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Conserved domains on  [gi|197313632|ref|NP_001093997|]
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secreted frizzled-related protein 3 precursor [Rattus norvegicus]

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List of domain hits

Name Accession Description Interval E-value
CRD_SFRP3 cd07441
Cysteine-rich domain of the secreted frizzled-related protein 3 (SFRP3, alias FRZB), a Wnt ...
32-157 9.56e-96

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: 281.94  E-value: 9.56e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632  32 AAACEPVRIPLCKSLPWNMTKMPNHLHHSTQANAILAIEQFEGLLGTHCSPDLLFFLCAMYAPICTIDFQHEPIKPCKSV 111
Cdd:cd07441    1 AASCEPVRIPMCKSMPWNMTKMPNHLHHSTQANAVLAIEQFEGLLGTQCSPDLLFFLCAMYAPICTIDFQHEPIKPCKSV 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 197313632 112 CERARQGCEPILIKYRHSWPESLACEELPVYDRGVCISPEAIVTAD 157
Cdd:cd07441   81 CERARAGCEPVLIRYRHTWPESLACEELPVYDRGVCISPEAIVTAE 126
NTR_Sfrp3_like cd03581
NTR domain, Secreted frizzled-related protein (Sfrp) 3-like subfamily; composed of proteins ...
188-297 7.83e-68

NTR domain, Secreted frizzled-related protein (Sfrp) 3-like subfamily; composed of proteins similar to human Sfrp3 and Sfrp4. 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 Sfrp3 may suppress the growth and invasiveness of androgen-independent prostate cancer cells.


:

Pssm-ID: 239636  Cd Length: 111  Bit Score: 210.02  E-value: 7.83e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632 188 KTYFRNNYNYVIRAKVKEVKMKCHDVTAIVEVKEILKASLVNIPRDTVNLYSTSGCLCPPLSVNEEYVIMGYEDEERSRL 267
Cdd:cd03581    1 KTYLKNNYNYVIRAKVKEVKRGCHEVTAVVEVKEILKSSLVNIPRDTVTLYTNSGCLCPPLTPNEEYIIMGYEDEERSRL 80
                         90       100       110
                 ....*....|....*....|....*....|
gi 197313632 268 LLVEGSIAEKWKDRLGKKVKRWDMKLRHLG 297
Cdd:cd03581   81 LLVEGSLAEKWKDRLGKKVKRWDQKLQHQR 110
 
Name Accession Description Interval E-value
CRD_SFRP3 cd07441
Cysteine-rich domain of the secreted frizzled-related protein 3 (SFRP3, alias FRZB), a Wnt ...
32-157 9.56e-96

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: 281.94  E-value: 9.56e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632  32 AAACEPVRIPLCKSLPWNMTKMPNHLHHSTQANAILAIEQFEGLLGTHCSPDLLFFLCAMYAPICTIDFQHEPIKPCKSV 111
Cdd:cd07441    1 AASCEPVRIPMCKSMPWNMTKMPNHLHHSTQANAVLAIEQFEGLLGTQCSPDLLFFLCAMYAPICTIDFQHEPIKPCKSV 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 197313632 112 CERARQGCEPILIKYRHSWPESLACEELPVYDRGVCISPEAIVTAD 157
Cdd:cd07441   81 CERARAGCEPVLIRYRHTWPESLACEELPVYDRGVCISPEAIVTAE 126
NTR_Sfrp3_like cd03581
NTR domain, Secreted frizzled-related protein (Sfrp) 3-like subfamily; composed of proteins ...
188-297 7.83e-68

NTR domain, Secreted frizzled-related protein (Sfrp) 3-like subfamily; composed of proteins similar to human Sfrp3 and Sfrp4. 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 Sfrp3 may suppress the growth and invasiveness of androgen-independent prostate cancer cells.


Pssm-ID: 239636  Cd Length: 111  Bit Score: 210.02  E-value: 7.83e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632 188 KTYFRNNYNYVIRAKVKEVKMKCHDVTAIVEVKEILKASLVNIPRDTVNLYSTSGCLCPPLSVNEEYVIMGYEDEERSRL 267
Cdd:cd03581    1 KTYLKNNYNYVIRAKVKEVKRGCHEVTAVVEVKEILKSSLVNIPRDTVTLYTNSGCLCPPLTPNEEYIIMGYEDEERSRL 80
                         90       100       110
                 ....*....|....*....|....*....|
gi 197313632 268 LLVEGSIAEKWKDRLGKKVKRWDMKLRHLG 297
Cdd:cd03581   81 LLVEGSLAEKWKDRLGKKVKRWDQKLQHQR 110
Fz pfam01392
Fz domain; Also known as the CRD (cysteine rich domain), the C6 box in MuSK receptor. This ...
35-148 3.66e-50

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: 250583  Cd Length: 114  Bit Score: 164.43  E-value: 3.66e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632   35 CEPVRIPLCKSLPWNMTKMPNHLHHSTQANAILAIEQFEGLLGTHCSPDLLFFLCAMYAPICTIDFqHEPIKPCKSVCER 114
Cdd:pfam01392   1 CEPIRGPLCQGLGYNYTLMPNLLGHETQAEAELQLTAWTPLVGTLCSPALQFFLCSLYAPVCLEGG-REPIPPCRSLCEA 79
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 197313632  115 ARQGCEPILIKYRHSWPESLACEELPVY-DRGVCI 148
Cdd:pfam01392  80 VKEGCEPVMITFGFGWPELLECSRLPSPeDPGLCI 114
FRI smart00063
Frizzled; Drosophila melanogaster frizzled mediates signalling that polarises a precursor cell ...
35-150 3.66e-49

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: 161.71  E-value: 3.66e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632    35 CEPVRIPLCKSLPWNMTKMPNHLHHSTQANAILAIEQFEGLLGTHCSPDLLFFLCAMYAPICTIDFQhePIKPCKSVCER 114
Cdd:smart00063   1 CEPITIPLCKDLGYNLTSMPNLLGHTTQEEAGLELEQFHPLLNVQCSPDLRFFLCSVYAPICTEDLR--PILPCRSLCEA 78
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 197313632   115 ARQGCEPILIKYRHSWPESLACEELPVYDrGVCISP 150
Cdd:smart00063  79 AREGCEPLMEKFGFPWPEFLRCDRFPVQE-ELCMDP 113
NTR pfam01759
UNC-6/NTR/C345C module; Sequence similarity between netrin UNC-6 and C345C complement protein ...
194-289 1.80e-23

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: 250843  Cd Length: 109  Bit Score: 92.83  E-value: 1.80e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632  194 NYNYVIRAKVKEVKMKCHDVTAIVEVKEILKASLVNIPRDTVNLYSTSG--CLCPPL-SVNEEYVIMGYE----DEERSR 266
Cdd:pfam01759   5 KSDYVYKVKVLSVEEEGSFDIYTVRVKEVYKEGTDRVRGGKVRLFVSRRdlCKCPKLlPLGKEYLIMGKSgdldSKGRGR 84
                          90       100
                  ....*....|....*....|...
gi 197313632  267 LLLVEGSIAEKWKDRLGKKVKRW 289
Cdd:pfam01759  85 YVLDPNTWVEKWPDKWECRLRRL 107
C345C smart00643
Netrin C-terminal Domain;
187-288 2.08e-10

Netrin C-terminal Domain;


Pssm-ID: 214759  Cd Length: 114  Bit Score: 56.61  E-value: 2.08e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632   187 QKTYFRNNYNYVIRAKVKEVKMKCHDVTAIVEVKEILKASLVNIPRDTVNLY---STSGCLCPP-LSVNEEYVIMG---- 258
Cdd:smart00643   1 LEKACKSDVDYVYKVKVLSVEEEGGFDKYTVKILEVIKSGTDELVRGKNKLRvfiSRASCRCPLlLKLGKSYLIMGksgd 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 197313632   259 -YEDEERSRLLLVEGSIAEKWKDRLGKKVKR 288
Cdd:smart00643  81 lWDAKGRGQYVLGKNSWVEEWPTEEECRLRR 111
 
Name Accession Description Interval E-value
CRD_SFRP3 cd07441
Cysteine-rich domain of the secreted frizzled-related protein 3 (SFRP3, alias FRZB), a Wnt ...
32-157 9.56e-96

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: 281.94  E-value: 9.56e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632  32 AAACEPVRIPLCKSLPWNMTKMPNHLHHSTQANAILAIEQFEGLLGTHCSPDLLFFLCAMYAPICTIDFQHEPIKPCKSV 111
Cdd:cd07441    1 AASCEPVRIPMCKSMPWNMTKMPNHLHHSTQANAVLAIEQFEGLLGTQCSPDLLFFLCAMYAPICTIDFQHEPIKPCKSV 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 197313632 112 CERARQGCEPILIKYRHSWPESLACEELPVYDRGVCISPEAIVTAD 157
Cdd:cd07441   81 CERARAGCEPVLIRYRHTWPESLACEELPVYDRGVCISPEAIVTAE 126
NTR_Sfrp3_like cd03581
NTR domain, Secreted frizzled-related protein (Sfrp) 3-like subfamily; composed of proteins ...
188-297 7.83e-68

NTR domain, Secreted frizzled-related protein (Sfrp) 3-like subfamily; composed of proteins similar to human Sfrp3 and Sfrp4. 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 Sfrp3 may suppress the growth and invasiveness of androgen-independent prostate cancer cells.


Pssm-ID: 239636  Cd Length: 111  Bit Score: 210.02  E-value: 7.83e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632 188 KTYFRNNYNYVIRAKVKEVKMKCHDVTAIVEVKEILKASLVNIPRDTVNLYSTSGCLCPPLSVNEEYVIMGYEDEERSRL 267
Cdd:cd03581    1 KTYLKNNYNYVIRAKVKEVKRGCHEVTAVVEVKEILKSSLVNIPRDTVTLYTNSGCLCPPLTPNEEYIIMGYEDEERSRL 80
                         90       100       110
                 ....*....|....*....|....*....|
gi 197313632 268 LLVEGSIAEKWKDRLGKKVKRWDMKLRHLG 297
Cdd:cd03581   81 LLVEGSLAEKWKDRLGKKVKRWDQKLQHQR 110
CRD_SFRP4 cd07442
Cysteine-rich domain of the secreted frizzled-related protein 4 (SFRP4), a Wnt antagonist; The ...
31-155 3.24e-76

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: 232.22  E-value: 3.24e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632  31 QAAACEPVRIPLCKSLPWNMTKMPNHLHHSTQANAILAIEQFEGLLGTHCSPDLLFFLCAMYAPICTIDFQHEPIKPCKS 110
Cdd:cd07442    1 QGAPCEAVRIPMCRHMPWNITRMPNHLHHSTQENAVLAIEQYEELVDTGCSPVLPFFLCAMYAPICTLEFLYDPIKPCRS 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 197313632 111 VCERARQGCEPILIKYRHSWPESLACEELPVYDRGVCISPEAIVT 155
Cdd:cd07442   81 VCQRARDGCEPIMRRYNHSWPESLACDDLPVYDRGVCISPEAIVT 125
Fz pfam01392
Fz domain; Also known as the CRD (cysteine rich domain), the C6 box in MuSK receptor. This ...
35-148 3.66e-50

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: 250583  Cd Length: 114  Bit Score: 164.43  E-value: 3.66e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632   35 CEPVRIPLCKSLPWNMTKMPNHLHHSTQANAILAIEQFEGLLGTHCSPDLLFFLCAMYAPICTIDFqHEPIKPCKSVCER 114
Cdd:pfam01392   1 CEPIRGPLCQGLGYNYTLMPNLLGHETQAEAELQLTAWTPLVGTLCSPALQFFLCSLYAPVCLEGG-REPIPPCRSLCEA 79
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 197313632  115 ARQGCEPILIKYRHSWPESLACEELPVY-DRGVCI 148
Cdd:pfam01392  80 VKEGCEPVMITFGFGWPELLECSRLPSPeDPGLCI 114
FRI smart00063
Frizzled; Drosophila melanogaster frizzled mediates signalling that polarises a precursor cell ...
35-150 3.66e-49

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: 161.71  E-value: 3.66e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632    35 CEPVRIPLCKSLPWNMTKMPNHLHHSTQANAILAIEQFEGLLGTHCSPDLLFFLCAMYAPICTIDFQhePIKPCKSVCER 114
Cdd:smart00063   1 CEPITIPLCKDLGYNLTSMPNLLGHTTQEEAGLELEQFHPLLNVQCSPDLRFFLCSVYAPICTEDLR--PILPCRSLCEA 78
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 197313632   115 ARQGCEPILIKYRHSWPESLACEELPVYDrGVCISP 150
Cdd:smart00063  79 AREGCEPLMEKFGFPWPEFLRCDRFPVQE-ELCMDP 113
CRD_FZ5_like cd07456
Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 5; The cysteine-rich ...
35-140 2.31e-44

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: 149.47  E-value: 2.31e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632  35 CEPVRIPLCKSLPWNMTKMPNHLHHSTQANAILAIEQFEGLLGTHCSPDLLFFLCAMYAPICTIDFqHEPIKPCKSVCER 114
Cdd:cd07456    2 CEEITIPMCKGIGYNMTYMPNQFNHDTQEEAGLEVHQFWPLVEIQCSPDLKFFLCSMYTPICLEDY-DKPLPPCRSVCER 80
                         90       100
                 ....*....|....*....|....*.
gi 197313632 115 ARQGCEPILIKYRHSWPESLACEELP 140
Cdd:cd07456   81 ARDGCAPIMRQYGFAWPERMSCDALP 106
CRD_FZ1_like cd07458
Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 1; The cysteine-rich ...
35-148 5.43e-43

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: 146.02  E-value: 5.43e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632  35 CEPVRIPLCKSLPWNMTKMPNHLHHSTQANAILAIEQFEGLLGTHCSPDLLFFLCAMYAPICTIdfQHEPIKPCKSVCER 114
Cdd:cd07458    3 CEPITIPLCTDIPYNMTIFPNLLGHTKQEDAGLEVHQFYPLVKVQCSPDLKFFLCSVYAPVCTV--LERPIPPCRSLCES 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 197313632 115 ARQGCEPILIKYRHSWPESLACEELPVY-DRGVCI 148
Cdd:cd07458   81 ARQGCEALMNKFGFQWPESLDCEKFPVHgAGDLCV 115
CRD_FZ cd07066
CRD_domain cysteine-rich domain, also known as Fz (frizzled) domain; CRD_FZ is an essential ...
35-151 8.52e-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: 142.65  E-value: 8.52e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632  35 CEPVRIPLCKSLPWNMTKMPNHLHHSTQANAILAIEQFEGLLGTHCSPDLLFFLCAMYAPICTIDFQhEPIKPCKSVCER 114
Cdd:cd07066    2 CEPIPLPLCRGLPYNTTRFPNLLGHESQEEAEQELESFTPLVNSGCHPDLRFFLCSLYFPECTPDGD-RPIPPCRSLCEE 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 197313632 115 ARQGCEPILIKYRHSWPESLACEELPV-YDRGVCISPE 151
Cdd:cd07066   81 VRDSCEPLMLAFGFPWPEPLDCDRFPDsNEEGLCISPP 118
CRD_FZ5 cd07460
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 5 (Fz5) receptor.proteins; The ...
31-144 3.91e-41

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  Cd Length: 127  Bit Score: 141.31  E-value: 3.91e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632  31 QAAACEPVRIPLCKSLPWNMTKMPNHLHHSTQANAILAIEQFEGLLGTHCSPDLLFFLCAMYAPICTIDFqHEPIKPCKS 110
Cdd:cd07460    1 KALVCQEITVPMCKGIGYNLTYMPNQFNHDTQDEAGLEVHQFWPLVEIQCSPDLRFFLCSMYTPICLPDY-RKPLPPCRS 79
                         90       100       110
                 ....*....|....*....|....*....|....
gi 197313632 111 VCERARQGCEPILIKYRHSWPESLACEELPVYDR 144
Cdd:cd07460   80 VCERAKAGCSPLMRQYGFAWPERMNCDRLPVLGD 113
CRD_FZ8 cd07461
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 8 (Fz8) receptor; The cysteine-rich ...
34-141 5.39e-39

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: 135.49  E-value: 5.39e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632  34 ACEPVRIPLCKSLPWNMTKMPNHLHHSTQANAILAIEQFEGLLGTHCSPDLLFFLCAMYAPICTIDFQhEPIKPCKSVCE 113
Cdd:cd07461    4 QCQEITVPLCKGIGYNYTYMPNQFNHDTQDEAGLEVHQFWPLVEIQCSPDLKFFLCSMYTPICLEDYK-KPLPPCRSVCE 82
                         90       100
                 ....*....|....*....|....*...
gi 197313632 114 RARQGCEPILIKYRHSWPESLACEELPV 141
Cdd:cd07461   83 RAKAGCAPLMRQYGFPWPDRMRCDLLPE 110
CRD_FZ7 cd07466
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 7 (Fz7) receptor; The cysteine-rich ...
35-148 3.73e-36

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  Cd Length: 125  Bit Score: 128.28  E-value: 3.73e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632  35 CEPVRIPLCKSLPWNMTKMPNHLHHSTQANAILAIEQFEGLLGTHCSPDLLFFLCAMYAPICTIdfQHEPIKPCKSVCER 114
Cdd:cd07466    5 CQPISIPLCTDIAYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSPELKFFLCSMYAPVCTV--LEQAIPPCRSLCER 82
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 197313632 115 ARQGCEPILIKYRHSWPESLACEELPVYDRG-VCI 148
Cdd:cd07466   83 ARQGCEALMNKFGFQWPERLRCENFPVHGAGeICV 117
CRD_FZ2 cd07464
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 2 (Fz2) receptor; The cysteine-rich ...
35-140 7.52e-35

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: 124.81  E-value: 7.52e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632  35 CEPVRIPLCKSLPWNMTKMPNHLHHSTQANAILAIEQFEGLLGTHCSPDLLFFLCAMYAPICTIdfQHEPIKPCKSVCER 114
Cdd:cd07464    5 CQPISIPLCTDIAYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSLELRFFLCSMYAPVCTV--LEQAIPPCRSICER 82
                         90       100
                 ....*....|....*....|....*.
gi 197313632 115 ARQGCEPILIKYRHSWPESLACEELP 140
Cdd:cd07464   83 ARQGCEALMNKFGFQWPERLRCENFP 108
CRD_FZ1 cd07465
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 1 (Fz1) receptor; The cysteine-rich ...
35-145 1.51e-34

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: 124.01  E-value: 1.51e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632  35 CEPVRIPLCKSLPWNMTKMPNHLHHSTQANAILAIEQFEGLLGTHCSPDLLFFLCAMYAPICTIDFQHEPikPCKSVCER 114
Cdd:cd07465    5 CQPISIPLCTDIAYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSAELKFFLCSMYAPVCTVLEQALP--PCRSLCER 82
                         90       100       110
                 ....*....|....*....|....*....|.
gi 197313632 115 ARQGCEPILIKYRHSWPESLACEELPVYDRG 145
Cdd:cd07465   83 ARQGCEALMNKFGFQWPDTLRCEKFPVHGAG 113
CRD_FZ9_like cd07457
Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 9; The cysteine-rich ...
33-140 2.84e-32

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: 117.59  E-value: 2.84e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632  33 AACEPVRIPLCKSLPWNMTKMPNHLHHSTQANAILAIEQFEGLLGTHCSPDLLFFLCAMYAPICTiDFQHEPIKPCKSVC 112
Cdd:cd07457    1 GKCERITIPMCQGIGYNMTRMPNLLGHESQSEAAISIHEFAPLVQYGCAEHLRFFLCSLYAPMCT-EQVSIPIPACRSMC 79
                         90       100
                 ....*....|....*....|....*...
gi 197313632 113 ERARQGCEPILIKYRHSWPESLACEELP 140
Cdd:cd07457   80 EQARDKCSPIMEQFSFSWPDSLDCDRLP 107
CRD_FZ9 cd07463
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 9 (Fz9) receptor; The cysteine-rich ...
31-140 3.66e-32

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: 117.43  E-value: 3.66e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632  31 QAAACEPVRIPLCKSLPWNMTKMPNHLHHSTQANAILAIEQFEGLLGTHCSPDLLFFLCAMYAPICTiDFQHEPIKPCKS 110
Cdd:cd07463    1 RAAKCQPVVIPMCRGIGYNLTRMPNFLGHDSQREAAIKLNEFAPLVEYGCHVHLRFFLCSLYAPMCT-DQVSTSIPACRP 79
                         90       100       110
                 ....*....|....*....|....*....|
gi 197313632 111 VCERARQGCEPILIKYRHSWPESLACEELP 140
Cdd:cd07463   80 MCEQARQKCSPIMEQFNFGWPESLDCSRLP 109
CRD_FZ4 cd07448
Cysteine-rich Wnt-binding domain of the frizzled 4 (Fz4) receptor; The cysteine-rich domain ...
35-141 4.34e-32

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: 117.18  E-value: 4.34e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632  35 CEPVRIPLCKSLPWNMTKMPNHLHHSTQANAILAIEQFEGLLGTHCSPDLLFFLCAMYAPICTiDFQHEPIKPCKSVCER 114
Cdd:cd07448    4 CEPIRIEMCQGLGYNVTRMPNLVGHELQTDAELQLQTFTPLIQYGCSSQLKFFLCSVYVPMCT-EKVPVPIGPCRPLCLS 82
                         90       100
                 ....*....|....*....|....*..
gi 197313632 115 ARQGCEPILIKYRHSWPESLACEELPV 141
Cdd:cd07448   83 VKKRCLPVLKEFGFPWPEALNCSKFPP 109
CRD_FZ10 cd07462
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 10 (Fz10) receptor; The cysteine-rich ...
35-140 2.32e-29

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: 109.72  E-value: 2.32e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632  35 CEPVRIPLCKSLPWNMTKMPNHLHHSTQANAILAIEQFEGLLGTHCSPDLLFFLCAMYAPICTIDFQhEPIKPCKSVCER 114
Cdd:cd07462    5 CQPIEIPMCKDIGYNMTRMPNLMGHENQREAAIQLHEFAPLVEYGCHSHLKFFLCSLYAPMCTEQVS-TPIPACRVMCEQ 83
                         90       100
                 ....*....|....*....|....*.
gi 197313632 115 ARQGCEPILIKYRHSWPESLACEELP 140
Cdd:cd07462   84 ARLKCSPIMEQFNFKWPDSLDCSKLP 109
NTR_like cd03523
NTR_like domain; a beta barrel with an oligosaccharide/oligonucleotide-binding fold found in ...
188-295 3.66e-28

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: 106.01  E-value: 3.66e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632 188 KTYFRNNYnyVIRAKVKEVKMKCHDVTAIVEVKEILKASLVN-IPRDTVNLYSTSGC--LCPPLSVNEEYVIMGYEDEER 264
Cdd:cd03523    1 KAFCKSDY--VVRAKIKEIKEENDDVKYEVKIIKIYKTGKAKaDKADLRFYYTAPACcpCHPILNPGREYLIMGKEEDSQ 78
                         90       100       110
                 ....*....|....*....|....*....|.
gi 197313632 265 SRLLLVEGSIAEKWKDRLgkkvKRWDMKLRH 295
Cdd:cd03523   79 GGLVLDPLSFVEPWSPLS----LRQDRRLRE 105
CRD_FZ3 cd07449
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 3 (Fz3) receptor; The cysteine-rich ...
34-150 1.87e-26

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  Cd Length: 127  Bit Score: 102.01  E-value: 1.87e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632  34 ACEPVRIPLCKSLPWNMTKMPNHLHHSTQANAILAIEQFEGLLGTHCSPDLLFFLCAMYAPICTiDFQHEPIkPCKSVCE 113
Cdd:cd07449    4 SCEPITLRMCQDLPYNTTFMPNLLNHYDQQTAALAMEPFHPMVNLECSRDFRPFLCALYAPVCM-EYGRVTL-PCRRLCQ 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 197313632 114 RARQGCEPILIKYRHSWPESLACEELP----VYDRGVCISP 150
Cdd:cd07449   82 RAYSECSKLMEMFGVPWPEDMECSRFPdcdePYPRLVDLSL 122
CRD_crescent cd07453
Cysteine-rich domain of the crescent protein; The cysteine-rich domain (CRD) is an essential ...
37-160 4.05e-25

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  Cd Length: 135  Bit Score: 98.47  E-value: 4.05e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632  37 PVRIPLCKSLPWNMTKMPNHLHHSTQANAILAIEQFEGLLGTHCSPDLLFFLCAMYAPICTidfqHEPIKPCKSVCERAR 116
Cdd:cd07453    7 PKSMALCYDIGYSEMRIPNLLEHETMAEVIQQSSSWLPLLARECHPDARIFLCSLFAPICW----DRPIYPCRSLCEAVR 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 197313632 117 QGCEPILIKYRHSWPESLACEELPVyDRGVCISPEAIVTADGAD 160
Cdd:cd07453   83 SSCAPLMACYGYPWPEILHCDKFPV-DHDLCISPQFIDTLSPER 125
NTR pfam01759
UNC-6/NTR/C345C module; Sequence similarity between netrin UNC-6 and C345C complement protein ...
194-289 1.80e-23

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: 250843  Cd Length: 109  Bit Score: 92.83  E-value: 1.80e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632  194 NYNYVIRAKVKEVKMKCHDVTAIVEVKEILKASLVNIPRDTVNLYSTSG--CLCPPL-SVNEEYVIMGYE----DEERSR 266
Cdd:pfam01759   5 KSDYVYKVKVLSVEEEGSFDIYTVRVKEVYKEGTDRVRGGKVRLFVSRRdlCKCPKLlPLGKEYLIMGKSgdldSKGRGR 84
                          90       100
                  ....*....|....*....|...
gi 197313632  267 LLLVEGSIAEKWKDRLGKKVKRW 289
Cdd:pfam01759  85 YVLDPNTWVEKWPDKWECRLRRL 107
CRD_corin_2 cd07888
One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease; ...
35-151 5.54e-23

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  Cd Length: 122  Bit Score: 92.00  E-value: 5.54e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632  35 CEPVRIPLCKSLPWNMTKMPNHLHHSTQANAILAIEQ--FEGLLGTHCSPDLLFFLCAMYAPICTIDFQhEPIKPCKSVC 112
Cdd:cd07888    2 CEPITLELCMNLPYNTTRYPNYLGHRTQKEASISWESslFPALVQTNCYKYLMFFACTILVPKCDPVTQ-QRIPPCRSLC 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 197313632 113 ERARQGCEPILIKYRHSWPESLACEELPV--YDRGVCISPE 151
Cdd:cd07888   81 RNSKERCESVLGIVGLQWPEDTDCAQFPEenSDNQTCLLPD 121
CRD_FZ6 cd07450
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 6 (Fz6) receptor; The cysteine-rich ...
35-140 1.13e-21

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  Cd Length: 127  Bit Score: 88.28  E-value: 1.13e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632  35 CEPVRIPLCKSLPWNMTKMPNHLHHSTQANAILAIEQFEGLLGTHCSPDLLFFLCAMYAPICTIdfQHEPIKPCKSVCER 114
Cdd:cd07450    5 CEPITVPRCLKMPYNMTFFPNLMGHYDQDIAAVEMEPFLPLANLRCSPNVHTFLCQAFVPTCTE--QIHVVRPCRELCEK 82
                         90       100
                 ....*....|....*....|....*.
gi 197313632 115 ARQGCEPILIKYRHSWPESLACEELP 140
Cdd:cd07450   83 VYSDCKKLIDTFGISWPEELECDRLQ 108
CRD_sizzled cd07452
Cysteine-rich domain of the sizzled protein; The cysteine-rich domain (CRD) is an essential ...
37-150 5.69e-21

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: 86.86  E-value: 5.69e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632  37 PVRIPLCKSLPWNMTKMPNHLHHSTQANAILAIEQFEGLLGTHCSPDLLFFLCAMYAPICTIDFqhepIKPCKSVCERAR 116
Cdd:cd07452   13 PPEMSMCQDVGYSEMRLPNLLGHTSMAEVVPKSADWQTLLHTGCHPHARTFLCSLFAPVCLDTF----IQPCRSMCVAVR 88
                         90       100       110
                 ....*....|....*....|....*....|....
gi 197313632 117 QGCEPILIKYRHSWPESLACEELPVyDRGVCISP 150
Cdd:cd07452   89 DSCAPVLACHGHSWPESLDCDRFPA-GEDMCLAS 121
CRD_SFRP5 cd07444
Cysteine-rich domain of the secreted frizzled-related protein 5 (SFRP5), a regulator of Wnt ...
37-149 6.32e-21

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: 86.15  E-value: 6.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632  37 PVRIPLCKSLPWNMTKMPNHLHHSTQANAILAIEQFEGLLGTHCSPDLLFFLCAMYAPICTidfqHEPIKPCKSVCERAR 116
Cdd:cd07444   11 PADLPLCHNVGYKRMRLPNLLEHESMAEVKQQASSWVPLLAKRCHADTQVFLCSLFAPVCL----DRPIYPCRSLCEAVR 86
                         90       100       110
                 ....*....|....*....|....*....|...
gi 197313632 117 QGCEPILIKYRHSWPESLACEELPVyDRGVCIS 149
Cdd:cd07444   87 DSCAPVMESYGFPWPEMLHCHKFPL-DNDLCIA 118
CRD_SFRP2 cd07446
Cysteine-rich domain of the secreted frizzled-related protein 2 (SFRP2), a regulator of Wnt ...
35-150 4.07e-19

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: 81.11  E-value: 4.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632  35 CEPVRIP--LCKSLPWNMTKMPNHLHHSTQANAILAIEQFEGLLGTHCSPDLLFFLCAMYAPICtIDFQHEPIKPCKSVC 112
Cdd:cd07446    5 CKPIPANmlLCHGIEYTNMRLPNLLGHETMKEVLQQAGSWIPLVQKQCHPDTKKFLCSLFAPVC-LDDLDEAIQPCRSLC 83
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 197313632 113 ERARQGCEPILIKYRHSWPESLACEELPVyDRGVCISP 150
Cdd:cd07446   84 EAVKDGCAPVMSAFGFPWPDMLDCTRFPL-DNDLCIPP 120
CRD_LIN_17 cd07454
Cysteine-rich domain (CRD) of LIN_17; A cysteine-rich domain (CRD) is an essential component ...
35-150 4.43e-19

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: 80.98  E-value: 4.43e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632  35 CEPVRIPLCKSLPWNMTKMPNHLHHSTQANAILAIEQFEGLLGTHCSPDLLFFLCAMYAPICTiDFQHEPIKPCKSVCER 114
Cdd:cd07454    5 CIPIDIELCKDLPYNYTYFPNTILHNDQHTLQTHTEHFKPLMKTKCHPHIHFFICSVFAPMCP-IGMPQAVTSCKSVCEQ 83
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 197313632 115 ARQGCEPILIKYRHSWPESLACEELPVyDRGVCISP 150
Cdd:cd07454   84 VKADCFSILEEFGIGWPEPLNCAQFPD-PPELCMKP 118
CRD_SFRP1 cd07443
Cysteine-rich domain of the secreted frizzled-related protein 1 (SFRP1), a regulator of Wnt ...
37-149 9.37e-17

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: 74.55  E-value: 9.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632  37 PVRIPLCKSLPWNMTKMPNHLHHSTQANAILAIEQFEGLLGTHCSPDLLFFLCAMYAPICTidfqHEPIKPCKSVCERAR 116
Cdd:cd07443   11 PADLRLCHNVGYKKMVLPNLLDHETMAEVKQQASSWVPLLNKNCHKGTQVFLCSLFAPVCL----DRPVYPCRWLCEAVR 86
                         90       100       110
                 ....*....|....*....|....*....|...
gi 197313632 117 QGCEPILIKYRHSWPESLACEELPVYDrgVCIS 149
Cdd:cd07443   87 DSCEPVMQFFGFYWPEMLKCDKFPEGE--VCIA 117
NTR_netrin-4_like cd03578
NTR domain, Netrin-4-like subfamily; composed of the C-terminal NTR domains of netrin-4 (beta ...
195-286 2.97e-11

NTR domain, Netrin-4-like subfamily; composed of the C-terminal NTR domains of netrin-4 (beta netrin) and similar proteins. Netrins are secreted proteins that function as tropic cues in the direction of axon growth and cell migration during neural development. Netrin-4 is a basement membrane component that is important in neural, kidney and vascular development. It may also be involved in regulating the outgrowth and shape of epithelial cells during lung branching morphogenesis.


Pssm-ID: 239633  Cd Length: 111  Bit Score: 59.11  E-value: 2.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632 195 YNYVIRAKVKEVKMKCHDVTAIVEVKEILKASLVNIPRDTVNLYSTS----GCLCPPLSVNEEYVIMGYEDEERSRLLLV 270
Cdd:cd03578    9 YAYVIKIKVLSAHDKGTHAEVNVKIKKVLKSTKLKLSRGKRTLYPESwtsrGCTCPILNPGLEYLVAGHEDVRTGRLIVN 88
                         90
                 ....*....|....*.
gi 197313632 271 EGSIAEKWKDRLGKKV 286
Cdd:cd03578   89 MKSFVQHWKPSLGRKV 104
CRD_Carboxypeptidase_Z cd07447
Cysteine-rich domain of carboxypeptidase Z, a member of the carboxypeptidase E family; The ...
33-150 3.96e-11

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: 59.00  E-value: 3.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632  33 AACEPVRIPLCKSLPWNMTKMPNHLHHSTQ-----ANAILAIEQFEGLLGTHCSPDLLFFLCAMYAPICTIDfqhEPIKP 107
Cdd:cd07447    2 ATCTDLLLSYCSDVSYTQTTFPNLLGHRSRevteaGAEYLLLSVLHGLLGGECNPDIRLLGCSVLAPRCEND---KVIKP 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 197313632 108 CKSVCERARQGCEPILIKYRHSWPESLACEELPVYDRGVCISP 150
Cdd:cd07447   79 CRSTCEALRKRCSHAFDAIQMAWPYFLDCDRFFAGEQEGCYDP 121
CRD_Collagen_XVIII cd07455
Cysteine-rich domain of the variant 3 of collagen XVIII (V3C18 ); The cysteine-rich domain ...
37-148 6.27e-11

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: 58.29  E-value: 6.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632  37 PVRIPLCKSLPWNMTKMPNHLHHSTQANAILAIEQFEGLLGTHCSPDLLFFLCAMYAPICTIDFQHEPIkPCKSVCERAR 116
Cdd:cd07455    9 PSSLPFCSRLGIRSFWLPNFLNHTSVEEVRAVLAEWAWLLESGCHPSLEWFFCLLLVPSCGGGPPPPPP-PCRQFCEVLQ 87
                         90       100       110
                 ....*....|....*....|....*....|..
gi 197313632 117 QGCEPILIKYRHswpeSLACEELPVYDRGVCI 148
Cdd:cd07455   88 DSCWNLLEGGRL----PVACASLPEQEDGYCV 115
CRD_corin_1 cd07445
One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease; ...
43-151 1.64e-10

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: 57.25  E-value: 1.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632  43 CKSLPWNMTKMpnHLHHSTQANAILAIEQ---------FEGLLGTHCSPDLLFFLCAMYAPICTIDFQHEP-IKPCKSVC 112
Cdd:cd07445    5 CMNITHSQCQM--LPYHSTLKPSLLSVKNmemekflkfFSYLHRLSCYQHIMLFGCSLALPECISDGDDRHgLLPCRSFC 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 197313632 113 ERARQGCEPILIKYRHSWPESLACE------ELPVYDRGVCISPE 151
Cdd:cd07445   83 EAAKEGCEPVLGMVNASWPDFLRCSqfrnntETAVENRALCFSPQ 127
C345C smart00643
Netrin C-terminal Domain;
187-288 2.08e-10

Netrin C-terminal Domain;


Pssm-ID: 214759  Cd Length: 114  Bit Score: 56.61  E-value: 2.08e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632   187 QKTYFRNNYNYVIRAKVKEVKMKCHDVTAIVEVKEILKASLVNIPRDTVNLY---STSGCLCPP-LSVNEEYVIMG---- 258
Cdd:smart00643   1 LEKACKSDVDYVYKVKVLSVEEEGGFDKYTVKILEVIKSGTDELVRGKNKLRvfiSRASCRCPLlLKLGKSYLIMGksgd 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 197313632   259 -YEDEERSRLLLVEGSIAEKWKDRLGKKVKR 288
Cdd:smart00643  81 lWDAKGRGQYVLGKNSWVEEWPTEEECRLRR 111
NTR_netrin-1_like cd03579
NTR domain, Netrin-1-like subfamily; The C-terminal NTR domain of netrins is also called ...
197-288 1.25e-06

NTR domain, Netrin-1-like subfamily; The C-terminal NTR domain of netrins is also called domain C in the context of C. elegans netrin UNC-6. Netrins are secreted proteins that function as tropic cues in the direction of axon growth and cell migration during neural development. These proteins may be chemoattractive to some neurons and chemorepellant for others. In the case of netrin-1, attraction and repulsion responses are mediated by the DCC and UNC-5 receptor families. The biological activities of C. elegans UNC-6, which may either attract or repel migrating cells or axons, are mediated by its different domains. The C-terminal NTR domain of UNC-6 has been shown to inhibit axon branching activity.


Pssm-ID: 239634  Cd Length: 115  Bit Score: 45.70  E-value: 1.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632 197 YVIRAKVKEVKMKCHDVTAIVEVKEILKASLVNIPRDTVNLYSTSG---CLCPPLSVNEEYVIMGYEDE--ERSRLLLVE 271
Cdd:cd03579    9 YAVQAQVLSRETAGEWAKFTVNVQTVYKRGTSRLRRGDQPLWVPRKdlaCKCPKLKVGKSYLLLGKDEDspERGGLILDK 88
                         90
                 ....*....|....*..
gi 197313632 272 GSIAEKWKDRLGKKVKR 288
Cdd:cd03579   89 RSLVIEWRDEWARRLRR 105
NTR_TIMP_like cd03577
NTR domain, TIMP-like subfamily; TIMPs, or tissue inibitors of metalloproteases, are essential ...
178-259 4.90e-04

NTR domain, TIMP-like subfamily; TIMPs, or tissue inibitors of metalloproteases, are essential regulators of extracellular matrix turnover and remodeling. They form complexes with matrix metalloproteases (MMPs) and inactivate them irreversibly by non-covalently binding their active zinc-binding sites. This group contains domains similar to the TIMP NTR domain, which binds MMPs. Members of this group may or may not function as MMP inhibitors.


Pssm-ID: 239632  Cd Length: 116  Bit Score: 38.11  E-value: 4.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197313632 178 CKCKPVRATQKTyfrNNYNYVIRAKVKEVKMKCHD--VTAIVEVKEILKASLVNIprDTVNLYS-TSGCLC-PPLSVNEE 253
Cdd:cd03577    1 CSCMPQHPQEKY---CQADFVIKVKVLKKKLDGAGlnIRYTIEIKKVYKGSEKSL--LPITIYTpSDDSACgIPLLEGKE 75

                 ....*.
gi 197313632 254 YVIMGY 259
Cdd:cd03577   76 YLIAGK 81
CRD_SMO cd07451
Cysteine-rich domain of the smoothened receptor (Smo) integral membrane protein; The ...
87-145 2.86e-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: 36.19  E-value: 2.86e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 197313632  87 FLCAMYAPIC---TIDFqhepikPCKSVCERARQGCEpILIKYRhSWPESLACEELPVYDRG 145
Cdd:cd07451   60 LLCALYMPKCengKVEL------PSQEMCQATRGPCK-IVENER-GWPDFLRCDNDRFPPRG 113
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.12
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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