVQEE 108
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 692-787 3.36e-11

Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR domains that contain 6 conserved cysteines. May bind bacterial antigens in the protein MARCO.


Pssm-ID: 214555 [Multi-domain]  Cd Length: 101  Bit Score: 60.82  E-value: 3.36e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827    692 VTLSKNGNSSS-LLTVHKSAKEHHVCADGWRETLSQLACKQMGLGEPSVTKL--IPGQEGQQWLRLYPNWENLNGStLQE 768
Cdd:smart00202    1 VRLVGGGSPCEgRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGsaYFGPGSGPIWLDNVRCSGTEAS-LSD 79

                            90       100
                    ....*....|....*....|..
gi 170295827    769 LL---VYRHSCPSRSEISLLCS 787
Cdd:smart00202   80 CPhsgWGSHNCSHGEDAGVVCS 101
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
582-616 8.23e-09

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 51.87  E-value: 8.23e-09
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 170295827   582 CSPSHFKCRSGRCVLGSRRCDGQADCDDDSDEENC 616
Cdd:pfam00057    3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 657-691 9.44e-09

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: 51.82  E-value: 9.44e-09
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 170295827  657 CQDNELECANHECVPRDLWCDGWVDCSDSSDEWGC 691
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
349-379 1.25e-08

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 51.48  E-value: 1.25e-08
                           10        20        30
                   ....*....|....*....|....*....|.
gi 170295827   349 EHRCGDGRCIAAEWVCDGDHDCVDKSDEVNC 379
Cdd:pfam00057    7 EFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 582-616 2.09e-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: 50.67  E-value: 2.09e-08
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 170295827  582 CSPSHFKCRSGRCVLGSRRCDGQADCDDDSDEENC 616
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 349-379 2.69e-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: 50.67  E-value: 2.69e-08
                          10        20        30
                  ....*....|....*....|....*....|.
gi 170295827  349 EHRCGDGRCIAAEWVCDGDHDCVDKSDEVNC 379
Cdd:cd00112     5 EFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 308-342 2.80e-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: 2.80e-08
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 170295827  308 CSKDLFHCGTGKCLHYSLLCDGYDDCGDLSDEQNC 342
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 389-416 5.44e-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: 49.51  E-value: 5.44e-08
                          10        20
                  ....*....|....*....|....*...
gi 170295827  389 CRSGQCIPSTFQCDGDEDCKDGSDEENC 416
Cdd:cd00112     8 CANGRCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
389-416 1.17e-07

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 48.78  E-value: 1.17e-07
                           10        20
                   ....*....|....*....|....*...
gi 170295827   389 CRSGQCIPSTFQCDGDEDCKDGSDEENC 416
Cdd:pfam00057   10 CGSGECIPRSWVCDGDPDCGDGSDEENC 37
SRCR_2 pfam15494
Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain ...
 715-795 1.39e-07

Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain family found largely on vertebrate sequences up-stream of the trypsin-like transmembrane serine protease, Spinesin.


Pssm-ID: 464747  Cd Length: 99  Bit Score: 50.41  E-value: 1.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827   715 VCADGWRETLSQLACKQMGLGEPSVTKLIP-----GQEGQQWLRLYPnwENLNGsTLQELLVYRHSCPSRSEISLLCSkq 789
Cdd:pfam15494   19 VCSDDWNPAYGRAACQQLGYLRLTHHKSVNltdisSNSSQSFMKLNS--SSLNT-DLYEALQPRDSCSSGSVVSLRCS-- 93


                   ....*.
gi 170295827   790 DCGRRP 795
Cdd:pfam15494   94 ECGLRS 99
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 271-306 2.32e-07

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: 47.97  E-value: 2.32e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 170295827  271 CGGGEsFLCTSGLCVPKKLQCNGYNDCDDWSDEAHC 306
Cdd:cd00112     1 CPPNE-FRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
308-342 3.30e-07

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 47.63  E-value: 3.30e-07
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 170295827   308 CSKDLFHCGTGKCLHYSLLCDGYDDCGDLSDEQNC 342
Cdd:pfam00057    3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 581-613 1.23e-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: 45.70  E-value: 1.23e-06
                            10        20        30
                    ....*....|....*....|....*....|...
gi 170295827    581 ECSPSHFKCRSGRCVLGSRRCDGQADCDDDSDE 613
Cdd:smart00192    1 TCPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 657-688 1.44e-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: 45.70  E-value: 1.44e-06
                            10        20        30
                    ....*....|....*....|....*....|..
gi 170295827    657 CQDNELECANHECVPRDLWCDGWVDCSDSSDE 688
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 342-376 1.82e-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: 45.32  E-value: 1.82e-06
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 170295827    342 CDCNltkEHRCGDGRCIAAEWVCDGDHDCVDKSDE 376
Cdd:smart00192    2 CPPG---EFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 389-413 2.13e-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: 44.93  E-value: 2.13e-06
                            10        20
                    ....*....|....*....|....*
gi 170295827    389 CRSGQCIPSTFQCDGDEDCKDGSDE 413
Cdd:smart00192    9 CDNGRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
271-306 2.46e-06

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 44.93  E-value: 2.46e-06
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 170295827   271 CGGGEsFLCTSGLCVPKKLQCNGYNDCDDWSDEAHC 306
Cdd:pfam00057    3 CSPNE-FQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 308-339 2.80e-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: 44.55  E-value: 2.80e-06
                            10        20        30
                    ....*....|....*....|....*....|..
gi 170295827    308 CSKDLFHCGTGKCLHYSLLCDGYDDCGDLSDE 339
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 271-303 2.26e-05

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: 42.24  E-value: 2.26e-05
                            10        20        30
                    ....*....|....*....|....*....|...
gi 170295827    271 CGGGEsFLCTSGLCVPKKLQCNGYNDCDDWSDE 303
Cdd:smart00192    2 CPPGE-FQCDNGRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
657-691 1.25e-04

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 40.31  E-value: 1.25e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 170295827   657 CQDNELECANHECVPRDLWCDGWVDCSDSSDEWGC 691
Cdd:pfam00057    3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 629-654 2.45e-03

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: 36.42  E-value: 2.45e-03
                          10        20
                  ....*....|....*....|....*.
gi 170295827  629 NKQCLKHTLICDGFPDCPDSMDEKNC 654
Cdd:cd00112    10 NGRCIPSSWVCDGEDDCGDGSDEENC 35
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 803-1034 7.60e-83

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 268.38  E-value: 7.60e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  803 ILGGRTSRPGRWPWQCSLQSEPSGHICGCVLIAKKWVLTVAHCFEGREDADvWKVVFGINNLDHPSGFMQTRFVKTILLH 882
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSN-YTVRLGSHDLSSNEGGGQVIKVKKVIVH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  883 PRYSRAVVDYDISVVELSDDINETSYVRPVCLPSPEEYLEPDTYCYITGWGHMGNKM--PFKLQEGEVRIIPLEQCQS-Y 959
Cdd:cd00190    80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGplPDVLQEVNVPIVSNAECKRaY 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 170295827  960 FDMKTITNRMICAGYESGTVDSCMGDSGGPLVCERPgGQWTLFGLTSWGSVCfSKVLGPGVYSNVSYFVGWIERQ 1034
Cdd:cd00190   160 SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGC-ARPNYPGVYTRVSSYLDWIQKT 232
CRD_corin_2 cd07888
One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ...
 456-577 4.61e-81

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: 259.18  E-value: 4.61e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  456 QCEPITLELCMNLPYNHTHYPNYLGHRTQKEASISWESSLFPALVQTNCYKYLMFFACTILVPKCDVNTGQRIPPCRLLC 535
Cdd:cd07888     1 QCEPITLELCMNLPYNTTRYPNYLGHRTQKEASISWESSLFPALVQTNCYKYLMFFACTILVPKCDPVTQQRIPPCRSLC 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 170295827  536 EHSKERCESVLGIVGLQWPEDTDCNQFPEESSDNQTCLLPNE 577
Cdd:cd07888    81 RNSKERCESVLGIVGLQWPEDTDCAQFPEENSDNQTCLLPDE 122
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 802-1031 1.28e-79

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 259.15  E-value: 1.28e-79
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827    802 RILGGRTSRPGRWPWQCSLQSEPSGHICGCVLIAKKWVLTVAHCFEGReDADVWKVVFGINNLDHPsGFMQTRFVKTILL 881
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSG-EEGQVIKVSKVII 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827    882 HPRYSRAVVDYDISVVELSDDINETSYVRPVCLPSPEEYLEPDTYCYITGWGHMGN---KMPFKLQEGEVRIIPLEQCQS 958
Cdd:smart00020   79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEgagSLPDTLQEVNVPIVSNATCRR 158

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 170295827    959 -YFDMKTITNRMICAGYESGTVDSCMGDSGGPLVCErpGGQWTLFGLTSWGSVCfSKVLGPGVYSNVSYFVGWI 1031
Cdd:smart00020  159 aYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGC-ARPGKPGVYTRVSSYLDWI 229
CRD_corin_1 cd07445
One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ...
 136-265 2.44e-76

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: 246.38  E-value: 2.44e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  136 NTSTCMNITHSQCQILPYHSTLAPLLPIVKNMDMEKFLKFFTYLHRLSCYQHILLFGCSLAFPECVVDGDDRHGLLPCRS 215
Cdd:cd07445     1 NTSACMNITHSQCQMLPYHSTLKPSLLSVKNMEMEKFLKFFSYLHRLSCYQHIMLFGCSLALPECISDGDDRHGLLPCRS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 170295827  216 FCEAAKEGCESVLGMVNSSWPDSLRCSQFRDHTETNSSVRKSCFSLQQEH 265
Cdd:cd07445    81 FCEAAKEGCEPVLGMVNASWPDFLRCSQFRNNTETAVENRALCFSPQQER 130
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 795-1035 4.79e-64

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 217.59  E-value: 4.79e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  795 PAARMNKRILGGRTSRPGRWPWQCSLQSE--PSGHICGCVLIAKKWVLTVAHCFEGREDADVwKVVFGINNLDHPSGfmQ 872
Cdd:COG5640    23 PAADAAPAIVGGTPATVGEYPWMVALQSSngPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDL-RVVIGSTDLSTSGG--T 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  873 TRFVKTILLHPRYSRAVVDYDISVVELSDDINETSYVRpvcLPSPEEYLEPDTYCYITGWGHMGN---KMPFKLQEGEVR 949
Cdd:COG5640   100 VVKVARIVVHPDYDPATPGNDIALLKLATPVPGVAPAP---LATSADAAAPGTPATVAGWGRTSEgpgSQSGTLRKADVP 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  950 IIPLEQCQSYFDMktITNRMICAGYESGTVDSCMGDSGGPLVcERPGGQWTLFGLTSWG-SVCFSKvlGPGVYSNVSYFV 1028
Cdd:COG5640   177 VVSDATCAAYGGF--DGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGgGPCAAG--YPGVYTRVSAYR 251


                  ....*..
gi 170295827 1029 GWIERQI 1035
Cdd:COG5640   252 DWIKSTA 258
Trypsin pfam00089
Trypsin;
803-1031 2.76e-63

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 213.84  E-value: 2.76e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827   803 ILGGRTSRPGRWPWQCSLQSEPSGHICGCVLIAKKWVLTVAHCFEGREDadvWKVVFGINNLDHPSGFMQTRFVKTILLH 882
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASD---VKVVLGAHNIVLREGGEQKFDVEKIIVH 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827   883 PRYSRAVVDYDISVVELSDDINETSYVRPVCLPSPEEYLEPDTYCYITGWGHMG-NKMPFKLQEGEVRIIPLEQCQSYFD 961
Cdd:pfam00089   78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKtLGPSDTLQEVTVPVVSRETCRSAYG 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827   962 mKTITNRMICAGYesGTVDSCMGDSGGPLVCERPggqwTLFGLTSWGSVCfSKVLGPGVYSNVSYFVGWI 1031
Cdd:pfam00089  158 -GTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGC-ASGNYPGVYTPVSSYLDWI 219
CRD_FZ cd07066
CRD_domain cysteine-rich domain, also known as Fz (frizzled) domain; CRD_FZ is an essential ...
 456-577 4.04e-33

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: 124.16  E-value: 4.04e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  456 QCEPITLELCMNLPYNHTHYPNYLGHRTQKEASIswESSLFPALVQTNCYKYLMFFACTILVPKCDVNTGQRIPPCRLLC 535
Cdd:cd07066     1 KCEPIPLPLCRGLPYNTTRFPNLLGHESQEEAEQ--ELESFTPLVNSGCHPDLRFFLCSLYFPECTPDGDRPIPPCRSLC 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 170295827  536 EHSKERCESVLGIVGLQWPEDTDCNQFPeESSDNQTCLLPNE 577
Cdd:cd07066    79 EEVRDSCEPLMLAFGFPWPEPLDCDRFP-DSNEEGLCISPPG 119
Fz pfam01392
Fz domain; Also known as the CRD (cysteine rich domain), the C6 box in MuSK receptor. This ...
 457-564 2.45e-31

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: 118.83  E-value: 2.45e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827   457 CEPITLELCMNLPYNHTHYPNYLGHRTQKEASISWES---SLFPALVQTNCYKYLMFFACTILVPKCDVNTGQR--IPPC 531
Cdd:pfam01392    1 CEPITLPMCLGLGYNATVFPNLLGHQTQEEAELSLAYlvlSEFEPLVDLSCSPSLRLFLCSLYFPPCTLGPSPKpvCPPC 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 170295827   532 RLLCEHSKERCESVLGIV--GLQWPEDTDCNQFPE 564
Cdd:pfam01392   81 RSLCEEVRYGCEPLLEEAkfGFSWPEFLDCDSLPA 115
CRD_FZ1_like cd07458
Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 1; The cysteine-rich ...
 455-569 1.11e-29

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: 114.05  E-value: 1.11e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  455 SQCEPITLELCMNLPYNHTHYPNYLGHRTQKEASIswESSLFPALVQTNCYKYLMFFACTILVPKCDVnTGQRIPPCRLL 534
Cdd:cd07458     1 GKCEPITIPLCTDIPYNMTIFPNLLGHTKQEDAGL--EVHQFYPLVKVQCSPDLKFFLCSVYAPVCTV-LERPIPPCRSL 77

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 170295827  535 CEHSKERCESVLGIVGLQWPEDTDCNQFPEESSDN 569
Cdd:cd07458    78 CESARQGCEALMNKFGFQWPESLDCEKFPVHGAGD 112
CRD_FZ4 cd07448
Cysteine-rich Wnt-binding domain of the frizzled 4 (Fz4) receptor; The cysteine-rich domain ...
 456-579 5.49e-29

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: 112.56  E-value: 5.49e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  456 QCEPITLELCMNLPYNHTHYPNYLGHRTQKEASISWESslFPALVQTNCYKYLMFFACTILVPKCDVNTGQRIPPCRLLC 535
Cdd:cd07448     3 RCEPIRIEMCQGLGYNVTRMPNLVGHELQTDAELQLQT--FTPLIQYGCSSQLKFFLCSVYVPMCTEKVPVPIGPCRPLC 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 170295827  536 EHSKERCESVLGIVGLQWPEDTDCNQFPEESSDNQTCLL-PNEDV 579
Cdd:cd07448    81 LSVKKRCLPVLKEFGFPWPEALNCSKFPPQNNHNHMCMEgPGDEE 125
FRI smart00063
Frizzled; Drosophila melanogaster frizzled mediates signalling that polarises a precursor cell ...
 457-565 1.44e-27

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: 107.78  E-value: 1.44e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827    457 CEPITLELCMNLPYNHTHYPNYLGHRTQKEASIswESSLFPALVQTNCYKYLMFFACTILVPKCDvNTGQRIPPCRLLCE 536
Cdd:smart00063    1 CEPITIPLCKDLGYNLTSMPNLLGHTTQEEAGL--ELEQFHPLLNVQCSPDLRFFLCSVYAPICT-EDLRPILPCRSLCE 77

                            90       100
                    ....*....|....*....|....*....
gi 170295827    537 HSKERCESVLGIVGLQWPEDTDCNQFPEE 565
Cdd:smart00063   78 AAREGCEPLMEKFGFPWPEFLRCDRFPVQ 106
CRD_FZ5_like cd07456
Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 5; The cysteine-rich ...
 457-577 1.68e-25

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: 102.48  E-value: 1.68e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  457 CEPITLELCMNLPYNHTHYPNYLGHRTQKEASIswESSLFPALVQTNCYKYLMFFACTILVPKCDVNTGQRIPPCRLLCE 536
Cdd:cd07456     2 CEEITIPMCKGIGYNMTYMPNQFNHDTQEEAGL--EVHQFWPLVEIQCSPDLKFFLCSMYTPICLEDYDKPLPPCRSVCE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 170295827  537 HSKERCESVLGIVGLQWPEDTDCNQFPEESSDNQTCLLPNE 577
Cdd:cd07456    80 RARDGCAPIMRQYGFAWPERMSCDALPEGGDPDNLCMDRNN 120
CRD_FZ9_like cd07457
Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 9; The cysteine-rich ...
 455-576 1.80e-25

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: 102.19  E-value: 1.80e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  455 SQCEPITLELCMNLPYNHTHYPNYLGHRTQKEASISWESslFPALVQTNCYKYLMFFACTILVPKCDVNTGQRIPPCRLL 534
Cdd:cd07457     1 GKCERITIPMCQGIGYNMTRMPNLLGHESQSEAAISIHE--FAPLVQYGCAEHLRFFLCSLYAPMCTEQVSIPIPACRSM 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 170295827  535 CEHSKERCESVLGIVGLQWPEDTDCNQFPEESSDNQTCLL-PN 576
Cdd:cd07457    79 CEQARDKCSPIMEQFSFSWPDSLDCDRLPRKNDPKDLCMEaPN 121
CRD_FZ10 cd07462
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 10 (Fz10) receptor; The cysteine-rich ...
 456-573 7.15e-24

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: 97.78  E-value: 7.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  456 QCEPITLELCMNLPYNHTHYPNYLGHRTQKEASISWESslFPALVQTNCYKYLMFFACTILVPKCDVNTGQRIPPCRLLC 535
Cdd:cd07462     4 RCQPIEIPMCKDIGYNMTRMPNLMGHENQREAAIQLHE--FAPLVEYGCHSHLKFFLCSLYAPMCTEQVSTPIPACRVMC 81

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 170295827  536 EHSKERCESVLGIVGLQWPEDTDCNQFPEESSDNQTCL 573
Cdd:cd07462    82 EQARLKCSPIMEQFNFKWPDSLDCSKLPNKNDPNYLCM 119
CRD_FZ9 cd07463
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 9 (Fz9) receptor; The cysteine-rich ...
 455-578 1.69e-23

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: 97.02  E-value: 1.69e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  455 SQCEPITLELCMNLPYNHTHYPNYLGHRTQKEASIswESSLFPALVQTNCYKYLMFFACTILVPKCDVNTGQRIPPCRLL 534
Cdd:cd07463     3 AKCQPVVIPMCRGIGYNLTRMPNFLGHDSQREAAI--KLNEFAPLVEYGCHVHLRFFLCSLYAPMCTDQVSTSIPACRPM 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 170295827  535 CEHSKERCESVLGIVGLQWPEDTDCNQFPEESSDNQTCLLPNED 578
Cdd:cd07463    81 CEQARQKCSPIMEQFNFGWPESLDCSRLPTRNDPNALCMEAPEN 124
CRD_FZ2 cd07464
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 2 (Fz2) receptor; The cysteine-rich ...
 457-584 1.49e-22

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: 94.00  E-value: 1.49e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  457 CEPITLELCMNLPYNHTHYPNYLGHRTQKEASIswESSLFPALVQTNCYKYLMFFACTILVPKCDVnTGQRIPPCRLLCE 536
Cdd:cd07464     5 CQPISIPLCTDIAYNQTIMPNLLGHTNQEDAGL--EVHQFYPLVKVQCSLELRFFLCSMYAPVCTV-LEQAIPPCRSICE 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 170295827  537 HSKERCESVLGIVGLQWPEDTDCNQFPEESSDnQTCLLPNEDvEECSP 584
Cdd:cd07464    82 RARQGCEALMNKFGFQWPERLRCENFPRHGAE-QICVGQNHS-EDGGP 127
Fz pfam01392
Fz domain; Also known as the CRD (cysteine rich domain), the C6 box in MuSK receptor. This ...
 140-247 1.92e-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: 93.40  E-value: 1.92e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827   140 CMNITHSQCQILPYHSTLAPLLPIVKNMDMEKFLKFFTYLH------RLSCYQHILLFGCSLAFPECVVDGDDRHGLLPC 213
Cdd:pfam01392    1 CEPITLPMCLGLGYNATVFPNLLGHQTQEEAELSLAYLVLSefeplvDLSCSPSLRLFLCSLYFPPCTLGPSPKPVCPPC 80

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 170295827   214 RSFCEAAKEGCESVLGMVNS--SWPDSLRCSQFRDH 247
Cdd:pfam01392   81 RSLCEEVRYGCEPLLEEAKFgfSWPEFLDCDSLPAD 116
CRD_FZ3 cd07449
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 3 (Fz3) receptor; The cysteine-rich ...
 457-564 2.99e-22

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: 93.15  E-value: 2.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  457 CEPITLELCMNLPYNHTHYPNYLGHRTQKEASISWESslFPALVQTNCYKYLMFFACTILVPKCdVNTGQRIPPCRLLCE 536
Cdd:cd07449     5 CEPITLRMCQDLPYNTTFMPNLLNHYDQQTAALAMEP--FHPMVNLECSRDFRPFLCALYAPVC-MEYGRVTLPCRRLCQ 81

                          90       100
                  ....*....|....*....|....*...
gi 170295827  537 HSKERCESVLGIVGLQWPEDTDCNQFPE 564
Cdd:cd07449    82 RAYSECSKLMEMFGVPWPEDMECSRFPD 109
CRD_FZ7 cd07466
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 7 (Fz7) receptor; The cysteine-rich ...
 457-563 4.34e-22

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: 92.84  E-value: 4.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  457 CEPITLELCMNLPYNHTHYPNYLGHRTQKEASIswESSLFPALVQTNCYKYLMFFACTILVPKCDVnTGQRIPPCRLLCE 536
Cdd:cd07466     5 CQPISIPLCTDIAYNQTIMPNLLGHTNQEDAGL--EVHQFYPLVKVQCSPELKFFLCSMYAPVCTV-LEQAIPPCRSLCE 81

                          90       100
                  ....*....|....*....|....*..
gi 170295827  537 HSKERCESVLGIVGLQWPEDTDCNQFP 563
Cdd:cd07466    82 RARQGCEALMNKFGFQWPERLRCENFP 108
CRD_FZ cd07066
CRD_domain cysteine-rich domain, also known as Fz (frizzled) domain; CRD_FZ is an essential ...
 139-251 4.95e-22

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: 92.18  E-value: 4.95e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  139 TCMNITHSQCQILPYHSTLAP-LLPIVKNMDMEKFLKFFTYLHRLSCYQHILLFGCSLAFPECVVDGDDRhgLLPCRSFC 217
Cdd:cd07066     1 KCEPIPLPLCRGLPYNTTRFPnLLGHESQEEAEQELESFTPLVNSGCHPDLRFFLCSLYFPECTPDGDRP--IPPCRSLC 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 170295827  218 EAAKEGCESVLGMVNSSWPDSLRCSQFRDHTETN 251
Cdd:cd07066    79 EEVRDSCEPLMLAFGFPWPEPLDCDRFPDSNEEG 112
CRD_FZ5 cd07460
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 5 (Fz5) receptor.proteins; The ...
 457-576 5.97e-22

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: 92.39  E-value: 5.97e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  457 CEPITLELCMNLPYNHTHYPNYLGHRTQKEASIswESSLFPALVQTNCYKYLMFFACTILVPKCDVNTGQRIPPCRLLCE 536
Cdd:cd07460     5 CQEITVPMCKGIGYNLTYMPNQFNHDTQDEAGL--EVHQFWPLVEIQCSPDLRFFLCSMYTPICLPDYRKPLPPCRSVCE 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 170295827  537 HSKERCESVLGIVGLQWPEDTDCNQFPEESSDNQTCLLPN 576
Cdd:cd07460    83 RAKAGCSPLMRQYGFAWPERMNCDRLPVLGDPETLCMDYN 122
CRD_FZ8 cd07461
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 8 (Fz8) receptor; The cysteine-rich ...
 456-573 1.00e-21

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: 91.58  E-value: 1.00e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  456 QCEPITLELCMNLPYNHTHYPNYLGHRTQKEASIswESSLFPALVQTNCYKYLMFFACTILVPKCDVNTGQRIPPCRLLC 535
Cdd:cd07461     4 QCQEITVPLCKGIGYNYTYMPNQFNHDTQDEAGL--EVHQFWPLVEIQCSPDLKFFLCSMYTPICLEDYKKPLPPCRSVC 81

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 170295827  536 EHSKERCESVLGIVGLQWPEDTDCNQFPEESSDNQTCL 573
Cdd:cd07461    82 ERAKAGCAPLMRQYGFPWPDRMRCDLLPEQGNPDTLCM 119
CRD_FZ1 cd07465
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 1 (Fz1) receptor; The cysteine-rich ...
 457-563 2.88e-21

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: 90.50  E-value: 2.88e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  457 CEPITLELCMNLPYNHTHYPNYLGHRTQKEASIswESSLFPALVQTNCYKYLMFFACTILVPKCDVnTGQRIPPCRLLCE 536
Cdd:cd07465     5 CQPISIPLCTDIAYNQTIMPNLLGHTNQEDAGL--EVHQFYPLVKVQCSAELKFFLCSMYAPVCTV-LEQALPPCRSLCE 81

                          90       100
                  ....*....|....*....|....*..
gi 170295827  537 HSKERCESVLGIVGLQWPEDTDCNQFP 563
Cdd:cd07465    82 RARQGCEALMNKFGFQWPDTLRCEKFP 108
CRD_SFRP3 cd07441
Cysteine-rich domain of the secreted frizzled-related protein 3 (SFRP3, alias FRZB), a Wnt ...
 454-575 2.91e-20

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: 87.41  E-value: 2.91e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  454 CSQCEPITLELCMNLPYNHTHYPNYLGHRTQKEASISWESslFPALVQTNCYKYLMFFACTILVPKCDVN-TGQRIPPCR 532
Cdd:cd07441     1 AASCEPVRIPMCKSMPWNMTKMPNHLHHSTQANAVLAIEQ--FEGLLGTQCSPDLLFFLCAMYAPICTIDfQHEPIKPCK 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 170295827  533 LLCEHSKERCESVLGIVGLQWPEDTDCNQFPeeSSDNQTCLLP 575
Cdd:cd07441    79 SVCERARAGCEPVLIRYRHTWPESLACEELP--VYDRGVCISP 119
CRD_LIN_17 cd07454
Cysteine-rich domain (CRD) of LIN_17; A cysteine-rich domain (CRD) is an essential component ...
 456-579 2.31e-18

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: 82.14  E-value: 2.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  456 QCEPITLELCMNLPYNHTHYPNYLghRTQKEASISWESSLFPALVQTNCYKYLMFFACTILVPKCDVNTGQRIPPCRLLC 535
Cdd:cd07454     4 KCIPIDIELCKDLPYNYTYFPNTI--LHNDQHTLQTHTEHFKPLMKTKCHPHIHFFICSVFAPMCPIGMPQAVTSCKSVC 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 170295827  536 EHSKERCESVLGIVGLQWPEDTDCNQFPEESSdnqTCLLPNEDV 579
Cdd:cd07454    82 EQVKADCFSILEEFGIGWPEPLNCAQFPDPPE---LCMKPTEDE 122
CRD_SFRP2 cd07446
Cysteine-rich domain of the secreted frizzled-related protein 2 (SFRP2), a regulator of Wnt ...
 455-575 1.89e-17

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: 79.57  E-value: 1.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  455 SQCEPI--TLELCMNLPYNHTHYPNYLGHRTQKEAsISWESSLFPaLVQTNCYKYLMFFACTILVPKCDVNTGQRIPPCR 532
Cdd:cd07446     3 SNCKPIpaNMLLCHGIEYTNMRLPNLLGHETMKEV-LQQAGSWIP-LVQKQCHPDTKKFLCSLFAPVCLDDLDEAIQPCR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 170295827  533 LLCEHSKERCESVLGIVGLQWPEDTDCNQFPEessDNQTCLLP 575
Cdd:cd07446    81 SLCEAVKDGCAPVMSAFGFPWPDMLDCTRFPL---DNDLCIPP 120
CRD_SFRP4 cd07442
Cysteine-rich domain of the secreted frizzled-related protein 4 (SFRP4), a Wnt antagonist; The ...
 457-575 4.56e-17

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: 78.53  E-value: 4.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  457 CEPITLELCMNLPYNHTHYPNYLGHRTQKEASISWESslFPALVQTNCYKYLMFFACTILVPKCDVN-TGQRIPPCRLLC 535
Cdd:cd07442     5 CEAVRIPMCRHMPWNITRMPNHLHHSTQENAVLAIEQ--YEELVDTGCSPVLPFFLCAMYAPICTLEfLYDPIKPCRSVC 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 170295827  536 EHSKERCESVLGIVGLQWPEDTDCNQFPeeSSDNQTCLLP 575
Cdd:cd07442    83 QRARDGCEPIMRRYNHSWPESLACDDLP--VYDRGVCISP 120
CRD_corin_2 cd07888
One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ...
 140-253 2.96e-16

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: 75.82  E-value: 2.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  140 CMNITHSQCQILPYHSTLAPLL---PIVKNMDMEKFLKFFTYLHRLSCYQHILLFGCSLAFPECVVDGDDRhgLLPCRSF 216
Cdd:cd07888     2 CEPITLELCMNLPYNTTRYPNYlghRTQKEASISWESSLFPALVQTNCYKYLMFFACTILVPKCDPVTQQR--IPPCRSL 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 170295827  217 CEAAKEGCESVLGMVNSSWPDSLRCSQFRDHTETNSS 253
Cdd:cd07888    80 CRNSKERCESVLGIVGLQWPEDTDCAQFPEENSDNQT 116
CRD_corin_1 cd07445
One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ...
 453-571 1.27e-15

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: 74.58  E-value: 1.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  453 NCSQCEPITLELCMNLPYNHTHYPNYLGHRtqkeaSISWESSL--FPALVQTNCYKYLMFFACTILVPKCDVNTGQR--I 528
Cdd:cd07445     1 NTSACMNITHSQCQMLPYHSTLKPSLLSVK-----NMEMEKFLkfFSYLHRLSCYQHIMLFGCSLALPECISDGDDRhgL 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 170295827  529 PPCRLLCEHSKERCESVLGIVGLQWPEDTDCNQFPEESSDNQT 571
Cdd:cd07445    76 LPCRSFCEAAKEGCEPVLGMVNASWPDFLRCSQFRNNTETAVE 118
CRD_FZ6 cd07450
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 6 (Fz6) receptor; The cysteine-rich ...
 457-563 2.69e-15

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


Pssm-ID: 143559 [Multi-domain]  Cd Length: 127  Bit Score: 73.26  E-value: 2.69e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  457 CEPITLELCMNLPYNHTHYPNYLGHRTQKEASISWESslFPALVQTNCYKYLMFFACTILVPKCDVNTGQrIPPCRLLCE 536
Cdd:cd07450     5 CEPITVPRCLKMPYNMTFFPNLMGHYDQDIAAVEMEP--FLPLANLRCSPNVHTFLCQAFVPTCTEQIHV-VRPCRELCE 81

                          90       100
                  ....*....|....*....|....*..
gi 170295827  537 HSKERCESVLGIVGLQWPEDTDCNQFP 563
Cdd:cd07450    82 KVYSDCKKLIDTFGISWPEELECDRLQ 108
CRD_Carboxypeptidase_Z cd07447
Cysteine-rich domain of carboxypeptidase Z, a member of the carboxypeptidase E family; The ...
 456-562 1.49e-14

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: 71.32  E-value: 1.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  456 QCEPITLELCMNLPYNHTHYPNYLGHRTQKEASISWES---SLFPALVQTNCYKYLMFFACTILVPKCDvnTGQRIPPCR 532
Cdd:cd07447     3 TCTDLLLSYCSDVSYTQTTFPNLLGHRSREVTEAGAEYlllSVLHGLLGGECNPDIRLLGCSVLAPRCE--NDKVIKPCR 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 170295827  533 LLCEHSKERCESVLGIVGLQWPEDTDCNQF 562
Cdd:cd07447    81 STCEALRKRCSHAFDAIQMAWPYFLDCDRF 110
CRD_SFRP1 cd07443
Cysteine-rich domain of the secreted frizzled-related protein 1 (SFRP1), a regulator of Wnt ...
 459-565 5.73e-14

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: 69.54  E-value: 5.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  459 PITLELCMNLPYNHTHYPNYLGHRTQKEasISWESSLFPALVQTNCYKYLMFFACTILVPKCdvnTGQRIPPCRLLCEHS 538
Cdd:cd07443    11 PADLRLCHNVGYKKMVLPNLLDHETMAE--VKQQASSWVPLLNKNCHKGTQVFLCSLFAPVC---LDRPVYPCRWLCEAV 85

                          90       100
                  ....*....|....*....|....*..
gi 170295827  539 KERCESVLGIVGLQWPEDTDCNQFPEE 565
Cdd:cd07443    86 RDSCEPVMQFFGFYWPEMLKCDKFPEG 112
FRI smart00063
Frizzled; Drosophila melanogaster frizzled mediates signalling that polarises a precursor cell ...
 140-249 7.95e-14

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: 68.88  E-value: 7.95e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827    140 CMNITHSQCQILPYHSTLAPLLPIVKNM-DMEKFLKFFTYLHRLSCYQHILLFGCSLAFPECvvdGDDRHGLLPCRSFCE 218
Cdd:smart00063    1 CEPITIPLCKDLGYNLTSMPNLLGHTTQeEAGLELEQFHPLLNVQCSPDLRFFLCSVYAPIC---TEDLRPILPCRSLCE 77

                            90       100       110
                    ....*....|....*....|....*....|.
gi 170295827    219 AAKEGCESVLGMVNSSWPDSLRCSQFRDHTE 249
Cdd:smart00063   78 AAREGCEPLMEKFGFPWPEFLRCDRFPVQEE 108
CRD_sizzled cd07452
Cysteine-rich domain of the sizzled protein; The cysteine-rich domain (CRD) is an essential ...
 455-575 1.12e-13

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: 69.14  E-value: 1.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  455 SQCEPITLE--LCMNLPYNHTHYPNYLGHRTQKEASISweSSLFPALVQTNCYKYLMFFACTILVPKCdvnTGQRIPPCR 532
Cdd:cd07452     7 TKCVPIPPEmsMCQDVGYSEMRLPNLLGHTSMAEVVPK--SADWQTLLHTGCHPHARTFLCSLFAPVC---LDTFIQPCR 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 170295827  533 LLCEHSKERCESVLGIVGLQWPEDTDCNQFPEESSDnqtCLLP 575
Cdd:cd07452    82 SMCVAVRDSCAPVLACHGHSWPESLDCDRFPAGEDM---CLAS 121
CRD_SFRP5 cd07444
Cysteine-rich domain of the secreted frizzled-related protein 5 (SFRP5), a regulator of Wnt ...
 455-573 1.91e-12

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: 65.35  E-value: 1.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  455 SQCE--PITLELCMNLPYNHTHYPNYLGHRTQKEASiSWESSLFPALVQtNCYKYLMFFACTILVPKCdvnTGQRIPPCR 532
Cdd:cd07444     5 PQCVdiPADLPLCHNVGYKRMRLPNLLEHESMAEVK-QQASSWVPLLAK-RCHADTQVFLCSLFAPVC---LDRPIYPCR 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 170295827  533 LLCEHSKERCESVLGIVGLQWPEDTDCNQFPeesSDNQTCL 573
Cdd:cd07444    80 SLCEAVRDSCAPVMESYGFPWPEMLHCHKFP---LDNDLCI 117
CRD_FZ1_like cd07458
Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 1; The cysteine-rich ...
 140-256 3.32e-12

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: 64.35  E-value: 3.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  140 CMNITHSQCQILPYHSTLAP-LLPIVKNMDMEKFLKFFTYLHRLSCYQHILLFGCSLAFPECVVDgddRHGLLPCRSFCE 218
Cdd:cd07458     3 CEPITIPLCTDIPYNMTIFPnLLGHTKQEDAGLEVHQFYPLVKVQCSPDLKFFLCSVYAPVCTVL---ERPIPPCRSLCE 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 170295827  219 AAKEGCESVLGMVNSSWPDSLRCSQFRDHTETNSSVRK 256
Cdd:cd07458    80 SARQGCEALMNKFGFQWPESLDCEKFPVHGAGDLCVGE 117
CRD_FZ3 cd07449
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 3 (Fz3) receptor; The cysteine-rich ...
 139-249 1.68e-11

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: 62.72  E-value: 1.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  139 TCMNITHSQCQILPYHSTLAP-LLPIVKNMDMEKFLKFFTYLHRLSCYQHILLFGCSLAFPECVVDGddrHGLLPCRSFC 217
Cdd:cd07449     4 SCEPITLRMCQDLPYNTTFMPnLLNHYDQQTAALAMEPFHPMVNLECSRDFRPFLCALYAPVCMEYG---RVTLPCRRLC 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 170295827  218 EAAKEGCESVLGMVNSSWPDSLRCSQFRDHTE 249
Cdd:cd07449    81 QRAYSECSKLMEMFGVPWPEDMECSRFPDCDE 112
CRD_crescent cd07453
Cysteine-rich domain of the crescent protein; The cysteine-rich domain (CRD) is an essential ...
 459-591 1.70e-11

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: 62.65  E-value: 1.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  459 PITLELCMNLPYNHTHYPNYLGHRTQKEAsISWESSLFPaLVQTNCYKYLMFFACTILVPKCdvnTGQRIPPCRLLCEHS 538
Cdd:cd07453     7 PKSMALCYDIGYSEMRIPNLLEHETMAEV-IQQSSSWLP-LLARECHPDARIFLCSLFAPIC---WDRPIYPCRSLCEAV 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 170295827  539 KERCESVLGIVGLQWPEDTDCNQFPEessDNQTCLLPnEDVEECSPSHFKCRS 591
Cdd:cd07453    82 RSSCAPLMACYGYPWPEILHCDKFPV---DHDLCISP-QFIDTLSPERVKPRA 130
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 692-787 3.36e-11

Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR domains that contain 6 conserved cysteines. May bind bacterial antigens in the protein MARCO.


Pssm-ID: 214555 [Multi-domain]  Cd Length: 101  Bit Score: 60.82  E-value: 3.36e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827    692 VTLSKNGNSSS-LLTVHKSAKEHHVCADGWRETLSQLACKQMGLGEPSVTKL--IPGQEGQQWLRLYPNWENLNGStLQE 768
Cdd:smart00202    1 VRLVGGGSPCEgRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGsaYFGPGSGPIWLDNVRCSGTEAS-LSD 79

                            90       100
                    ....*....|....*....|..
gi 170295827    769 LL---VYRHSCPSRSEISLLCS 787
Cdd:smart00202   80 CPhsgWGSHNCSHGEDAGVVCS 101
CRD_FZ4 cd07448
Cysteine-rich Wnt-binding domain of the frizzled 4 (Fz4) receptor; The cysteine-rich domain ...
 139-244 6.01e-11

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: 60.94  E-value: 6.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  139 TCMNITHSQCQILPYHSTLAP-LLPIVKNMDMEKFLKFFTYLHRLSCYQHILLFGCSLAFPECVVDGDDRHGllPCRSFC 217
Cdd:cd07448     3 RCEPIRIEMCQGLGYNVTRMPnLVGHELQTDAELQLQTFTPLIQYGCSSQLKFFLCSVYVPMCTEKVPVPIG--PCRPLC 80

                          90       100
                  ....*....|....*....|....*..
gi 170295827  218 EAAKEGCESVLGMVNSSWPDSLRCSQF 244
Cdd:cd07448    81 LSVKKRCLPVLKEFGFPWPEALNCSKF 107
CRD_FZ2 cd07464
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 2 (Fz2) receptor; The cysteine-rich ...
 140-247 5.01e-10

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: 58.17  E-value: 5.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  140 CMNITHSQCQILPYHSTLAP-LLPIVKNMDMEKFLKFFTYLHRLSCYQHILLFGCSLAFPECVVDgddRHGLLPCRSFCE 218
Cdd:cd07464     5 CQPISIPLCTDIAYNQTIMPnLLGHTNQEDAGLEVHQFYPLVKVQCSLELRFFLCSMYAPVCTVL---EQAIPPCRSICE 81

                          90       100
                  ....*....|....*....|....*....
gi 170295827  219 AAKEGCESVLGMVNSSWPDSLRCSQFRDH 247
Cdd:cd07464    82 RARQGCEALMNKFGFQWPERLRCENFPRH 110
CRD_FZ1 cd07465
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 1 (Fz1) receptor; The cysteine-rich ...
 140-247 7.26e-10

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: 57.76  E-value: 7.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  140 CMNITHSQCQILPYHSTLAP-LLPIVKNMDMEKFLKFFTYLHRLSCYQHILLFGCSLAFPECVVDgddRHGLLPCRSFCE 218
Cdd:cd07465     5 CQPISIPLCTDIAYNQTIMPnLLGHTNQEDAGLEVHQFYPLVKVQCSAELKFFLCSMYAPVCTVL---EQALPPCRSLCE 81

                          90       100
                  ....*....|....*....|....*....
gi 170295827  219 AAKEGCESVLGMVNSSWPDSLRCSQFRDH 247
Cdd:cd07465    82 RARQGCEALMNKFGFQWPDTLRCEKFPVH 110
CRD_FZ7 cd07466
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 7 (Fz7) receptor; The cysteine-rich ...
 140-247 9.22e-10

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: 57.40  E-value: 9.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  140 CMNITHSQCQILPYHSTLAP-LLPIVKNMDMEKFLKFFTYLHRLSCYQHILLFGCSLAFPECVVDgddRHGLLPCRSFCE 218
Cdd:cd07466     5 CQPISIPLCTDIAYNQTIMPnLLGHTNQEDAGLEVHQFYPLVKVQCSPELKFFLCSMYAPVCTVL---EQAIPPCRSLCE 81

                          90       100
                  ....*....|....*....|....*....
gi 170295827  219 AAKEGCESVLGMVNSSWPDSLRCSQFRDH 247
Cdd:cd07466    82 RARQGCEALMNKFGFQWPERLRCENFPVH 110
CRD_FZ5_like cd07456
Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 5; The cysteine-rich ...
 176-251 1.37e-09

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: 57.02  E-value: 1.37e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 170295827  176 FTYLHRLSCYQHILLFGCSLAFPECVVDGDdrHGLLPCRSFCEAAKEGCESVLGMVNSSWPDSLRCSQFRDHTETN 251
Cdd:cd07456    39 FWPLVEIQCSPDLKFFLCSMYTPICLEDYD--KPLPPCRSVCERARDGCAPIMRQYGFAWPERMSCDALPEGGDPD 112
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
582-616 8.23e-09

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 51.87  E-value: 8.23e-09
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 170295827   582 CSPSHFKCRSGRCVLGSRRCDGQADCDDDSDEENC 616
Cdd:pfam00057    3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 657-691 9.44e-09

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: 51.82  E-value: 9.44e-09
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 170295827  657 CQDNELECANHECVPRDLWCDGWVDCSDSSDEWGC 691
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
349-379 1.25e-08

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 51.48  E-value: 1.25e-08
                           10        20        30
                   ....*....|....*....|....*....|.
gi 170295827   349 EHRCGDGRCIAAEWVCDGDHDCVDKSDEVNC 379
Cdd:pfam00057    7 EFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
CRD_SFRP3 cd07441
Cysteine-rich domain of the secreted frizzled-related protein 3 (SFRP3, alias FRZB), a Wnt ...
 137-244 1.44e-08

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: 54.29  E-value: 1.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  137 TSTCMNITHSQCQILPY----------HSTLAPLLpivknMDMEKFLKFFTylhrLSCYQHILLFGCSLAFPECVVDGDd 206
Cdd:cd07441     1 AASCEPVRIPMCKSMPWnmtkmpnhlhHSTQANAV-----LAIEQFEGLLG----TQCSPDLLFFLCAMYAPICTIDFQ- 70

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 170295827  207 RHGLLPCRSFCEAAKEGCESVLGMVNSSWPDSLRCSQF 244
Cdd:cd07441    71 HEPIKPCKSVCERARAGCEPVLIRYRHTWPESLACEEL 108
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 582-616 2.09e-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: 50.67  E-value: 2.09e-08
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 170295827  582 CSPSHFKCRSGRCVLGSRRCDGQADCDDDSDEENC 616
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 818-1009 2.24e-08

V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 55.07  E-value: 2.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  818 CSLQSEPSGHICGCVLIAKKWVLTVAHCFEGRED---ADVWKVVFGINNLDHpsgfmQTRFVKTILLHPRY-SRAVVDYD 893
Cdd:COG3591     3 GRLETDGGGGVCTGTLIGPNLVLTAGHCVYDGAGggwATNIVFVPGYNGGPY-----GTATATRFRVPPGWvASGDAGYD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  894 ISVVELSDDINETsyVRPVCLPSPEEYLEPDTYcYITGWGhmGNKmPFKL---QEGEVRiipleqcqsyfdmkTITNRMI 970
Cdd:COG3591    78 YALLRLDEPLGDT--TGWLGLAFNDAPLAGEPV-TIIGYP--GDR-PKDLsldCSGRVT--------------GVQGNRL 137

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 170295827  971 cagyeSGTVDSCMGDSGGPLVCERPGGqWTLFGLTSWGS 1009
Cdd:COG3591   138 -----SYDCDTTGGSSGSPVLDDSDGG-GRVVGVHSAGG 170
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 349-379 2.69e-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: 50.67  E-value: 2.69e-08
                          10        20        30
                  ....*....|....*....|....*....|.
gi 170295827  349 EHRCGDGRCIAAEWVCDGDHDCVDKSDEVNC 379
Cdd:cd00112     5 EFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 308-342 2.80e-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: 2.80e-08
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 170295827  308 CSKDLFHCGTGKCLHYSLLCDGYDDCGDLSDEQNC 342
Cdd:cd00112     1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
CRD_LIN_17 cd07454
Cysteine-rich domain (CRD) of LIN_17; A cysteine-rich domain (CRD) is an essential component ...
 140-244 3.68e-08

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: 52.86  E-value: 3.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  140 CMNITHSQCQILPYHSTLAP-LLPIVKNMDMEKFLKFFTYLHRLSCYQHILLFGCSLAFPECvvDGDDRHGLLPCRSFCE 218
Cdd:cd07454     5 CIPIDIELCKDLPYNYTYFPnTILHNDQHTLQTHTEHFKPLMKTKCHPHIHFFICSVFAPMC--PIGMPQAVTSCKSVCE 82

                          90       100
                  ....*....|....*....|....*.
gi 170295827  219 AAKEGCESVLGMVNSSWPDSLRCSQF 244
Cdd:cd07454    83 QVKADCFSILEEFGIGWPEPLNCAQF 108
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 389-416 5.44e-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: 49.51  E-value: 5.44e-08
                          10        20
                  ....*....|....*....|....*...
gi 170295827  389 CRSGQCIPSTFQCDGDEDCKDGSDEENC 416
Cdd:cd00112     8 CANGRCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
389-416 1.17e-07

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 48.78  E-value: 1.17e-07
                           10        20
                   ....*....|....*....|....*...
gi 170295827   389 CRSGQCIPSTFQCDGDEDCKDGSDEENC 416
Cdd:pfam00057   10 CGSGECIPRSWVCDGDPDCGDGSDEENC 37
CRD_FZ9_like cd07457
Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 9; The cysteine-rich ...
 138-241 1.37e-07

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: 51.34  E-value: 1.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  138 STCMNITHSQCQILPYHSTLAP-LLPIVKNMDMEKFLKFFTYLHRLSCYQHILLFGCSLAFPECVVDGDDRhgLLPCRSF 216
Cdd:cd07457     1 GKCERITIPMCQGIGYNMTRMPnLLGHESQSEAAISIHEFAPLVQYGCAEHLRFFLCSLYAPMCTEQVSIP--IPACRSM 78

                          90       100
                  ....*....|....*....|....*
gi 170295827  217 CEAAKEGCESVLGMVNSSWPDSLRC 241
Cdd:cd07457    79 CEQARDKCSPIMEQFSFSWPDSLDC 103
CRD_FZ8 cd07461
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 8 (Fz8) receptor; The cysteine-rich ...
 139-241 1.39e-07

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: 51.14  E-value: 1.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  139 TCMNITHSQCQILPYHSTLaplLPIVKNMDMEKFLKF----FTYLHRLSCYQHILLFGCSLAFPECVvdGDDRHGLLPCR 214
Cdd:cd07461     4 QCQEITVPLCKGIGYNYTY---MPNQFNHDTQDEAGLevhqFWPLVEIQCSPDLKFFLCSMYTPICL--EDYKKPLPPCR 78

                          90       100
                  ....*....|....*....|....*..
gi 170295827  215 SFCEAAKEGCESVLGMVNSSWPDSLRC 241
Cdd:cd07461    79 SVCERAKAGCAPLMRQYGFPWPDRMRC 105
SRCR_2 pfam15494
Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain ...
 715-795 1.39e-07

Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain family found largely on vertebrate sequences up-stream of the trypsin-like transmembrane serine protease, Spinesin.


Pssm-ID: 464747  Cd Length: 99  Bit Score: 50.41  E-value: 1.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827   715 VCADGWRETLSQLACKQMGLGEPSVTKLIP-----GQEGQQWLRLYPnwENLNGsTLQELLVYRHSCPSRSEISLLCSkq 789
Cdd:pfam15494   19 VCSDDWNPAYGRAACQQLGYLRLTHHKSVNltdisSNSSQSFMKLNS--SSLNT-DLYEALQPRDSCSSGSVVSLRCS-- 93


                   ....*.
gi 170295827   790 DCGRRP 795
Cdd:pfam15494   94 ECGLRS 99
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 271-306 2.32e-07

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: 47.97  E-value: 2.32e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 170295827  271 CGGGEsFLCTSGLCVPKKLQCNGYNDCDDWSDEAHC 306
Cdd:cd00112     1 CPPNE-FRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
CRD_FZ10 cd07462
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 10 (Fz10) receptor; The cysteine-rich ...
 140-251 2.85e-07

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: 50.40  E-value: 2.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  140 CMNITHSQCQILPYHSTLAPLLPIVKNMDMEKF-LKFFTYLHRLSCYQHILLFGCSLAFPECVvdgDDRHGLLP-CRSFC 217
Cdd:cd07462     5 CQPIEIPMCKDIGYNMTRMPNLMGHENQREAAIqLHEFAPLVEYGCHSHLKFFLCSLYAPMCT---EQVSTPIPaCRVMC 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 170295827  218 EAAKEGCESVLGMVNSSWPDSLRCSQFRDHTETN 251
Cdd:cd07462    82 EQARLKCSPIMEQFNFKWPDSLDCSKLPNKNDPN 115
CRD_SFRP2 cd07446
Cysteine-rich domain of the secreted frizzled-related protein 2 (SFRP2), a regulator of Wnt ...
 184-244 2.85e-07

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: 50.29  E-value: 2.85e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 170295827  184 CYQHILLFGCSLAFPECVVDGDDrhGLLPCRSFCEAAKEGCESVLGMVNSSWPDSLRCSQF 244
Cdd:cd07446    52 CHPDTKKFLCSLFAPVCLDDLDE--AIQPCRSLCEAVKDGCAPVMSAFGFPWPDMLDCTRF 110
CRD_FZ6 cd07450
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 6 (Fz6) receptor; The cysteine-rich ...
 139-250 3.30e-07

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: 50.15  E-value: 3.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  139 TCMNITHSQCQILPYHSTLAPllpivkNMdMEKF--------LKFFTYLHRLSCYQHILLFGCSLAFPECVvdgDDRHGL 210
Cdd:cd07450     4 TCEPITVPRCLKMPYNMTFFP------NL-MGHYdqdiaaveMEPFLPLANLRCSPNVHTFLCQAFVPTCT---EQIHVV 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 170295827  211 LPCRSFCEAAKEGCESVLGMVNSSWPDSLRCSQFRDHTET 250
Cdd:cd07450    74 RPCRELCEKVYSDCKKLIDTFGISWPEELECDRLQYCDET 113
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
308-342 3.30e-07

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 47.63  E-value: 3.30e-07
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 170295827   308 CSKDLFHCGTGKCLHYSLLCDGYDDCGDLSDEQNC 342
Cdd:pfam00057    3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
CRD_Collagen_XVIII cd07455
Cysteine-rich domain of the variant 3 of collagen XVIII (V3C18 ); The cysteine-rich domain ...
 459-547 3.93e-07

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: 49.81  E-value: 3.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  459 PITLELCMNLPYNHTHYPNYLGHRTQKE---ASISWEsslfpALVQTNCYKYLMFFACTILVPKCDVNTGQRIPPCRLLC 535
Cdd:cd07455     9 PSSLPFCSRLGIRSFWLPNFLNHTSVEEvraVLAEWA-----WLLESGCHPSLEWFFCLLLVPSCGGGPPPPPPPCRQFC 83

                          90
                  ....*....|..
gi 170295827  536 EHSKERCESVLG 547
Cdd:cd07455    84 EVLQDSCWNLLE 95
CRD_FZ9 cd07463
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 9 (Fz9) receptor; The cysteine-rich ...
 140-252 5.02e-07

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: 49.64  E-value: 5.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  140 CMNITHSQCQILPYHSTLAP-LLPIVKNMDMEKFLKFFTYLHRLSCYQHILLFGCSLAFPECVvdgDDRHGLLP-CRSFC 217
Cdd:cd07463     5 CQPVVIPMCRGIGYNLTRMPnFLGHDSQREAAIKLNEFAPLVEYGCHVHLRFFLCSLYAPMCT---DQVSTSIPaCRPMC 81

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 170295827  218 EAAKEGCESVLGMVNSSWPDSLRCSQFRDHTETNS 252
Cdd:cd07463    82 EQARQKCSPIMEQFNFGWPESLDCSRLPTRNDPNA 116
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 581-613 1.23e-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: 45.70  E-value: 1.23e-06
                            10        20        30
                    ....*....|....*....|....*....|...
gi 170295827    581 ECSPSHFKCRSGRCVLGSRRCDGQADCDDDSDE 613
Cdd:smart00192    1 TCPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 657-688 1.44e-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: 45.70  E-value: 1.44e-06
                            10        20        30
                    ....*....|....*....|....*....|..
gi 170295827    657 CQDNELECANHECVPRDLWCDGWVDCSDSSDE 688
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
CRD_FZ5 cd07460
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 5 (Fz5) receptor.proteins; The ...
 140-250 1.81e-06

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: 48.09  E-value: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  140 CMNITHSQCQILPYHSTLaplLPIVKNMDMEKFLKF----FTYLHRLSCYQHILLFGCSLAFPECVvdGDDRHGLLPCRS 215
Cdd:cd07460     5 CQEITVPMCKGIGYNLTY---MPNQFNHDTQDEAGLevhqFWPLVEIQCSPDLRFFLCSMYTPICL--PDYRKPLPPCRS 79

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 170295827  216 FCEAAKEGCESVLGMVNSSWPDSLRCSQFRDHTET 250
Cdd:cd07460    80 VCERAKAGCSPLMRQYGFAWPERMNCDRLPVLGDP 114
CRD_SFRP4 cd07442
Cysteine-rich domain of the secreted frizzled-related protein 4 (SFRP4), a Wnt antagonist; The ...
 184-244 1.81e-06

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: 48.10  E-value: 1.81e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 170295827  184 CYQHILLFGCSLAFPECVVDGDdRHGLLPCRSFCEAAKEGCESVLGMVNSSWPDSLRCSQF 244
Cdd:cd07442    50 CSPVLPFFLCAMYAPICTLEFL-YDPIKPCRSVCQRARDGCEPIMRRYNHSWPESLACDDL 109
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 342-376 1.82e-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: 45.32  E-value: 1.82e-06
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 170295827    342 CDCNltkEHRCGDGRCIAAEWVCDGDHDCVDKSDE 376
Cdd:smart00192    2 CPPG---EFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 389-413 2.13e-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: 44.93  E-value: 2.13e-06
                            10        20
                    ....*....|....*....|....*
gi 170295827    389 CRSGQCIPSTFQCDGDEDCKDGSDE 413
Cdd:smart00192    9 CDNGRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
271-306 2.46e-06

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 44.93  E-value: 2.46e-06
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 170295827   271 CGGGEsFLCTSGLCVPKKLQCNGYNDCDDWSDEAHC 306
Cdd:pfam00057    3 CSPNE-FQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
CRD_SFRP1 cd07443
Cysteine-rich domain of the secreted frizzled-related protein 1 (SFRP1), a regulator of Wnt ...
 183-244 2.60e-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: 47.59  E-value: 2.60e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 170295827  183 SCYQHILLFGCSLAFPECVvdgdDRhGLLPCRSFCEAAKEGCESVLGMVNSSWPDSLRCSQF 244
Cdd:cd07443    53 NCHKGTQVFLCSLFAPVCL----DR-PVYPCRWLCEAVRDSCEPVMQFFGFYWPEMLKCDKF 109
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 308-339 2.80e-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: 44.55  E-value: 2.80e-06
                            10        20        30
                    ....*....|....*....|....*....|..
gi 170295827    308 CSKDLFHCGTGKCLHYSLLCDGYDDCGDLSDE 339
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
CRD_sizzled cd07452
Cysteine-rich domain of the sizzled protein; The cysteine-rich domain (CRD) is an essential ...
 146-244 4.51e-06

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: 47.18  E-value: 4.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  146 SQCQILPYHSTLAPLLPIVKNMDmEKFLKFFTYLHRL--SCYQHILLFGCSLAFPECVvdgdDRHgLLPCRSFCEAAKEG 223
Cdd:cd07452    17 SMCQDVGYSEMRLPNLLGHTSMA-EVVPKSADWQTLLhtGCHPHARTFLCSLFAPVCL----DTF-IQPCRSMCVAVRDS 90

                          90       100
                  ....*....|....*....|.
gi 170295827  224 CESVLGMVNSSWPDSLRCSQF 244
Cdd:cd07452    91 CAPVLACHGHSWPESLDCDRF 111
CRD_SFRP5 cd07444
Cysteine-rich domain of the secreted frizzled-related protein 5 (SFRP5), a regulator of Wnt ...
 184-244 5.70e-06

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: 46.86  E-value: 5.70e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 170295827  184 CYQHILLFGCSLAFPECVvdgdDRhGLLPCRSFCEAAKEGCESVLGMVNSSWPDSLRCSQF 244
Cdd:cd07444    54 CHADTQVFLCSLFAPVCL----DR-PIYPCRSLCEAVRDSCAPVMESYGFPWPEMLHCHKF 109
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 271-303 2.26e-05

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: 42.24  E-value: 2.26e-05
                            10        20        30
                    ....*....|....*....|....*....|...
gi 170295827    271 CGGGEsFLCTSGLCVPKKLQCNGYNDCDDWSDE 303
Cdd:smart00192    2 CPPGE-FQCDNGRCIPSSWVCDGVDDCGDGSDE 33
CRD_crescent cd07453
Cysteine-rich domain of the crescent protein; The cysteine-rich domain (CRD) is an essential ...
 184-244 3.92e-05

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: 44.55  E-value: 3.92e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 170295827  184 CYQHILLFGCSLAFPECVvdgdDRHgLLPCRSFCEAAKEGCESVLGMVNSSWPDSLRCSQF 244
Cdd:cd07453    50 CHPDARIFLCSLFAPICW----DRP-IYPCRSLCEAVRSSCAPLMACYGYPWPEILHCDKF 105
CRD_Carboxypeptidase_Z cd07447
Cysteine-rich domain of carboxypeptidase Z, a member of the carboxypeptidase E family; The ...
 139-244 5.34e-05

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: 43.97  E-value: 5.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  139 TCMNITHSQCQILPYHSTLAP-LLPIVKNMDMEKFLKF--FTYLHRL---SCYQHILLFGCSLAFPECVVDGDDRhgllP 212
Cdd:cd07447     3 TCTDLLLSYCSDVSYTQTTFPnLLGHRSREVTEAGAEYllLSVLHGLlggECNPDIRLLGCSVLAPRCENDKVIK----P 78

                          90       100       110
                  ....*....|....*....|....*....|..
gi 170295827  213 CRSFCEAAKEGCESVLGMVNSSWPDSLRCSQF 244
Cdd:cd07447    79 CRSTCEALRKRCSHAFDAIQMAWPYFLDCDRF 110
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
657-691 1.25e-04

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 40.31  E-value: 1.25e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 170295827   657 CQDNELECANHECVPRDLWCDGWVDCSDSSDEWGC 691
Cdd:pfam00057    3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 629-654 2.45e-03

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: 36.42  E-value: 2.45e-03
                          10        20
                  ....*....|....*....|....*.
gi 170295827  629 NKQCLKHTLICDGFPDCPDSMDEKNC 654
Cdd:cd00112    10 NGRCIPSSWVCDGEDDCGDGSDEENC 35
CRD_SMO cd07451
Cysteine-rich domain of the smoothened receptor (Smo) integral membrane protein; The ...
 151-241 3.41e-03

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: 38.89  E-value: 3.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170295827  151 LPYHSTLAPLLPIVKNMD--MEKFLKFFTYLHRLSCYQHILLFGCSLAFPECVVDGDDrhglLPCRSFCEAAKEGCESVL 228
Cdd:cd07451    18 LPYTYTSLDLVPDSTTQEevQEKLHLWSGLRNVPKCWAVIQPLLCALYMPKCENGKVE----LPSQEMCQATRGPCKIVE 93

                          90
                  ....*....|...
gi 170295827  229 gmVNSSWPDSLRC 241
Cdd:cd07451    94 --NERGWPDFLRC 104
 
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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