Q08463 · FZD1_RAT
- ProteinFrizzled-1
- GeneFzd1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids641 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Receptor for Wnt proteins. Activated by WNT3A, WNT3, WNT1 and to a lesser extent WNT2, but apparently not by WNT4, WNT5A, WNT5B, WNT6 or WNT7A. Contradictory results have been reported for activation by WNT7B. Functions in the canonical Wnt/beta-catenin signaling pathway. 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 (By similarity).
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)
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
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFrizzled-1
- Short namesFz-1; rFz1
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionQ08463
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 | 69-316 | Extracellular | ||||
Sequence: VRAQPAGQVSGPGQQRPPPPQPQQGGQQYNGERGISIPDHGYCQPISIPLCTDIAYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSAELKFFLCSMYAPVCTVLEQALPPCRSLCERAQGCEALMNKFGFQWPDTLKCEKFPVHGAGELCVGQNTSDKGTPTPSLLPEFWTSNPQHGGGGYRGGYPGGAGPVERGKFSCPRALRVPSYLNYHFLGEKDCGAPCEPTKVYGLMYFGPEELRFSRTW | ||||||
Transmembrane | 317-337 | Helical; Name=1 | ||||
Sequence: IGIWSVLCCASTLFTVLTYLV | ||||||
Topological domain | 338-348 | Cytoplasmic | ||||
Sequence: DMRRFSYPERP | ||||||
Transmembrane | 349-369 | Helical; Name=2 | ||||
Sequence: IIFLSGCYTAVAVAYIAGFLL | ||||||
Topological domain | 370-396 | Extracellular | ||||
Sequence: EDRVVCNDKFAEDGARTVAQGTKKEGC | ||||||
Transmembrane | 397-417 | Helical; Name=3 | ||||
Sequence: TILFMMLYFFSMASSIWWVIL | ||||||
Topological domain | 418-439 | Cytoplasmic | ||||
Sequence: SLTWFLAAGMKWGHEAIEANSQ | ||||||
Transmembrane | 440-460 | Helical; Name=4 | ||||
Sequence: YFHLAAWAVPAIKTITILALG | ||||||
Topological domain | 461-483 | Extracellular | ||||
Sequence: QVDGDVLSGVCFVGLNNVDALRG | ||||||
Transmembrane | 484-504 | Helical; Name=5 | ||||
Sequence: FVLAPLFVYLFIGTSFLLAGF | ||||||
Topological domain | 505-530 | Cytoplasmic | ||||
Sequence: VSLFRIRTIMKHDGTKTEKLEKLMVR | ||||||
Transmembrane | 531-551 | Helical; Name=6 | ||||
Sequence: IGVFSVLYTVPATIVIACYFY | ||||||
Topological domain | 552-595 | Extracellular | ||||
Sequence: EQAFRDQWERSWVAQSCKSYAIPCPHLQGGGGVPPHPPMSPDFT | ||||||
Transmembrane | 596-616 | Helical; Name=7 | ||||
Sequence: VFMIKYLMTLIVGITSGFWIW | ||||||
Topological domain | 617-641 | Cytoplasmic | ||||
Sequence: SGKTLNSWRKFYTRLTNSKQGETTV |
Keywords
- Cellular component
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-68 | |||||
Sequence: MAEEAVPSESRAAGRPSLELCAVALPGRREEVGHQDTAGHRRPRAHSRCWARGLLLLLWLLEAPLLLG | ||||||
Chain | PRO_0000012975 | 69-641 | Frizzled-1 | |||
Sequence: VRAQPAGQVSGPGQQRPPPPQPQQGGQQYNGERGISIPDHGYCQPISIPLCTDIAYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSAELKFFLCSMYAPVCTVLEQALPPCRSLCERAQGCEALMNKFGFQWPDTLKCEKFPVHGAGELCVGQNTSDKGTPTPSLLPEFWTSNPQHGGGGYRGGYPGGAGPVERGKFSCPRALRVPSYLNYHFLGEKDCGAPCEPTKVYGLMYFGPEELRFSRTWIGIWSVLCCASTLFTVLTYLVDMRRFSYPERPIIFLSGCYTAVAVAYIAGFLLEDRVVCNDKFAEDGARTVAQGTKKEGCTILFMMLYFFSMASSIWWVILSLTWFLAAGMKWGHEAIEANSQYFHLAAWAVPAIKTITILALGQVDGDVLSGVCFVGLNNVDALRGFVLAPLFVYLFIGTSFLLAGFVSLFRIRTIMKHDGTKTEKLEKLMVRIGVFSVLYTVPATIVIACYFYEQAFRDQWERSWVAQSCKSYAIPCPHLQGGGGVPPHPPMSPDFTVFMIKYLMTLIVGITSGFWIWSGKTLNSWRKFYTRLTNSKQGETTV | ||||||
Disulfide bond | 111↔172 | |||||
Sequence: CQPISIPLCTDIAYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSAELKFFLCSMYAPVC | ||||||
Disulfide bond | 119↔165 | |||||
Sequence: CTDIAYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSAELKFFLC | ||||||
Glycosylation | 125 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 156↔192 | |||||
Sequence: CSAELKFFLCSMYAPVCTVLEQALPPCRSLCERAQGC | ||||||
Disulfide bond | 182↔221 | |||||
Sequence: CRSLCERAQGCEALMNKFGFQWPDTLKCEKFPVHGAGELC | ||||||
Disulfide bond | 186↔209 | |||||
Sequence: CERAQGCEALMNKFGFQWPDTLKC | ||||||
Glycosylation | 225 | 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
Tissue specificity
Widely expressed. Most abundant in kidney, liver, uterus, ovary and heart. Lower levels seen in brain and intestine. Extremely low in calvaria, mammary glands and testis.
Developmental stage
Expressed predominantly in neonatal tissues, at lower levels in adult.
Interaction
Subunit
Interacts with MYOC (By similarity).
Interacts with WNT7B (By similarity).
Interacts with WNT7B (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q08463 | Fzd1 Q08463 | 4 | EBI-8766455, EBI-8766455 | |
BINARY | Q08463 | Fzd2 Q08464 | 6 | EBI-8766455, EBI-7402050 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 74-99 | Disordered | ||||
Sequence: AGQVSGPGQQRPPPPQPQQGGQQYNG | ||||||
Domain | 106-224 | FZ | ||||
Sequence: PDHGYCQPISIPLCTDIAYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSAELKFFLCSMYAPVCTVLEQALPPCRSLCERAQGCEALMNKFGFQWPDTLKCEKFPVHGAGELCVGQ | ||||||
Motif | 619-624 | Lys-Thr-X-X-X-Trp motif, mediates interaction with the PDZ domain of Dvl family members | ||||
Sequence: KTLNSW | ||||||
Motif | 639-641 | 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.
- Length641
- Mass (Da)71,027
- Last updated1996-11-01 v1
- ChecksumD82E2C113E81B8B6
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I6ACQ8 | A0A8I6ACQ8_RAT | Fzd1 | 555 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L02529 EMBL· GenBank· DDBJ | AAA41173.1 EMBL· GenBank· DDBJ | mRNA |