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Conserved domains on  [gi|37183120|gb|AAQ89360|]
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sFRP-2 [Homo sapiens]

Protein Classification

frizzled family protein( domain architecture ID 10165233)

frizzled family protein similar to the ten frizzleds (Fzd1-10) and smoothened (Smo), which are involved in transmitting the signals of Wnts and hedgehog proteins and are seven transmembrane-spanning proteins that constitute an unconventional class of G protein-coupled receptors; contains an N-terminal extracellular cysteine-rich domain (CRD) associated with their role in binding to Wnt ligands

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CRD_SFRP2 cd07446
Cysteine-rich domain of the secreted frizzled-related protein 2 (SFRP2), a regulator of Wnt ...
 36-163 1.77e-91

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: 267.16  E-value: 1.77e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37183120  36 KRSNCKPIPVNLQLCHGIEYQNMRLPNLLGHETMKEVLEQAGAWIPLVMKQCHPDTKKFLCSLFAPVCLDDLDETIQPCH 115
Cdd:cd07446   1 KKSNCKPIPANMLLCHGIEYTNMRLPNLLGHETMKEVLQQAGSWIPLVQKQCHPDTKKFLCSLFAPVCLDDLDEAIQPCR 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 37183120 116 SLCVQVKDRCAPVMSAFGFPWPDMLECDRFPQDNDLCIPLASSDHLLP 163
Cdd:cd07446  81 SLCEAVKDGCAPVMSAFGFPWPDMLDCTRFPLDNDLCIPPAGSDHLLP 128
NTR_Sfrp1_like cd03580
NTR domain, Secreted frizzled-related protein (Sfrp) 1-like subfamily; composed of proteins ...
 169-295 2.52e-55

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


:

Pssm-ID: 239635  Cd Length: 126  Bit Score: 175.18  E-value: 2.52e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37183120 169 PKVCEACKNKNDDDNDIMETLCKNDFALKIKVKEITYINRDTKIILETKsKTIYKLNGVSERDLKKSVLWLKDSLQCTCE 248
Cdd:cd03580   1 PKVCPPCENEEESAKTLLDNFCASDFALKVKIKEISYENGDRKVIGEKK-KEILKQGPLKKKDLKKLVLWLKNGANCPCP 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 37183120 249 EMNDINAPYLVMGQKQGGELVITSVKRWQKGQREFKRISRSIRKLQC 295
Cdd:cd03580  80 QLDNLNGVYLVMGRKVDGKLLLTSIYKWQKKNKEFKRAVRKWKKHKC 126
 
Name Accession Description Interval E-value
CRD_SFRP2 cd07446
Cysteine-rich domain of the secreted frizzled-related protein 2 (SFRP2), a regulator of Wnt ...
 36-163 1.77e-91

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: 267.16  E-value: 1.77e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37183120  36 KRSNCKPIPVNLQLCHGIEYQNMRLPNLLGHETMKEVLEQAGAWIPLVMKQCHPDTKKFLCSLFAPVCLDDLDETIQPCH 115
Cdd:cd07446   1 KKSNCKPIPANMLLCHGIEYTNMRLPNLLGHETMKEVLQQAGSWIPLVQKQCHPDTKKFLCSLFAPVCLDDLDEAIQPCR 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 37183120 116 SLCVQVKDRCAPVMSAFGFPWPDMLECDRFPQDNDLCIPLASSDHLLP 163
Cdd:cd07446  81 SLCEAVKDGCAPVMSAFGFPWPDMLDCTRFPLDNDLCIPPAGSDHLLP 128
NTR_Sfrp1_like cd03580
NTR domain, Secreted frizzled-related protein (Sfrp) 1-like subfamily; composed of proteins ...
 169-295 2.52e-55

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


Pssm-ID: 239635  Cd Length: 126  Bit Score: 175.18  E-value: 2.52e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37183120 169 PKVCEACKNKNDDDNDIMETLCKNDFALKIKVKEITYINRDTKIILETKsKTIYKLNGVSERDLKKSVLWLKDSLQCTCE 248
Cdd:cd03580   1 PKVCPPCENEEESAKTLLDNFCASDFALKVKIKEISYENGDRKVIGEKK-KEILKQGPLKKKDLKKLVLWLKNGANCPCP 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 37183120 249 EMNDINAPYLVMGQKQGGELVITSVKRWQKGQREFKRISRSIRKLQC 295
Cdd:cd03580  80 QLDNLNGVYLVMGRKVDGKLLLTSIYKWQKKNKEFKRAVRKWKKHKC 126
FRI smart00063
Frizzled; Drosophila melanogaster frizzled mediates signalling that polarises a precursor cell ...
 43-154 7.63e-52

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: 165.95  E-value: 7.63e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37183120     43 IPVNLQLCHGIEYQNMRLPNLLGHETMKEVLEQAGAWIPLVMKQCHPDTKKFLCSLFAPVCLDDLDeTIQPCHSLCVQVK 122
Cdd:smart00063   2 EPITIPLCKDLGYNLTSMPNLLGHTTQEEAGLELEQFHPLLNVQCSPDLRFFLCSVYAPICTEDLR-PILPCRSLCEAAR 80

                           90       100       110
                   ....*....|....*....|....*....|..
gi 37183120    123 DRCAPVMSAFGFPWPDMLECDRFPQDNDLCIP 154
Cdd:smart00063  81 EGCEPLMEKFGFPWPEFLRCDRFPVQEELCMD 112
Fz pfam01392
Fz domain; Also known as the CRD (cysteine rich domain), the C6 box in MuSK receptor. This ...
 44-148 7.37e-32

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: 114.59  E-value: 7.37e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37183120    44 PVNLQLCHGIEYQNMRLPNLLGHETMKEVLEQA-----GAWIPLVMKQCHPDTKKFLCSLFAPVC--LDDLDETIQPCHS 116
Cdd:pfam01392   3 PITLPMCLGLGYNATVFPNLLGHQTQEEAELSLaylvlSEFEPLVDLSCSPSLRLFLCSLYFPPCtlGPSPKPVCPPCRS 82

                          90       100       110
                  ....*....|....*....|....*....|....
gi 37183120   117 LCVQVKDRCAPVM--SAFGFPWPDMLECDRFPQD 148
Cdd:pfam01392  83 LCEEVRYGCEPLLeeAKFGFSWPEFLDCDSLPAD 116
C345C smart00643
Netrin C-terminal Domain;
186-288 1.34e-15

Netrin C-terminal Domain;


Pssm-ID: 214759  Cd Length: 114  Bit Score: 71.24  E-value: 1.34e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37183120    186 METLCK--NDFALKIKVKEITYINRDTKIilETKSKTIYKLnGVSERDLKKSVLWLKDS-LQCTCEEMNDINAPYLVMGQ 262
Cdd:smart00643   1 LEKACKsdVDYVYKVKVLSVEEEGGFDKY--TVKILEVIKS-GTDELVRGKNKLRVFISrASCRCPLLLKLGKSYLIMGK 77

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 37183120    263 -------KQGGELVITS---VKRWQKGQ-REFKRISR 288
Cdd:smart00643  78 sgdlwdaKGRGQYVLGKnswVEEWPTEEeCRLRRLQK 114
NTR pfam01759
UNC-6/NTR/C345C module; Sequence similarity between netrin UNC-6 and C345C complement protein ...
 187-285 2.51e-13

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


Pssm-ID: 396359  Cd Length: 106  Bit Score: 65.06  E-value: 2.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37183120   187 ETLCKN-DFALKIKVKEITyiNRDTKIILETKSKTIYKlNGVSERDLKKSVLWLKDSlQCTCEEMNdINAPYLVMGQK-- 263
Cdd:pfam01759   1 KKACKGsDYVYKVKVLSVE--EEGSFDKYTVKVKEVLK-EGTDKIQRGKVRLFLKRG-DCRCPQLR-LGKEYLIMGKVgd 75

                          90       100       110
                  ....*....|....*....|....*....|.
gi 37183120   264 ---------QGGELVITSVKRWQKGQREFKR 285
Cdd:pfam01759  76 legrgryvlDKNSWVEPWPTKWECKLRELQK 106
 
Name Accession Description Interval E-value
CRD_SFRP2 cd07446
Cysteine-rich domain of the secreted frizzled-related protein 2 (SFRP2), a regulator of Wnt ...
 36-163 1.77e-91

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: 267.16  E-value: 1.77e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37183120  36 KRSNCKPIPVNLQLCHGIEYQNMRLPNLLGHETMKEVLEQAGAWIPLVMKQCHPDTKKFLCSLFAPVCLDDLDETIQPCH 115
Cdd:cd07446   1 KKSNCKPIPANMLLCHGIEYTNMRLPNLLGHETMKEVLQQAGSWIPLVQKQCHPDTKKFLCSLFAPVCLDDLDEAIQPCR 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 37183120 116 SLCVQVKDRCAPVMSAFGFPWPDMLECDRFPQDNDLCIPLASSDHLLP 163
Cdd:cd07446  81 SLCEAVKDGCAPVMSAFGFPWPDMLDCTRFPLDNDLCIPPAGSDHLLP 128
CRD_SFRP5 cd07444
Cysteine-rich domain of the secreted frizzled-related protein 5 (SFRP5), a regulator of Wnt ...
 36-155 8.71e-56

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: 176.29  E-value: 8.71e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37183120  36 KRSNCKPIPVNLQLCHGIEYQNMRLPNLLGHETMKEVLEQAGAWIPLVMKQCHPDTKKFLCSLFAPVClddLDETIQPCH 115
Cdd:cd07444   3 KQPQCVDIPADLPLCHNVGYKRMRLPNLLEHESMAEVKQQASSWVPLLAKRCHADTQVFLCSLFAPVC---LDRPIYPCR 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 37183120 116 SLCVQVKDRCAPVMSAFGFPWPDMLECDRFPQDNDLCIPL 155
Cdd:cd07444  80 SLCEAVRDSCAPVMESYGFPWPEMLHCHKFPLDNDLCIAV 119
NTR_Sfrp1_like cd03580
NTR domain, Secreted frizzled-related protein (Sfrp) 1-like subfamily; composed of proteins ...
 169-295 2.52e-55

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


Pssm-ID: 239635  Cd Length: 126  Bit Score: 175.18  E-value: 2.52e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37183120 169 PKVCEACKNKNDDDNDIMETLCKNDFALKIKVKEITYINRDTKIILETKsKTIYKLNGVSERDLKKSVLWLKDSLQCTCE 248
Cdd:cd03580   1 PKVCPPCENEEESAKTLLDNFCASDFALKVKIKEISYENGDRKVIGEKK-KEILKQGPLKKKDLKKLVLWLKNGANCPCP 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 37183120 249 EMNDINAPYLVMGQKQGGELVITSVKRWQKGQREFKRISRSIRKLQC 295
Cdd:cd03580  80 QLDNLNGVYLVMGRKVDGKLLLTSIYKWQKKNKEFKRAVRKWKKHKC 126
FRI smart00063
Frizzled; Drosophila melanogaster frizzled mediates signalling that polarises a precursor cell ...
 43-154 7.63e-52

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: 165.95  E-value: 7.63e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37183120     43 IPVNLQLCHGIEYQNMRLPNLLGHETMKEVLEQAGAWIPLVMKQCHPDTKKFLCSLFAPVCLDDLDeTIQPCHSLCVQVK 122
Cdd:smart00063   2 EPITIPLCKDLGYNLTSMPNLLGHTTQEEAGLELEQFHPLLNVQCSPDLRFFLCSVYAPICTEDLR-PILPCRSLCEAAR 80

                           90       100       110
                   ....*....|....*....|....*....|..
gi 37183120    123 DRCAPVMSAFGFPWPDMLECDRFPQDNDLCIP 154
Cdd:smart00063  81 EGCEPLMEKFGFPWPEFLRCDRFPVQEELCMD 112
CRD_crescent cd07453
Cysteine-rich domain of the crescent protein; The cysteine-rich domain (CRD) is an essential ...
 38-177 7.38e-50

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: 161.65  E-value: 7.38e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37183120  38 SNCKPIPVNLQLCHGIEYQNMRLPNLLGHETMKEVLEQAGAWIPLVMKQCHPDTKKFLCSLFAPVCLDDLdetIQPCHSL 117
Cdd:cd07453   1 SPCMRIPKSMALCYDIGYSEMRIPNLLEHETMAEVIQQSSSWLPLLARECHPDARIFLCSLFAPICWDRP---IYPCRSL 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 37183120 118 CVQVKDRCAPVMSAFGFPWPDMLECDRFPQDNDLCIPLASSDHLLPateEAPKVCEACKN 177
Cdd:cd07453  78 CEAVRSSCAPLMACYGYPWPEILHCDKFPVDHDLCISPQFIDTLSP---ERVKPRASCED 134
CRD_SFRP1 cd07443
Cysteine-rich domain of the secreted frizzled-related protein 1 (SFRP1), a regulator of Wnt ...
 36-153 1.64e-47

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: 155.06  E-value: 1.64e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37183120  36 KRSNCKPIPVNLQLCHGIEYQNMRLPNLLGHETMKEVLEQAGAWIPLVMKQCHPDTKKFLCSLFAPVClddLDETIQPCH 115
Cdd:cd07443   3 KPPQCVDIPADLRLCHNVGYKKMVLPNLLDHETMAEVKQQASSWVPLLNKNCHKGTQVFLCSLFAPVC---LDRPVYPCR 79

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 37183120 116 SLCVQVKDRCAPVMSAFGFPWPDMLECDRFPQDnDLCI 153
Cdd:cd07443  80 WLCEAVRDSCEPVMQFFGFYWPEMLKCDKFPEG-EVCI 116
CRD_FZ cd07066
CRD_domain cysteine-rich domain, also known as Fz (frizzled) domain; CRD_FZ is an essential ...
 40-154 8.13e-42

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: 140.33  E-value: 8.13e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37183120  40 CKPIPvnLQLCHGIEYQNMRLPNLLGHETMKEVLEQAGAWIPLVMKQCHPDTKKFLCSLFAPVCLDDLDETIQPCHSLCV 119
Cdd:cd07066   2 CEPIP--LPLCRGLPYNTTRFPNLLGHESQEEAEQELESFTPLVNSGCHPDLRFFLCSLYFPECTPDGDRPIPPCRSLCE 79

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 37183120 120 QVKDRCAPVMSAFGFPWPDMLECDRFPQDN--DLCIP 154
Cdd:cd07066  80 EVRDSCEPLMLAFGFPWPEPLDCDRFPDSNeeGLCIS 116
CRD_sizzled cd07452
Cysteine-rich domain of the sizzled protein; The cysteine-rich domain (CRD) is an essential ...
 38-175 4.70e-41

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: 139.25  E-value: 4.70e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37183120  38 SNCKPIPVNLQLCHGIEYQNMRLPNLLGHETMKEVLEQAGAWIPLVMKQCHPDTKKFLCSLFAPVCLDDLdetIQPCHSL 117
Cdd:cd07452   7 TKCVPIPPEMSMCQDVGYSEMRLPNLLGHTSMAEVVPKSADWQTLLHTGCHPHARTFLCSLFAPVCLDTF---IQPCRSM 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 37183120 118 CVQVKDRCAPVMSAFGFPWPDMLECDRFPQDNDLCipLAS-SDHLLPATEEAPK-VCEAC 175
Cdd:cd07452  84 CVAVRDSCAPVLACHGHSWPESLDCDRFPAGEDMC--LASlSKEYQYFYKEFPKpACQSC 141
CRD_FZ4 cd07448
Cysteine-rich Wnt-binding domain of the frizzled 4 (Fz4) receptor; The cysteine-rich domain ...
 44-150 6.58e-35

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: 122.57  E-value: 6.58e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37183120  44 PVNLQLCHGIEYQNMRLPNLLGHETMKEVLEQAGAWIPLVMKQCHPDTKKFLCSLFAPVCLDDLDETIQPCHSLCVQVKD 123
Cdd:cd07448   6 PIRIEMCQGLGYNVTRMPNLVGHELQTDAELQLQTFTPLIQYGCSSQLKFFLCSVYVPMCTEKVPVPIGPCRPLCLSVKK 85

                        90       100
                ....*....|....*....|....*..
gi 37183120 124 RCAPVMSAFGFPWPDMLECDRFPQDND 150
Cdd:cd07448  86 RCLPVLKEFGFPWPEALNCSKFPPQNN 112
CRD_FZ9_like cd07457
Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 9; The cysteine-rich ...
 38-153 2.78e-33

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: 118.37  E-value: 2.78e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37183120  38 SNCKPIPVNLqlCHGIEYQNMRLPNLLGHETMKEVLEQAGAWIPLVMKQCHPDTKKFLCSLFAPVCLDDLDETIQPCHSL 117
Cdd:cd07457   1 GKCERITIPM--CQGIGYNMTRMPNLLGHESQSEAAISIHEFAPLVQYGCAEHLRFFLCSLYAPMCTEQVSIPIPACRSM 78

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 37183120 118 CVQVKDRCAPVMSAFGFPWPDMLECDRFPQDND---LCI 153
Cdd:cd07457  79 CEQARDKCSPIMEQFSFSWPDSLDCDRLPRKNDpkdLCM 117
CRD_FZ5_like cd07456
Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 5; The cysteine-rich ...
 40-153 3.34e-33

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: 117.88  E-value: 3.34e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37183120  40 CKPIPVnlQLCHGIEYQNMRLPNLLGHETMKEVLEQAGAWIPLVMKQCHPDTKKFLCSLFAPVCLDDLDETIQPCHSLCV 119
Cdd:cd07456   2 CEEITI--PMCKGIGYNMTYMPNQFNHDTQEEAGLEVHQFWPLVEIQCSPDLKFFLCSMYTPICLEDYDKPLPPCRSVCE 79

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 37183120 120 QVKDRCAPVMSAFGFPWPDMLECDRFPQ---DNDLCI 153
Cdd:cd07456  80 RARDGCAPIMRQYGFAWPERMSCDALPEggdPDNLCM 116
CRD_FZ8 cd07461
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 8 (Fz8) receptor; The cysteine-rich ...
 36-159 4.46e-32

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: 115.46  E-value: 4.46e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37183120  36 KRSNCKPIPVnlQLCHGIEYQNMRLPNLLGHETMKEVLEQAGAWIPLVMKQCHPDTKKFLCSLFAPVCLDDLDETIQPCH 115
Cdd:cd07461   1 KELQCQEITV--PLCKGIGYNYTYMPNQFNHDTQDEAGLEVHQFWPLVEIQCSPDLKFFLCSMYTPICLEDYKKPLPPCR 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 37183120 116 SLCVQVKDRCAPVMSAFGFPWPDMLECDRFPQDND---LCIPLASSD 159
Cdd:cd07461  79 SVCERAKAGCAPLMRQYGFPWPDRMRCDLLPEQGNpdtLCMDYNRTD 125
Fz pfam01392
Fz domain; Also known as the CRD (cysteine rich domain), the C6 box in MuSK receptor. This ...
 44-148 7.37e-32

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: 114.59  E-value: 7.37e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37183120    44 PVNLQLCHGIEYQNMRLPNLLGHETMKEVLEQA-----GAWIPLVMKQCHPDTKKFLCSLFAPVC--LDDLDETIQPCHS 116
Cdd:pfam01392   3 PITLPMCLGLGYNATVFPNLLGHQTQEEAELSLaylvlSEFEPLVDLSCSPSLRLFLCSLYFPPCtlGPSPKPVCPPCRS 82

                          90       100       110
                  ....*....|....*....|....*....|....
gi 37183120   117 LCVQVKDRCAPVM--SAFGFPWPDMLECDRFPQD 148
Cdd:pfam01392  83 LCEEVRYGCEPLLeeAKFGFSWPEFLDCDSLPAD 116
CRD_FZ9 cd07463
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 9 (Fz9) receptor; The cysteine-rich ...
 44-153 1.15e-31

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: 114.35  E-value: 1.15e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37183120  44 PVNLQLCHGIEYQNMRLPNLLGHETMKEVLEQAGAWIPLVMKQCHPDTKKFLCSLFAPVCLDDLDETIQPCHSLCVQVKD 123
Cdd:cd07463   7 PVVIPMCRGIGYNLTRMPNFLGHDSQREAAIKLNEFAPLVEYGCHVHLRFFLCSLYAPMCTDQVSTSIPACRPMCEQARQ 86

                        90       100       110
                ....*....|....*....|....*....|...
gi 37183120 124 RCAPVMSAFGFPWPDMLECDRFPQDND---LCI 153
Cdd:cd07463  87 KCSPIMEQFNFGWPESLDCSRLPTRNDpnaLCM 119
CRD_FZ1_like cd07458
Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 1; The cysteine-rich ...
 40-153 8.58e-31

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


Pssm-ID: 143567  Cd Length: 119  Bit Score: 111.73  E-value: 8.58e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37183120  40 CKPIPVnlQLCHGIEYQNMRLPNLLGHETMKEVLEQAGAWIPLVMKQCHPDTKKFLCSLFAPVClDDLDETIQPCHSLCV 119
Cdd:cd07458   3 CEPITI--PLCTDIPYNMTIFPNLLGHTKQEDAGLEVHQFYPLVKVQCSPDLKFFLCSVYAPVC-TVLERPIPPCRSLCE 79

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 37183120 120 QVKDRCAPVMSAFGFPWPDMLECDRFPQDN--DLCI 153
Cdd:cd07458  80 SARQGCEALMNKFGFQWPESLDCEKFPVHGagDLCV 115
CRD_FZ5 cd07460
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 5 (Fz5) receptor.proteins; The ...
 40-153 9.72e-29

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


Pssm-ID: 143569 [Multi-domain]  Cd Length: 127  Bit Score: 106.64  E-value: 9.72e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37183120  40 CKPIPVnlQLCHGIEYQNMRLPNLLGHETMKEVLEQAGAWIPLVMKQCHPDTKKFLCSLFAPVCLDDLDETIQPCHSLCV 119
Cdd:cd07460   5 CQEITV--PMCKGIGYNLTYMPNQFNHDTQDEAGLEVHQFWPLVEIQCSPDLRFFLCSMYTPICLPDYRKPLPPCRSVCE 82

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 37183120 120 QVKDRCAPVMSAFGFPWPDMLECDRFPQDND---LCI 153
Cdd:cd07460  83 RAKAGCSPLMRQYGFAWPERMNCDRLPVLGDpetLCM 119
CRD_FZ10 cd07462
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 10 (Fz10) receptor; The cysteine-rich ...
 44-153 2.44e-28

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


Pssm-ID: 143571  Cd Length: 127  Bit Score: 105.87  E-value: 2.44e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37183120  44 PVNLQLCHGIEYQNMRLPNLLGHETMKEVLEQAGAWIPLVMKQCHPDTKKFLCSLFAPVCLDDLDETIQPCHSLCVQVKD 123
Cdd:cd07462   7 PIEIPMCKDIGYNMTRMPNLMGHENQREAAIQLHEFAPLVEYGCHSHLKFFLCSLYAPMCTEQVSTPIPACRVMCEQARL 86

                        90       100       110
                ....*....|....*....|....*....|...
gi 37183120 124 RCAPVMSAFGFPWPDMLECDRFPQDND---LCI 153
Cdd:cd07462  87 KCSPIMEQFNFKWPDSLDCSKLPNKNDpnyLCM 119
CRD_FZ7 cd07466
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 7 (Fz7) receptor; The cysteine-rich ...
 44-160 2.75e-25

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


Pssm-ID: 143575 [Multi-domain]  Cd Length: 125  Bit Score: 97.46  E-value: 2.75e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37183120  44 PVNLQLCHGIEYQNMRLPNLLGHETMKEVLEQAGAWIPLVMKQCHPDTKKFLCSLFAPVClDDLDETIQPCHSLCVQVKD 123
Cdd:cd07466   7 PISIPLCTDIAYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSPELKFFLCSMYAPVC-TVLEQAIPPCRSLCERARQ 85

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 37183120 124 RCAPVMSAFGFPWPDMLECDRFPQD--NDLCIPLASSDH 160
Cdd:cd07466  86 GCEALMNKFGFQWPERLRCENFPVHgaGEICVGQNTSDA 124
CRD_FZ1 cd07465
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 1 (Fz1) receptor; The cysteine-rich ...
 44-163 4.48e-25

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


Pssm-ID: 143574  Cd Length: 127  Bit Score: 97.05  E-value: 4.48e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37183120  44 PVNLQLCHGIEYQNMRLPNLLGHETMKEVLEQAGAWIPLVMKQCHPDTKKFLCSLFAPVClDDLDETIQPCHSLCVQVKD 123
Cdd:cd07465   7 PISIPLCTDIAYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSAELKFFLCSMYAPVC-TVLEQALPPCRSLCERARQ 85

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 37183120 124 RCAPVMSAFGFPWPDMLECDRFPQD--NDLCIPLASSDHLLP 163
Cdd:cd07465  86 GCEALMNKFGFQWPDTLRCEKFPVHgaGELCVGQNTSESGTP 127
CRD_FZ2 cd07464
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 2 (Fz2) receptor; The cysteine-rich ...
 44-147 9.63e-25

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


Pssm-ID: 143573  Cd Length: 127  Bit Score: 96.31  E-value: 9.63e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37183120  44 PVNLQLCHGIEYQNMRLPNLLGHETMKEVLEQAGAWIPLVMKQCHPDTKKFLCSLFAPVClDDLDETIQPCHSLCVQVKD 123
Cdd:cd07464   7 PISIPLCTDIAYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSLELRFFLCSMYAPVC-TVLEQAIPPCRSICERARQ 85

                        90       100
                ....*....|....*....|....
gi 37183120 124 RCAPVMSAFGFPWPDMLECDRFPQ 147
Cdd:cd07464  86 GCEALMNKFGFQWPERLRCENFPR 109
CRD_FZ3 cd07449
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 3 (Fz3) receptor; The cysteine-rich ...
 44-147 9.92e-24

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: 93.53  E-value: 9.92e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37183120  44 PVNLQLCHGIEYQNMRLPNLLGHETMKEVLEQAGAWIPLVMKQCHPDTKKFLCSLFAPVCLDDLDETIqPCHSLCVQVKD 123
Cdd:cd07449   7 PITLRMCQDLPYNTTFMPNLLNHYDQQTAALAMEPFHPMVNLECSRDFRPFLCALYAPVCMEYGRVTL-PCRRLCQRAYS 85

                        90       100
                ....*....|....*....|....
gi 37183120 124 RCAPVMSAFGFPWPDMLECDRFPQ 147
Cdd:cd07449  86 ECSKLMEMFGVPWPEDMECSRFPD 109
CRD_LIN_17 cd07454
Cysteine-rich domain (CRD) of LIN_17; A cysteine-rich domain (CRD) is an essential component ...
 43-153 6.06e-23

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: 91.38  E-value: 6.06e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37183120  43 IPVNLQLCHGIEYQNMRLPNLLGHETMKEVLEQAGAWIPLVMKQCHPDTKKFLCSLFAPVCLDDLDETIQPCHSLCVQVK 122
Cdd:cd07454   6 IPIDIELCKDLPYNYTYFPNTILHNDQHTLQTHTEHFKPLMKTKCHPHIHFFICSVFAPMCPIGMPQAVTSCKSVCEQVK 85

                        90       100       110
                ....*....|....*....|....*....|.
gi 37183120 123 DRCAPVMSAFGFPWPDMLECDRFPQDNDLCI 153
Cdd:cd07454  86 ADCFSILEEFGIGWPEPLNCAQFPDPPELCM 116
CRD_corin_2 cd07888
One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ...
 44-153 6.35e-22

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: 88.53  E-value: 6.35e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37183120  44 PVNLQLCHGIEYQNMRLPNLLGHETMKE--VLEQAGAWIPLVMKQCHPDTKKFLCSLFAPVCLDDLDETIQPCHSLCVQV 121
Cdd:cd07888   4 PITLELCMNLPYNTTRYPNYLGHRTQKEasISWESSLFPALVQTNCYKYLMFFACTILVPKCDPVTQQRIPPCRSLCRNS 83

                        90       100       110
                ....*....|....*....|....*....|....*
gi 37183120 122 KDRCAPVMSAFGFPWPDMLECDRFP---QDNDLCI 153
Cdd:cd07888  84 KERCESVLGIVGLQWPEDTDCAQFPeenSDNQTCL 118
CRD_SFRP4 cd07442
Cysteine-rich domain of the secreted frizzled-related protein 4 (SFRP4), a Wnt antagonist; The ...
 45-153 9.55e-20

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


Pssm-ID: 143551  Cd Length: 127  Bit Score: 83.15  E-value: 9.55e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37183120  45 VNLQLCHGIEYQNMRLPNLLGHETMKEVLEQAGAWIPLVMKQCHPDTKKFLCSLFAPVC-LDDLDETIQPCHSLCVQVKD 123
Cdd:cd07442   8 VRIPMCRHMPWNITRMPNHLHHSTQENAVLAIEQYEELVDTGCSPVLPFFLCAMYAPICtLEFLYDPIKPCRSVCQRARD 87

                        90       100       110
                ....*....|....*....|....*....|.
gi 37183120 124 RCAPVMSAFGFPWPDMLECDRFP-QDNDLCI 153
Cdd:cd07442  88 GCEPIMRRYNHSWPESLACDDLPvYDRGVCI 118
CRD_SFRP3 cd07441
Cysteine-rich domain of the secreted frizzled-related protein 3 (SFRP3, alias FRZB), a Wnt ...
 44-153 9.00e-19

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: 80.48  E-value: 9.00e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37183120  44 PVNLQLCHGIEYQNMRLPNLLGHETMKEVLEQAGAWIPLVMKQCHPDTKKFLCSLFAPVCLDDLD-ETIQPCHSLCVQVK 122
Cdd:cd07441   6 PVRIPMCKSMPWNMTKMPNHLHHSTQANAVLAIEQFEGLLGTQCSPDLLFFLCAMYAPICTIDFQhEPIKPCKSVCERAR 85

                        90       100       110
                ....*....|....*....|....*....|..
gi 37183120 123 DRCAPVMSAFGFPWPDMLECDRFP-QDNDLCI 153
Cdd:cd07441  86 AGCEPVLIRYRHTWPESLACEELPvYDRGVCI 117
CRD_FZ6 cd07450
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 6 (Fz6) receptor; The cysteine-rich ...
 40-146 1.63e-16

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: 74.42  E-value: 1.63e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37183120  40 CKPIPVnlQLCHGIEYQNMRLPNLLGHETMKEVLEQAGAWIPLVMKQCHPDTKKFLCSLFAPVCLDDLdETIQPCHSLCV 119
Cdd:cd07450   5 CEPITV--PRCLKMPYNMTFFPNLMGHYDQDIAAVEMEPFLPLANLRCSPNVHTFLCQAFVPTCTEQI-HVVRPCRELCE 81

                        90       100
                ....*....|....*....|....*..
gi 37183120 120 QVKDRCAPVMSAFGFPWPDMLECDRFP 146
Cdd:cd07450  82 KVYSDCKKLIDTFGISWPEELECDRLQ 108
C345C smart00643
Netrin C-terminal Domain;
186-288 1.34e-15

Netrin C-terminal Domain;


Pssm-ID: 214759  Cd Length: 114  Bit Score: 71.24  E-value: 1.34e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37183120    186 METLCK--NDFALKIKVKEITYINRDTKIilETKSKTIYKLnGVSERDLKKSVLWLKDS-LQCTCEEMNDINAPYLVMGQ 262
Cdd:smart00643   1 LEKACKsdVDYVYKVKVLSVEEEGGFDKY--TVKILEVIKS-GTDELVRGKNKLRVFISrASCRCPLLLKLGKSYLIMGK 77

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 37183120    263 -------KQGGELVITS---VKRWQKGQ-REFKRISR 288
Cdd:smart00643  78 sgdlwdaKGRGQYVLGKnswVEEWPTEEeCRLRRLQK 114
CRD_Carboxypeptidase_Z cd07447
Cysteine-rich domain of carboxypeptidase Z, a member of the carboxypeptidase E family; The ...
 43-145 1.80e-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: 68.63  E-value: 1.80e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37183120  43 IPVNLQLCHGIEYQNMRLPNLLGHETmKEVLEQAGAWI------PLVMKQCHPDTKKFLCSLFAPVCldDLDETIQPCHS 116
Cdd:cd07447   5 TDLLLSYCSDVSYTQTTFPNLLGHRS-REVTEAGAEYLllsvlhGLLGGECNPDIRLLGCSVLAPRC--ENDKVIKPCRS 81

                        90       100
                ....*....|....*....|....*....
gi 37183120 117 LCVQVKDRCAPVMSAFGFPWPDMLECDRF 145
Cdd:cd07447  82 TCEALRKRCSHAFDAIQMAWPYFLDCDRF 110
CRD_Collagen_XVIII cd07455
Cysteine-rich domain of the variant 3 of collagen XVIII (V3C18 ); The cysteine-rich domain ...
 37-150 3.71e-14

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: 67.53  E-value: 3.71e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37183120  37 RSNCKPIPVNLQLCHGIEYQNMRLPNLLGHETMKEVLEQAGAWIPLVMKQCHPDTKKFLCSLFAPVCLDDLDETIQPCHS 116
Cdd:cd07455   2 RPRCLPVPSSLPFCSRLGIRSFWLPNFLNHTSVEEVRAVLAEWAWLLESGCHPSLEWFFCLLLVPSCGGGPPPPPPPCRQ 81

                        90       100       110
                ....*....|....*....|....*....|....
gi 37183120 117 LCVQVKDRCAPVMSAFGFPwpdmLECDRFPQDND 150
Cdd:cd07455  82 FCEVLQDSCWNLLEGGRLP----VACASLPEQED 111
NTR pfam01759
UNC-6/NTR/C345C module; Sequence similarity between netrin UNC-6 and C345C complement protein ...
 187-285 2.51e-13

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


Pssm-ID: 396359  Cd Length: 106  Bit Score: 65.06  E-value: 2.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37183120   187 ETLCKN-DFALKIKVKEITyiNRDTKIILETKSKTIYKlNGVSERDLKKSVLWLKDSlQCTCEEMNdINAPYLVMGQK-- 263
Cdd:pfam01759   1 KKACKGsDYVYKVKVLSVE--EEGSFDKYTVKVKEVLK-EGTDKIQRGKVRLFLKRG-DCRCPQLR-LGKEYLIMGKVgd 75

                          90       100       110
                  ....*....|....*....|....*....|.
gi 37183120   264 ---------QGGELVITSVKRWQKGQREFKR 285
Cdd:pfam01759  76 legrgryvlDKNSWVEPWPTKWECKLRELQK 106
NTR_like cd03523
NTR_like domain; a beta barrel with an oligosaccharide/oligonucleotide-binding fold found in ...
 187-272 2.11e-10

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


Pssm-ID: 239600  Cd Length: 105  Bit Score: 56.71  E-value: 2.11e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37183120 187 ETLCKNDFALKIKVKEITYINRDTKIilETKSKTIYKlNGVSERDLKKSVLWLKDSLQCTCEEMNDINAPYLVMGQKQG- 265
Cdd:cd03523   1 KAFCKSDYVVRAKIKEIKEENDDVKY--EVKIIKIYK-TGKAKADKADLRFYYTAPACCPCHPILNPGREYLIMGKEEDs 77


                ....*...
gi 37183120 266 -GELVITS 272
Cdd:cd03523  78 qGGLVLDP 85
CRD_corin_1 cd07445
One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ...
 87-145 5.14e-07

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


Pssm-ID: 143554  Cd Length: 130  Bit Score: 48.01  E-value: 5.14e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37183120  87 CHPDTKKFLCSLFAPVCLDDLDET--IQPCHSLCVQVKDRCAPVMSAFGFPWPDMLECDRF 145
Cdd:cd07445  49 CYQHIMLFGCSLALPECISDGDDRhgLLPCRSFCEAAKEGCEPVLGMVNASWPDFLRCSQF 109
 
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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