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Q08463 (FZD1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Frizzled-1

Short name=Fz-1
Short name=rFz1
Gene names
Name:Fzd1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length641 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. 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. Activation by Wnt8 induces expression of beta-catenin target genes.

Subunit structure

Interacts with MYOC By similarity.

Subcellular location

Membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein By similarity.

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.

Domain

Lys-Thr-X-X-X-Trp motif interacts with the PDZ doman of Dvl (Disheveled) family members and is involved in the activation of the Wnt/beta-catenin signaling pathway By similarity.

The FZ domain is involved in binding with Wnt ligands By similarity.

Post-translational modification

Ubiquitinated by ZNRF3, leading to its degradation by the proteasome By similarity.

Sequence similarities

Belongs to the G-protein coupled receptor Fz/Smo family.

Contains 1 FZ (frizzled) domain.

Ontologies

Keywords
   Biological processWnt signaling pathway
   Cellular componentCell membrane
Membrane
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionDevelopmental protein
G-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway coupled to cGMP nucleotide second messenger

Inferred from Biological aspect of Ancestor. Source: RefGenome

Wnt signaling pathway

Inferred from direct assay PubMed 10559239. Source: RGD

Wnt signaling pathway, calcium modulating pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

axonogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

brain development

Inferred from Biological aspect of Ancestor. Source: RefGenome

canonical Wnt signaling pathway

Inferred from direct assay PubMed 14688793PubMed 18945944. Source: BHF-UCL

cellular response to growth factor stimulus

Inferred from expression pattern Ref.1. Source: RGD

cellular response to peptide hormone stimulus

Inferred from expression pattern Ref.1PubMed 15962290. Source: RGD

cellular response to vitamin D

Inferred from expression pattern Ref.1. Source: RGD

epithelial cell differentiation

Inferred from Biological aspect of Ancestor. Source: RefGenome

gonad development

Inferred from Biological aspect of Ancestor. Source: RefGenome

lung alveolus development

Inferred from expression pattern PubMed 17911382. Source: RGD

negative regulation of BMP signaling pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of canonical Wnt signaling pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 14688793PubMed 18945944. Source: BHF-UCL

regulation of osteoblast differentiation

Inferred from expression pattern Ref.1. Source: RGD

vasculature development

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentapical part of cell

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytoplasm

Inferred from Biological aspect of Ancestor. Source: RefGenome

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

neuron projection

Inferred from direct assay PubMed 19883499. Source: RGD

neuron projection membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

plasma membrane

Inferred from direct assay PubMed 14688793. Source: BHF-UCL

   Molecular_functionG-protein coupled receptor activity

Inferred from electronic annotation. Source: UniProtKB-KW

PDZ domain binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

Wnt-activated receptor activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Wnt-protein binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

identical protein binding

Inferred from physical interaction PubMed 14688793. Source: IntAct

protein binding

Inferred from physical interaction PubMed 14688793. Source: IntAct

protein heterodimerization activity

Inferred from physical interaction PubMed 14688793. Source: BHF-UCL

protein homodimerization activity

Inferred from physical interaction PubMed 14688793. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself4EBI-8766455,EBI-8766455
Fzd2Q084646EBI-8766455,EBI-7402050

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 6868 Potential
Chain69 – 641573Frizzled-1
PRO_0000012975

Regions

Topological domain69 – 316248Extracellular Potential
Transmembrane317 – 33721Helical; Name=1; Potential
Topological domain338 – 34811Cytoplasmic Potential
Transmembrane349 – 36921Helical; Name=2; Potential
Topological domain370 – 39627Extracellular Potential
Transmembrane397 – 41721Helical; Name=3; Potential
Topological domain418 – 43922Cytoplasmic Potential
Transmembrane440 – 46021Helical; Name=4; Potential
Topological domain461 – 48323Extracellular Potential
Transmembrane484 – 50421Helical; Name=5; Potential
Topological domain505 – 53026Cytoplasmic Potential
Transmembrane531 – 55121Helical; Name=6; Potential
Topological domain552 – 59544Extracellular Potential
Transmembrane596 – 61621Helical; Name=7; Potential
Topological domain617 – 64125Cytoplasmic Potential
Domain106 – 224119FZ
Motif619 – 6246Lys-Thr-X-X-X-Trp motif, mediates interaction with the PDZ domain of Dvl family members By similarity
Motif639 – 6413PDZ-binding
Compositional bias85 – 906Poly-Pro

Amino acid modifications

Glycosylation1251N-linked (GlcNAc...) Potential
Glycosylation2251N-linked (GlcNAc...) Potential
Disulfide bond111 ↔ 172 By similarity
Disulfide bond119 ↔ 165 By similarity
Disulfide bond156 ↔ 192 By similarity
Disulfide bond182 ↔ 221 By similarity
Disulfide bond186 ↔ 209 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q08463 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: D82E2C113E81B8B6

FASTA64171,027
        10         20         30         40         50         60 
MAEEAVPSES RAAGRPSLEL CAVALPGRRE EVGHQDTAGH RRPRAHSRCW ARGLLLLLWL 

        70         80         90        100        110        120 
LEAPLLLGVR AQPAGQVSGP GQQRPPPPQP QQGGQQYNGE RGISIPDHGY CQPISIPLCT 

       130        140        150        160        170        180 
DIAYNQTIMP NLLGHTNQED AGLEVHQFYP LVKVQCSAEL KFFLCSMYAP VCTVLEQALP 

       190        200        210        220        230        240 
PCRSLCERAQ GCEALMNKFG FQWPDTLKCE KFPVHGAGEL CVGQNTSDKG TPTPSLLPEF 

       250        260        270        280        290        300 
WTSNPQHGGG GYRGGYPGGA GPVERGKFSC PRALRVPSYL NYHFLGEKDC GAPCEPTKVY 

       310        320        330        340        350        360 
GLMYFGPEEL RFSRTWIGIW SVLCCASTLF TVLTYLVDMR RFSYPERPII FLSGCYTAVA 

       370        380        390        400        410        420 
VAYIAGFLLE DRVVCNDKFA EDGARTVAQG TKKEGCTILF MMLYFFSMAS SIWWVILSLT 

       430        440        450        460        470        480 
WFLAAGMKWG HEAIEANSQY FHLAAWAVPA IKTITILALG QVDGDVLSGV CFVGLNNVDA 

       490        500        510        520        530        540 
LRGFVLAPLF VYLFIGTSFL LAGFVSLFRI RTIMKHDGTK TEKLEKLMVR IGVFSVLYTV 

       550        560        570        580        590        600 
PATIVIACYF YEQAFRDQWE RSWVAQSCKS YAIPCPHLQG GGGVPPHPPM SPDFTVFMIK 

       610        620        630        640 
YLMTLIVGIT SGFWIWSGKT LNSWRKFYTR LTNSKQGETT V 

« Hide

References

[1]"Two homologs of the Drosophila polarity gene frizzled (fz) are widely expressed in mammalian tissues."
Chan S.D.H., Karpf D.B., Fowlkes M.E., Hooks M., Bradley M.S., Vuong V., Bambino T., Liu M.Y.C., Arnaud C.D., Strewler G.J., Nissenson R.A.
J. Biol. Chem. 267:25202-25207(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Osteosarcoma.
[2]"Protein kinase C is differentially stimulated by Wnt and Frizzled homologs in a G-protein-dependent manner."
Sheldahl L.C., Park M., Malbon C.C., Moon R.T.
Curr. Biol. 9:695-698(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: COUPLING TO BETA-CATENIN PATHWAY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L02529 mRNA. Translation: AAA41173.1.
PIRA45054.
UniGeneRn.6575.

3D structure databases

ProteinModelPortalQ08463.
SMRQ08463. Positions 109-225.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ08463. 1 interaction.
STRING10116.ENSRNOP00000021979.

Chemistry

GuidetoPHARMACOLOGY229.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteQ08463.

Proteomic databases

PaxDbQ08463.
PRIDEQ08463.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:61916. rat.

Organism-specific databases

RGD61916. Fzd1.

Phylogenomic databases

eggNOGNOG257258.
HOGENOMHOG000233236.
HOVERGENHBG006977.
InParanoidQ08463.
PhylomeDBQ08463.

Gene expression databases

GenevestigatorQ08463.

Family and domain databases

Gene3D1.10.2000.10. 1 hit.
InterProIPR000539. Frizzled.
IPR015526. Frizzled/SFRP.
IPR020067. Frizzled_dom.
IPR026548. FZD1.
IPR017981. GPCR_2-like.
[Graphical view]
PANTHERPTHR11309. PTHR11309. 1 hit.
PTHR11309:SF81. PTHR11309:SF81. 1 hit.
PfamPF01534. Frizzled. 1 hit.
PF01392. Fz. 1 hit.
[Graphical view]
PRINTSPR00489. FRIZZLED.
SMARTSM00063. FRI. 1 hit.
[Graphical view]
SUPFAMSSF63501. SSF63501. 1 hit.
PROSITEPS50038. FZ. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ08463.

Entry information

Entry nameFZD1_RAT
AccessionPrimary (citable) accession number: Q08463
Entry history
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries