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Q9EQD0 (FZD5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Frizzled-5

Short name=Fz-5
Short name=mFz5
Gene names
Name:Fzd5
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length585 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. Plays a role in yolk sac angiogenesis and in placental vascularization. Binds to Wnt2, Wnt10B, Wnt5A, but not to Wnt2B or Wnt4.

Subunit structure

Interacts with GOPC. Ref.8

Subcellular location

Cell membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein. Note: Localized at the plasma membrane and also found at the Golgi. Ref.8

Tissue specificity

Expressed in eye, kidney, lung, chondrocytes, epithelial cells of the small intestine and gobelet cells of the colon. Ref.7

Developmental stage

Expressed in the yolk sac, placenta, eye and lung bud at 9.5 dpc. At 10.5 dpc, also expressed in the placental blood vessel of embryonic origin.

Domain

The PDZ-binding motif mediates interaction with GOPC By similarity.

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

Post-translational modification

Ubiquitinated by RNF43 and 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.

Sequence caution

The sequence AAG39355.1 differs from that shown. Reason: Frameshift at several positions.

Ontologies

Keywords
   Biological processAngiogenesis
Differentiation
Wnt signaling pathway
   Cellular componentCell membrane
Golgi apparatus
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_processSpemann organizer formation

Inferred from electronic annotation. Source: Ensembl

T cell differentiation in thymus

Inferred from mutant phenotype PubMed 11265645. Source: MGI

Wnt signaling pathway

Inferred from genetic interaction Ref.1. Source: MGI

Wnt signaling pathway involved in dorsal/ventral axis specification

Inferred from electronic annotation. Source: Ensembl

angiogenesis

Inferred from mutant phenotype Ref.1. Source: MGI

anterior/posterior axis specification, embryo

Inferred from electronic annotation. Source: Ensembl

apoptotic process involved in morphogenesis

Inferred from mutant phenotype PubMed 18791178. Source: MGI

axonogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

brain development

Inferred from Biological aspect of Ancestor. Source: RefGenome

branching involved in labyrinthine layer morphogenesis

Inferred from mutant phenotype PubMed 23610556. Source: MGI

canonical Wnt signaling pathway

Inferred from mutant phenotype PubMed 11265645. Source: MGI

cell maturation

Inferred from mutant phenotype PubMed 15778706. Source: MGI

cellular response to molecule of bacterial origin

Inferred from electronic annotation. Source: Ensembl

chorionic trophoblast cell differentiation

Inferred from mutant phenotype PubMed 23610556. Source: MGI

embryonic camera-type eye development

Inferred from mutant phenotype PubMed 18791178. Source: MGI

gonad development

Inferred from Biological aspect of Ancestor. Source: RefGenome

labyrinthine layer blood vessel development

Inferred from mutant phenotype Ref.1. Source: MGI

negative regulation of cell proliferation

Inferred from mutant phenotype PubMed 18791178. Source: MGI

positive regulation of JUN kinase activity

Inferred from direct assay PubMed 15195140. Source: MGI

positive regulation of interferon-gamma production

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 23610556. Source: MGI

post-embryonic camera-type eye development

Inferred from mutant phenotype PubMed 18791178. Source: MGI

regulation of canonical Wnt signaling pathway

Inferred from mutant phenotype PubMed 23610556. Source: MGI

regulation of chorionic trophoblast cell proliferation

Inferred from mutant phenotype PubMed 23610556. Source: MGI

regulation of tight junction assembly

Inferred from mutant phenotype PubMed 23610556. Source: MGI

regulation of transcription from RNA polymerase II promoter

Inferred from Biological aspect of Ancestor. Source: RefGenome

syncytiotrophoblast cell differentiation involved in labyrinthine layer development

Inferred from mutant phenotype PubMed 23610556. Source: MGI

vasculature development

Inferred from mutant phenotype PubMed 18791178. Source: MGI

   Cellular_componentGolgi apparatus

Inferred from direct assay Ref.8. Source: BHF-UCL

Golgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell projection

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

perinuclear region of cytoplasm

Inferred from direct assay Ref.8. Source: BHF-UCL

plasma membrane

Inferred from direct assay Ref.8PubMed 16890161. Source: BHF-UCL

tight junction

Inferred from direct assay PubMed 23610556. Source: MGI

   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 18606138. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GopcQ8BH603EBI-7938232,EBI-296357

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 585559Frizzled-5
PRO_0000243936

Regions

Topological domain27 – 238212Extracellular Potential
Transmembrane239 – 25921Helical; Name=1; Potential
Topological domain260 – 27011Cytoplasmic Potential
Transmembrane271 – 29121Helical; Name=2; Potential
Topological domain292 – 31524Extracellular Potential
Transmembrane316 – 33621Helical; Name=3; Potential
Topological domain337 – 35822Cytoplasmic Potential
Transmembrane359 – 37921Helical; Name=4; Potential
Topological domain380 – 40223Extracellular Potential
Transmembrane403 – 42321Helical; Name=5; Potential
Topological domain424 – 44926Cytoplasmic Potential
Transmembrane450 – 47021Helical; Name=6; Potential
Topological domain471 – 50030Extracellular Potential
Transmembrane501 – 52121Helical; Name=7; Potential
Topological domain522 – 58564Cytoplasmic Potential
Domain28 – 150123FZ
Motif582 – 5843PDZ-binding By similarity

Amino acid modifications

Glycosylation471N-linked (GlcNAc...) Potential
Glycosylation1511N-linked (GlcNAc...) Potential
Disulfide bond33 ↔ 94 By similarity
Disulfide bond41 ↔ 87 By similarity
Disulfide bond78 ↔ 116 By similarity
Disulfide bond105 ↔ 147 By similarity
Disulfide bond109 ↔ 133 By similarity

Experimental info

Sequence conflict41P → T in BAC26789. Ref.3
Sequence conflict123 – 1242YG → S in BAC53981. Ref.2
Sequence conflict4021G → S in AAG39355. Ref.1
Sequence conflict4191L → H in BAC53981. Ref.2
Sequence conflict4441E → G in BAC53981. Ref.2
Sequence conflict4771S → T in AAG39355. Ref.1
Sequence conflict4811A → P in AAG39355. Ref.1
Sequence conflict4891P → T in AAG39355. Ref.1
Sequence conflict5211I → F in BAC53981. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9EQD0 [UniParc].

Last modified October 3, 2012. Version 3.
Checksum: 5FC03620AF087733

FASTA58564,138
        10         20         30         40         50         60 
MARPDPSAPP SLLLLLLAQL VGRAAAASKA PVCQEITVPM CRGIGYNLTH MPNQFNHDTQ 

        70         80         90        100        110        120 
DEAGLEVHQF WPLVEIHCSP DLRFFLCSMY TPICLPDYHK PLPPCRSVCE RAKAGCSPLM 

       130        140        150        160        170        180 
RQYGFAWPER MSCDRLPVLG GDAEVLCMDY NRSEATTASP KSFPAKPTLP GPPGAPSSGG 

       190        200        210        220        230        240 
ECPSGGPSVC TCREPFVPIL KESHPLYNKV RTGQVPNCAV PCYQPSFSPD ERTFATFWIG 

       250        260        270        280        290        300 
LWSVLCFIST STTVATFLID MERFRYPERP IIFLSACYLC VSLGFLVRLV VGHASVACSR 

       310        320        330        340        350        360 
EHSHIHYETT GPALCTVVFL LVYFFGMASS IWWVILSLTW FLAAGMKWGN EAIAGYAQYF 

       370        380        390        400        410        420 
HLAAWLIPSV KSITALALSS VDGDPVAGIC YVGNQNLNSL RGFVLGPLVL YLLVGTLFLL 

       430        440        450        460        470        480 
AGFVSLFRIR SVIKQGGTKT DKLEKLMIRI GIFTLLYTVP ASIVVACYLY EQHYRESWEA 

       490        500        510        520        530        540 
ALTCACPGPD AGQPRAKPEY WVLMLKYFMC LVVGITSGVW IWSGKTLESW RRFTSRCCCS 

       550        560        570        580 
SRRGHKSGGA MAAGDYAEAS AALTGRTGPP GPTAAYHKQV SLSHV 

« Hide

References

« Hide 'large scale' references
[1]"Mouse Wnt receptor gene Fzd5 is essential for yolk sac and placental angiogenesis."
Ishikawa T., Tamai Y., Zorn A.M., Yoshida H., Seldin M.F., Nishikawa S., Taketo M.M.
Development 128:25-33(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6N.
Tissue: Intestine.
[2]"Molecular cloning and characterization of a gene encoding for rat Frizzled 5."
Ito S., Imamura T., Shiota K.
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"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: Testis.
[4]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[5]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].
[6]Johnson M.A., Greenberg N.M.
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 211-300.
Strain: C57BL/6.
Tissue: Prostate.
[7]"A large family of putative transmembrane receptors homologous to the product of the Drosophila tissue polarity gene frizzled."
Wang Y., Macke J.P., Abella B.S., Andreasson K., Worley P., Gilbert D.J., Copeland N.G., Jenkins N.A., Nathans J.
J. Biol. Chem. 271:4468-4476(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[8]"Identification of a PDZ domain containing Golgi protein, GOPC, as an interaction partner of frizzled."
Yao R., Maeda T., Takada S., Noda T.
Biochem. Biophys. Res. Commun. 286:771-778(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GOPC, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF272146 mRNA. Translation: AAG39355.1. Frameshift.
AB052910 mRNA. Translation: BAC53981.1.
AK030111 mRNA. Translation: BAC26789.1.
AC101915 Genomic DNA. No translation available.
CH466548 Genomic DNA. Translation: EDL00208.1.
CH466548 Genomic DNA. Translation: EDL00209.1.
AF005203 mRNA. Translation: AAC01953.1.
RefSeqNP_001036124.1. NM_001042659.1.
NP_073558.2. NM_022721.3.
UniGeneMm.150813.
Mm.470210.

3D structure databases

ProteinModelPortalQ9EQD0.
SMRQ9EQD0. Positions 33-149, 197-532.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199778. 1 interaction.
DIPDIP-41260N.
IntActQ9EQD0. 4 interactions.
MINTMINT-1783095.
STRING10090.ENSMUSP00000067783.

Protein family/group databases

MEROPSI93.001.
GPCRDBSearch...

PTM databases

PhosphoSiteQ9EQD0.

Proteomic databases

PRIDEQ9EQD0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000063982; ENSMUSP00000067783; ENSMUSG00000045005.
ENSMUST00000116133; ENSMUSP00000111828; ENSMUSG00000045005.
GeneID14367.
KEGGmmu:14367.
UCSCuc007bgy.1. mouse.

Organism-specific databases

CTD7855.
MGIMGI:108571. Fzd5.

Phylogenomic databases

eggNOGNOG257258.
GeneTreeENSGT00750000117488.
HOGENOMHOG000233236.
HOVERGENHBG006977.
InParanoidQ9EQD0.
KOK02375.
OMAAATYHKQ.
OrthoDBEOG7M3J01.
TreeFamTF317907.

Gene expression databases

CleanExMM_FZD5.
GenevestigatorQ9EQD0.

Family and domain databases

Gene3D1.10.2000.10. 1 hit.
InterProIPR000539. Frizzled.
IPR015526. Frizzled/SFRP.
IPR020067. Frizzled_dom.
IPR026547. FZD5/FZD8.
IPR017981. GPCR_2-like.
[Graphical view]
PANTHERPTHR11309. PTHR11309. 1 hit.
PTHR11309:SF29. PTHR11309:SF29. 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

NextBio285839.
PROQ9EQD0.
SOURCESearch...

Entry information

Entry nameFZD5_MOUSE
AccessionPrimary (citable) accession number: Q9EQD0
Secondary accession number(s): G5E8F0 expand/collapse secondary AC list , O08975, Q8BMR2, Q8CHK9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: October 3, 2012
Last modified: April 16, 2014
This is version 120 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