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Conserved domains on  [gi|6755999|ref|NP_036045|]
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wnt inhibitory factor 1 precursor [Mus musculus]

Protein Classification

WIF domain-containing protein( domain architecture ID 10648936)

WIF domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WIF smart00469
Wnt-inhibitory factor-1 like domain; Occurs as extracellular domain in metazoan Ryk receptor ...
 35-179 9.86e-66

Wnt-inhibitory factor-1 like domain; Occurs as extracellular domain in metazoan Ryk receptor tyrosine kinases. C. elegans Ryk is required for cell-cuticle recognition. WIF-1 binds to Wnt and inhibits its activity.


:

Pssm-ID: 128745  Cd Length: 136  Bit Score: 205.02  E-value: 9.86e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755999      35 SLYLWIDAHQARVLIGFEEDILIVSEGKMAPFTHDFrkaqqrMPAIPVNIHSMNFTWQAAGQaEYFYEFLSLRSLDKGIM 114
Cdd:smart00469   1 SLNLFLSAHEVRRLIGVSAELYYVREGKISPYALNF------MVPVPANIHDLSFTWQALGQ-EYVPYSLNVRSDDKEVL 73

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6755999     115 ADPTVNVPLLGTVPHKASVVQVGFPCLGKQDgvAAFEVNVIVMNSEGNTILRTPQNAIFFKTCQQ 179
Cdd:smart00469  74 PRPIVNISLLGTVPHTLQVFQVELKCSGKRD--AEVEVTVIVEVSLGSTKNPTPLNFRRKKICLQ 136
 
Name Accession Description Interval E-value
WIF smart00469
Wnt-inhibitory factor-1 like domain; Occurs as extracellular domain in metazoan Ryk receptor ...
 35-179 9.86e-66

Wnt-inhibitory factor-1 like domain; Occurs as extracellular domain in metazoan Ryk receptor tyrosine kinases. C. elegans Ryk is required for cell-cuticle recognition. WIF-1 binds to Wnt and inhibits its activity.


Pssm-ID: 128745  Cd Length: 136  Bit Score: 205.02  E-value: 9.86e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755999      35 SLYLWIDAHQARVLIGFEEDILIVSEGKMAPFTHDFrkaqqrMPAIPVNIHSMNFTWQAAGQaEYFYEFLSLRSLDKGIM 114
Cdd:smart00469   1 SLNLFLSAHEVRRLIGVSAELYYVREGKISPYALNF------MVPVPANIHDLSFTWQALGQ-EYVPYSLNVRSDDKEVL 73

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6755999     115 ADPTVNVPLLGTVPHKASVVQVGFPCLGKQDgvAAFEVNVIVMNSEGNTILRTPQNAIFFKTCQQ 179
Cdd:smart00469  74 PRPIVNISLLGTVPHTLQVFQVELKCSGKRD--AEVEVTVIVEVSLGSTKNPTPLNFRRKKICLQ 136
WIF pfam02019
WIF domain; The WIF domain is found in the RYK tyrosine kinase receptors and WIF, the ...
 39-169 3.19e-46

WIF domain; The WIF domain is found in the RYK tyrosine kinase receptors and WIF, the Wnt-inhibitory- factor. The domain is extracellular and contains two conserved cysteines that may form a disulphide bridge. This domain is Wnt binding in WIF, and it has been suggested that RYK may also bind to Wnt. The WIF domain is a member of the immunoglobulin superfamily, and it comprises nine beta-strands and two alpha-helices, with two of the beta-strands (6 and 9) interrupted by four and six residues of irregular secondary structure, respectively. Considering that the activity of Wnts depends on the presence of a palmitoylated cysteine residue in their amino-terminal polypeptide segment, Wnt proteins are lipid-modified and can act as stem cell growth factors, it is likely that the WIF domain recognizes and binds to Wnts that have been activated by palmitoylation and that the recognition of palmitoylated Wnts by WIF-1 is effected by its WIF domain rather than by its EGF domains. A strong binding affinity for palmitoylated cysteine residues would further explain the remarkably high affinity of human WIF-1 not only for mammalian Wnts, but also for Wnts from Xenopus and Drosophila.


Pssm-ID: 460414  Cd Length: 126  Bit Score: 154.31  E-value: 3.19e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755999     39 WIDAHQARVLIGFEEDILIVSEGKMAPFTHDFrkaqqrMPAIPVNIHSMNFTWQAAGQAEYFYEFlSLRSLDKGIMADPT 118
Cdd:pfam02019   1 YIDEQEVKRLLGLEAELYYVREGIVNPYALDF------LPPVPSEVNSLNFTWKSGGKKKVPYSF-SLESDDESILNPPT 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 6755999    119 VNVPLLGTVPHKASVVQVGFPCLGKQDGVAAFEVNVIVM--NSEGNTILRTPQ 169
Cdd:pfam02019  74 LNISLKGTVPREPSVFSVLLPCSGNRSGEATVSIQLNITigSSLNGTPLNLKR 126
 
Name Accession Description Interval E-value
WIF smart00469
Wnt-inhibitory factor-1 like domain; Occurs as extracellular domain in metazoan Ryk receptor ...
 35-179 9.86e-66

Wnt-inhibitory factor-1 like domain; Occurs as extracellular domain in metazoan Ryk receptor tyrosine kinases. C. elegans Ryk is required for cell-cuticle recognition. WIF-1 binds to Wnt and inhibits its activity.


Pssm-ID: 128745  Cd Length: 136  Bit Score: 205.02  E-value: 9.86e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755999      35 SLYLWIDAHQARVLIGFEEDILIVSEGKMAPFTHDFrkaqqrMPAIPVNIHSMNFTWQAAGQaEYFYEFLSLRSLDKGIM 114
Cdd:smart00469   1 SLNLFLSAHEVRRLIGVSAELYYVREGKISPYALNF------MVPVPANIHDLSFTWQALGQ-EYVPYSLNVRSDDKEVL 73

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6755999     115 ADPTVNVPLLGTVPHKASVVQVGFPCLGKQDgvAAFEVNVIVMNSEGNTILRTPQNAIFFKTCQQ 179
Cdd:smart00469  74 PRPIVNISLLGTVPHTLQVFQVELKCSGKRD--AEVEVTVIVEVSLGSTKNPTPLNFRRKKICLQ 136
WIF pfam02019
WIF domain; The WIF domain is found in the RYK tyrosine kinase receptors and WIF, the ...
 39-169 3.19e-46

WIF domain; The WIF domain is found in the RYK tyrosine kinase receptors and WIF, the Wnt-inhibitory- factor. The domain is extracellular and contains two conserved cysteines that may form a disulphide bridge. This domain is Wnt binding in WIF, and it has been suggested that RYK may also bind to Wnt. The WIF domain is a member of the immunoglobulin superfamily, and it comprises nine beta-strands and two alpha-helices, with two of the beta-strands (6 and 9) interrupted by four and six residues of irregular secondary structure, respectively. Considering that the activity of Wnts depends on the presence of a palmitoylated cysteine residue in their amino-terminal polypeptide segment, Wnt proteins are lipid-modified and can act as stem cell growth factors, it is likely that the WIF domain recognizes and binds to Wnts that have been activated by palmitoylation and that the recognition of palmitoylated Wnts by WIF-1 is effected by its WIF domain rather than by its EGF domains. A strong binding affinity for palmitoylated cysteine residues would further explain the remarkably high affinity of human WIF-1 not only for mammalian Wnts, but also for Wnts from Xenopus and Drosophila.


Pssm-ID: 460414  Cd Length: 126  Bit Score: 154.31  E-value: 3.19e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755999     39 WIDAHQARVLIGFEEDILIVSEGKMAPFTHDFrkaqqrMPAIPVNIHSMNFTWQAAGQAEYFYEFlSLRSLDKGIMADPT 118
Cdd:pfam02019   1 YIDEQEVKRLLGLEAELYYVREGIVNPYALDF------LPPVPSEVNSLNFTWKSGGKKKVPYSF-SLESDDESILNPPT 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 6755999    119 VNVPLLGTVPHKASVVQVGFPCLGKQDGVAAFEVNVIVM--NSEGNTILRTPQ 169
Cdd:pfam02019  74 LNISLKGTVPREPSVFSVLLPCSGNRSGEATVSIQLNITigSSLNGTPLNLKR 126
 
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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