O70421 · FZD1_MOUSE
- ProteinFrizzled-1
- GeneFzd1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids642 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Receptor for Wnt proteins (PubMed:15923619).
Activated by WNT7B (PubMed:15923619).
Activated by WNT3A, WNT3, WNT1 and to a lesser extent WNT2, but apparently not by WNT4, WNT5A, WNT5B, WNT6, WNT7A or WNT7B (By similarity).
Contradictory results showing activation by WNT7B have been described for mouse (PubMed:15923619).
Functions in the canonical Wnt/beta-catenin signaling pathway (PubMed:15923619).
The canonical Wnt/beta-catenin signaling pathway leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes (PubMed:15923619).
A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues (Probable)
Activated by WNT7B (PubMed:15923619).
Activated by WNT3A, WNT3, WNT1 and to a lesser extent WNT2, but apparently not by WNT4, WNT5A, WNT5B, WNT6, WNT7A or WNT7B (By similarity).
Contradictory results showing activation by WNT7B have been described for mouse (PubMed:15923619).
Functions in the canonical Wnt/beta-catenin signaling pathway (PubMed:15923619).
The canonical Wnt/beta-catenin signaling pathway leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes (PubMed:15923619).
A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues (Probable)
GO annotations
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFrizzled-1
- Short namesFz-1; mFz1
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionO70421
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 69-317 | Extracellular | ||||
Sequence: VRAQAAGQVSGPGQQAPPPPQPQQSGQQYNGERGISIPDHGYCQPISIPLCTDIAYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSAELKFFLCSMYAPVCTVLEQALPPCRSLCERARQGCEALMNKFGFQWPDTLKCEKFPVHGAGELCVGQNTSDKGTPTPSLLPEFWTSNPQHGGGGYRGGYPGGAGTVERGKFSCPRALRVPSYLNYHFLGEKDCGAPCEPTKVYGLMYFGPEELRFSRTW | ||||||
Transmembrane | 318-338 | Helical; Name=1 | ||||
Sequence: IGIWSVLCCASTLFTVLTYLV | ||||||
Topological domain | 339-349 | Cytoplasmic | ||||
Sequence: DMRRFSYPERP | ||||||
Transmembrane | 350-370 | Helical; Name=2 | ||||
Sequence: IIFLSGCYTAVAVAYIAGFLL | ||||||
Topological domain | 371-397 | Extracellular | ||||
Sequence: EDRVVCNDKFAEDGARTVAQGTKKEGC | ||||||
Transmembrane | 398-418 | Helical; Name=3 | ||||
Sequence: TILFMMLYFFSMASSIWWVIL | ||||||
Topological domain | 419-440 | Cytoplasmic | ||||
Sequence: SLTWFLAAGMKWGHEAIEANSQ | ||||||
Transmembrane | 441-461 | Helical; Name=4 | ||||
Sequence: YFHLAAWAVPAIKTITILALG | ||||||
Topological domain | 462-484 | Extracellular | ||||
Sequence: QVDGDVLSGVCFVGLNNVDALRG | ||||||
Transmembrane | 485-505 | Helical; Name=5 | ||||
Sequence: FVLAPLFVYLFIGTSFLLAGF | ||||||
Topological domain | 506-531 | Cytoplasmic | ||||
Sequence: VSLFRIRTIMKHDGTKTEKLEKLMVR | ||||||
Transmembrane | 532-552 | Helical; Name=6 | ||||
Sequence: IGVFSVLYTVPATIVIACYFY | ||||||
Topological domain | 553-593 | Extracellular | ||||
Sequence: EQAFRDQWERSWVAQSCKSYAIPCPHLQGGGGVPPHPPMSP | ||||||
Transmembrane | 594-614 | Helical; Name=7 | ||||
Sequence: DFTVFMIKYLMTLIVGITSGF | ||||||
Topological domain | 615-642 | Cytoplasmic | ||||
Sequence: WIWSGKTLNSWRKFYTRLTNSKQGETTV |
Keywords
- Cellular component
Phenotypes & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 27 variants from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-68 | |||||
Sequence: MAEEAAPSESRAAGRLSLELCAEALPGRREEVGHEDTASHRRPRADPRRWASGLLLLLWLLEAPLLLG | ||||||
Chain | PRO_0000012974 | 69-642 | Frizzled-1 | |||
Sequence: VRAQAAGQVSGPGQQAPPPPQPQQSGQQYNGERGISIPDHGYCQPISIPLCTDIAYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSAELKFFLCSMYAPVCTVLEQALPPCRSLCERARQGCEALMNKFGFQWPDTLKCEKFPVHGAGELCVGQNTSDKGTPTPSLLPEFWTSNPQHGGGGYRGGYPGGAGTVERGKFSCPRALRVPSYLNYHFLGEKDCGAPCEPTKVYGLMYFGPEELRFSRTWIGIWSVLCCASTLFTVLTYLVDMRRFSYPERPIIFLSGCYTAVAVAYIAGFLLEDRVVCNDKFAEDGARTVAQGTKKEGCTILFMMLYFFSMASSIWWVILSLTWFLAAGMKWGHEAIEANSQYFHLAAWAVPAIKTITILALGQVDGDVLSGVCFVGLNNVDALRGFVLAPLFVYLFIGTSFLLAGFVSLFRIRTIMKHDGTKTEKLEKLMVRIGVFSVLYTVPATIVIACYFYEQAFRDQWERSWVAQSCKSYAIPCPHLQGGGGVPPHPPMSPDFTVFMIKYLMTLIVGITSGFWIWSGKTLNSWRKFYTRLTNSKQGETTV | ||||||
Disulfide bond | 111↔172 | |||||
Sequence: CQPISIPLCTDIAYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSAELKFFLCSMYAPVC | ||||||
Disulfide bond | 119↔165 | |||||
Sequence: CTDIAYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSAELKFFLC | ||||||
Glycosylation | 125 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 156↔193 | |||||
Sequence: CSAELKFFLCSMYAPVCTVLEQALPPCRSLCERARQGC | ||||||
Disulfide bond | 182↔222 | |||||
Sequence: CRSLCERARQGCEALMNKFGFQWPDTLKCEKFPVHGAGELC | ||||||
Disulfide bond | 186↔210 | |||||
Sequence: CERARQGCEALMNKFGFQWPDTLKC | ||||||
Glycosylation | 226 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
Ubiquitinated by ZNRF3, leading to its degradation by the proteasome.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Structure
Family & Domains
Features
Showing features for region, domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 26-45 | Disordered | ||||
Sequence: PGRREEVGHEDTASHRRPRA | ||||||
Region | 76-99 | Disordered | ||||
Sequence: QVSGPGQQAPPPPQPQQSGQQYNG | ||||||
Domain | 106-225 | FZ | ||||
Sequence: PDHGYCQPISIPLCTDIAYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSAELKFFLCSMYAPVCTVLEQALPPCRSLCERARQGCEALMNKFGFQWPDTLKCEKFPVHGAGELCVGQ | ||||||
Motif | 620-625 | Lys-Thr-X-X-X-Trp motif, mediates interaction with the PDZ domain of Dvl family members | ||||
Sequence: KTLNSW | ||||||
Motif | 640-642 | PDZ-binding | ||||
Sequence: TTV |
Domain
Lys-Thr-X-X-X-Trp motif interacts with the PDZ domain of Dvl (Disheveled) family members and is involved in the activation of the Wnt/beta-catenin signaling pathway.
The FZ domain is involved in binding with Wnt ligands.
Sequence similarities
Belongs to the G-protein coupled receptor Fz/Smo family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Protein family/group databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length642
- Mass (Da)71,127
- Last updated2011-07-27 v3
- Checksum7674583F819014E2
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 122 | in Ref. 1; AAC12873 | ||||
Sequence: I → M | ||||||
Sequence conflict | 246 | in Ref. 1; AAC12873 | ||||
Sequence: P → G | ||||||
Sequence conflict | 341 | in Ref. 1; AAC12873 | ||||
Sequence: R → P | ||||||
Sequence conflict | 352 | in Ref. 1; AAC12873 | ||||
Sequence: F → S | ||||||
Sequence conflict | 393 | in Ref. 1; AAC12873 | ||||
Sequence: K → N | ||||||
Sequence conflict | 474 | in Ref. 1; AAC12873 | ||||
Sequence: V → L | ||||||
Sequence conflict | 615 | in Ref. 1; AAC12873 | ||||
Sequence: W → R |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF054623 EMBL· GenBank· DDBJ | AAC12873.2 EMBL· GenBank· DDBJ | mRNA | ||
AK143101 EMBL· GenBank· DDBJ | BAE25269.1 EMBL· GenBank· DDBJ | mRNA | ||
CH466600 EMBL· GenBank· DDBJ | EDL14633.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC053010 EMBL· GenBank· DDBJ | AAH53010.1 EMBL· GenBank· DDBJ | mRNA | ||
AF005202 EMBL· GenBank· DDBJ | AAC01952.1 EMBL· GenBank· DDBJ | mRNA |