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O70421 (FZD1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Frizzled-1

Short name=Fz-1
Short name=mFz1
Gene names
Name:Fzd1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length642 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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.

Subunit structure

Interacts with MYOC By similarity.

Subcellular location

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

Tissue specificity

Expressed in chondrocytes.

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 genetic interaction PubMed 15923619. Source: MGI

Wnt signaling pathway, calcium modulating pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

autocrine signaling

Inferred from electronic annotation. Source: Ensembl

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 mutant phenotype PubMed 15143170. Source: MGI

canonical Wnt signaling pathway involved in mesenchymal stem cell differentiation

Inferred from electronic annotation. Source: Ensembl

canonical Wnt signaling pathway involved in osteoblast differentiation

Inferred from electronic annotation. Source: Ensembl

cell-cell signaling

Inferred from direct assay PubMed 15809042. Source: MGI

epithelial cell differentiation

Inferred from direct assay PubMed 15809042. Source: MGI

gonad development

Inferred from Biological aspect of Ancestor. Source: RefGenome

hard palate development

Inferred from genetic interaction PubMed 20940229. Source: MGI

lung alveolus development

Inferred from Biological aspect of Ancestor. Source: RefGenome

membranous septum morphogenesis

Inferred from genetic interaction PubMed 20940229. Source: MGI

muscular septum morphogenesis

Inferred from genetic interaction PubMed 20940229. Source: MGI

negative regulation of BMP signaling pathway

Inferred from direct assay PubMed 14627707. Source: MGI

negative regulation of canonical Wnt signaling pathway

Inferred from direct assay PubMed 14662765. Source: MGI

negative regulation of catenin import into nucleus

Inferred from direct assay PubMed 14627707. Source: MGI

negative regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 16936075. Source: MGI

outflow tract morphogenesis

Inferred from genetic interaction PubMed 20940229. Source: MGI

planar cell polarity pathway involved in neural tube closure

Inferred from genetic interaction PubMed 20940229. Source: MGI

positive regulation of protein phosphorylation

Inferred from mutant phenotype PubMed 15143170. Source: MGI

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

regulation of transcription from RNA polymerase II promoter

Inferred from Biological aspect of Ancestor. Source: RefGenome

response to drug

Inferred from electronic annotation. Source: Ensembl

vasculature development

Inferred from Biological aspect of Ancestor. Source: RefGenome

ventricular septum morphogenesis

Inferred from genetic interaction PubMed 20940229. Source: MGI

   Cellular_componentapical part of cell

Inferred from Biological aspect of Ancestor. Source: RefGenome

cell surface

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from Biological aspect of Ancestor. Source: RefGenome

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

neuron projection membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

   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 physical interaction PubMed 15923619. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 6868 Potential
Chain69 – 642574Frizzled-1
PRO_0000012974

Regions

Topological domain69 – 317249Extracellular Potential
Transmembrane318 – 33821Helical; Name=1; Potential
Topological domain339 – 34911Cytoplasmic Potential
Transmembrane350 – 37021Helical; Name=2; Potential
Topological domain371 – 39727Extracellular Potential
Transmembrane398 – 41821Helical; Name=3; Potential
Topological domain419 – 44022Cytoplasmic Potential
Transmembrane441 – 46121Helical; Name=4; Potential
Topological domain462 – 48423Extracellular Potential
Transmembrane485 – 50521Helical; Name=5; Potential
Topological domain506 – 53126Cytoplasmic Potential
Transmembrane532 – 55221Helical; Name=6; Potential
Topological domain553 – 59341Extracellular Potential
Transmembrane594 – 61421Helical; Name=7; Potential
Topological domain615 – 64228Cytoplasmic Potential
Domain106 – 225120FZ
Motif620 – 6256Lys-Thr-X-X-X-Trp motif, mediates interaction with the PDZ domain of Dvl family members By similarity
Motif640 – 6423PDZ-binding
Compositional bias85 – 906Poly-Pro

Amino acid modifications

Glycosylation1251N-linked (GlcNAc...) Potential
Glycosylation2261N-linked (GlcNAc...) Potential
Disulfide bond111 ↔ 172 By similarity
Disulfide bond119 ↔ 165 By similarity
Disulfide bond156 ↔ 193 By similarity
Disulfide bond182 ↔ 222 By similarity
Disulfide bond186 ↔ 210 By similarity

Experimental info

Sequence conflict1221I → M in AAC12873. Ref.1
Sequence conflict2461P → G in AAC12873. Ref.1
Sequence conflict3411R → P in AAC12873. Ref.1
Sequence conflict3521F → S in AAC12873. Ref.1
Sequence conflict3931K → N in AAC12873. Ref.1
Sequence conflict4741V → L in AAC12873. Ref.1
Sequence conflict6151W → R in AAC12873. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O70421 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 7674583F819014E2

FASTA64271,127
        10         20         30         40         50         60 
MAEEAAPSES RAAGRLSLEL CAEALPGRRE EVGHEDTASH RRPRADPRRW ASGLLLLLWL 

        70         80         90        100        110        120 
LEAPLLLGVR AQAAGQVSGP GQQAPPPPQP QQSGQQYNGE RGISIPDHGY CQPISIPLCT 

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

       190        200        210        220        230        240 
PCRSLCERAR QGCEALMNKF GFQWPDTLKC EKFPVHGAGE LCVGQNTSDK GTPTPSLLPE 

       250        260        270        280        290        300 
FWTSNPQHGG GGYRGGYPGG AGTVERGKFS CPRALRVPSY LNYHFLGEKD CGAPCEPTKV 

       310        320        330        340        350        360 
YGLMYFGPEE LRFSRTWIGI WSVLCCASTL FTVLTYLVDM RRFSYPERPI IFLSGCYTAV 

       370        380        390        400        410        420 
AVAYIAGFLL EDRVVCNDKF AEDGARTVAQ GTKKEGCTIL FMMLYFFSMA SSIWWVILSL 

       430        440        450        460        470        480 
TWFLAAGMKW GHEAIEANSQ YFHLAAWAVP AIKTITILAL GQVDGDVLSG VCFVGLNNVD 

       490        500        510        520        530        540 
ALRGFVLAPL FVYLFIGTSF LLAGFVSLFR IRTIMKHDGT KTEKLEKLMV RIGVFSVLYT 

       550        560        570        580        590        600 
VPATIVIACY FYEQAFRDQW ERSWVAQSCK SYAIPCPHLQ GGGGVPPHPP MSPDFTVFMI 

       610        620        630        640 
KYLMTLIVGI TSGFWIWSGK TLNSWRKFYT RLTNSKQGET TV 

« Hide

References

« Hide 'large scale' references
[1]"Expression of frizzled genes in mouse costochondral chondrocytes."
Xu L., Tan L., Goldring M.B., Olsen B.R., Li Y.
Matrix Biol. 20:147-151(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
Tissue: Embryo.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Eye.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
[5]Johnson M.A., Greenberg N.M.
Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 302-376.
Tissue: Prostate.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF054623 mRNA. Translation: AAC12873.2.
AK143101 mRNA. Translation: BAE25269.1.
CH466600 Genomic DNA. Translation: EDL14633.1.
BC053010 mRNA. Translation: AAH53010.1.
AF005202 mRNA. Translation: AAC01952.1.
CCDSCCDS19072.1.
RefSeqNP_067432.2. NM_021457.3.
UniGeneMm.246003.

3D structure databases

ProteinModelPortalO70421.
SMRO70421. Positions 111-217, 291-633.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199775. 3 interactions.
IntActO70421. 4 interactions.
MINTMINT-1779162.
STRING10090.ENSMUSP00000058629.

Chemistry

GuidetoPHARMACOLOGY229.

Protein family/group databases

MEROPSI93.001.
GPCRDBSearch...

PTM databases

PhosphoSiteO70421.

Proteomic databases

PRIDEO70421.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000054294; ENSMUSP00000058629; ENSMUSG00000044674.
GeneID14362.
KEGGmmu:14362.
UCSCuc008wig.2. mouse.

Organism-specific databases

CTD8321.
MGIMGI:1196625. Fzd1.

Phylogenomic databases

eggNOGNOG257258.
GeneTreeENSGT00740000114899.
HOGENOMHOG000233236.
HOVERGENHBG006977.
InParanoidQ7TS82.
KOK02432.
OMAHGAGELC.
OrthoDBEOG7M3J01.
TreeFamTF317907.

Gene expression databases

BgeeO70421.
CleanExMM_FZD1.
GenevestigatorO70421.

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

NextBio285827.
PROO70421.
SOURCESearch...

Entry information

Entry nameFZD1_MOUSE
AccessionPrimary (citable) accession number: O70421
Secondary accession number(s): O08974, Q7TS82
Entry history
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 122 of the entry and version 3 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries