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Q9R216 (FZD9_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. 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-9

Short name=Fz-9
Short name=mFz3
Short name=mFz9
Alternative name(s):
CD_antigen=CD349
Gene names
Name:Fzd9
Synonyms:Fzd3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length592 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.

Subcellular location

Cell membrane; Multi-pass membrane protein.

Tissue specificity

In the embryo, found in the neural tube, trunk skeletal muscle precursors (myotomes), limb skeletal anlagen, craniofacial regions and nephric ducts. In the adult, expression is abundant in heart, brain, testis and skeletal muscle. In the testis, expressed in all spermatogenic cell types. Lower levels in adult lung, liver and kidney. Barely detectable in spleen. Expressed also in chondrocytes.

Developmental stage

Not detected at embryonic day 7 (E7), weakly at E11 and strongly at E15 and E17. Expression covers the entire neural tube at 9.5 dpc, decreases at 10.5 dpc and becomes detectable only in the lumbar to tail regions at 11.5 dpc. In the somites, expression begins at 10.5 dpc to become up-regulated all along the rostrocaudal trunk axis at 11.5 dpc. In craniofacial territories, expression is first detected at 11.5 dpc in restricted areas of the nose, the maxillar mandibular and second branchial arch anlagen. At 11.5 dpc, predominantly expressed in restricted areas of the nose, dorsally to the eye and in the caudal pharyngeal region. Ref.1

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.

Caution

Has been first described as FZD3 in literature.

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_processB cell differentiation

Inferred from mutant phenotype PubMed 15572594. Source: MGI

brain development

Inferred from Biological aspect of Ancestor. Source: RefGenome

canonical Wnt signaling pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

embryo development

Inferred from Biological aspect of Ancestor. Source: RefGenome

gonad development

Inferred from Biological aspect of Ancestor. Source: RefGenome

learning or memory

Inferred from mutant phenotype PubMed 15930120. Source: MGI

neuroblast proliferation

Inferred from mutant phenotype PubMed 15930120. Source: MGI

regulation of transcription from RNA polymerase II promoter

Inferred from Biological aspect of Ancestor. Source: RefGenome

vasculature development

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentcell surface

Inferred from electronic annotation. Source: Ensembl

filopodium membrane

Inferred from direct assay Ref.1. Source: MGI

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

perinuclear region of cytoplasm

Inferred from direct assay Ref.1. Source: MGI

plasma membrane

Inferred from direct assay Ref.1. 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 Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 592569Frizzled-9
PRO_0000013004

Regions

Topological domain24 – 230207Extracellular
Transmembrane231 – 25121Helical; Name=1; Potential
Topological domain252 – 26716Cytoplasmic Potential
Transmembrane268 – 28821Helical; Name=2; Potential
Topological domain289 – 31628Extracellular Potential
Transmembrane317 – 33721Helical; Name=3; Potential
Topological domain338 – 35619Cytoplasmic Potential
Transmembrane357 – 37721Helical; Name=4; Potential
Topological domain378 – 40124Extracellular Potential
Transmembrane402 – 42221Helical; Name=5; Potential
Topological domain423 – 44826Cytoplasmic Potential
Transmembrane449 – 46921Helical; Name=6; Potential
Topological domain470 – 50940Extracellular Potential
Transmembrane510 – 53021Helical; Name=7; Potential
Topological domain531 – 59262Cytoplasmic Potential
Domain35 – 156122FZ
Motif533 – 5386Lys-Thr-X-X-X-Trp motif, mediates interaction with the PDZ domain of Dvl family members By similarity

Amino acid modifications

Glycosylation541N-linked (GlcNAc...) Potential
Glycosylation1591N-linked (GlcNAc...) Potential
Disulfide bond40 ↔ 101 By similarity
Disulfide bond48 ↔ 94 By similarity
Disulfide bond85 ↔ 123 By similarity
Disulfide bond112 ↔ 153 By similarity
Disulfide bond116 ↔ 140 By similarity

Experimental info

Sequence conflict661S → P in AAB87503. Ref.3
Sequence conflict73 – 742QL → HC in BAB32311. Ref.2
Sequence conflict931L → F in BAB32311. Ref.2
Sequence conflict1441P → S in CAB44237. Ref.4
Sequence conflict2211E → K in CAB44237. Ref.4
Sequence conflict2371A → P in CAB44237. Ref.4
Sequence conflict3081G → D in AAB87503. Ref.3
Sequence conflict3741V → F in CAB44237. Ref.4
Sequence conflict5921L → P in BAB32311. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9R216 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 21B2D4F8CE232965

FASTA59264,995
        10         20         30         40         50         60 
MAVPPLLRGA LLLWQLLATG GAALEIGRFD PERGRGPAPC QAMEIPMCRG IGYNLTRMPN 

        70         80         90        100        110        120 
LLGHTSQGEA AAQLAEFSPL VQYGCHSHLR FFLCSLYAPM CTDQVSTPIP ACRPMCEQAR 

       130        140        150        160        170        180 
LRCAPIMEQF NFGWPDSLDC ARLPTRNDPH ALCMEAPENA TAGPTEPHKG LGMLPVAPRP 

       190        200        210        220        230        240 
ARPPGDSAPG PGSGGTCDNP EKFQYVEKSR SCAPRCGPGV EVFWSRRDKD FALVWMAVWS 

       250        260        270        280        290        300 
ALCFFSTAFT VFTFLLEPHR FQYPERPIIF LSMCYNVYSL AFLIRAVAGA QSVACDQEAG 

       310        320        330        340        350        360 
ALYVIQEGLE NTGCTLVFLL LYYFGMASSL WWVVLTLTWF LAAGKKWGHE AIEAHGSYFH 

       370        380        390        400        410        420 
MAAWGLPALK TIVVLTLRKV AGDELTGLCY VASMDPAALT GFVLVPLSCY LVLGTSFLLT 

       430        440        450        460        470        480 
GFVALFHIRK IMKTGGTNTE KLEKLMVKIG VFSILYTVPA TCVIVCYVYE RLNMDFWRLR 

       490        500        510        520        530        540 
ATEQPCTAAT VPGGRRDCSL PGGSVPTVAV FMLKIFMSLV VGITSGVWVW SSKTFQTWQS 

       550        560        570        580        590 
LCYRKMAAGR ARAKACRTPG GYGRGTHCHY KAPTVVLHMT KTDPSLENPT HL 

« Hide

References

« Hide 'large scale' references
[1]"Characterization and expression pattern of the frizzled gene Fzd9, the mouse homolog of FZD9 which is deleted in Williams-Beuren syndrome."
Wang Y.-K., Spoerle R., Paperna T., Schughart K., Francke U.
Genomics 57:235-248(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DEVELOPMENTAL STAGE.
Strain: 129/SvJ.
Tissue: Brain.
[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: Embryonic head.
[3]"A novel mouse frizzled gene expressed in early neural development."
Van Raay T.J., Rasmussen J.T., Rao M.S.
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 44-592.
[4]"Localization of the mouse frizzled gene mFZD3 in the olfactory epithelium and in the vomeronasal organ."
Calo L., Mimmack M.L., Keverne E.B., Emson P.C.
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 144-592.
Strain: BALB/c.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF088850 Genomic DNA. Translation: AAD27789.1.
AK021164 mRNA. Translation: BAB32311.1.
AF033585 mRNA. Translation: AAB87503.2.
Y17709 mRNA. Translation: CAB44237.1.
RefSeqNP_034376.1. NM_010246.1.
UniGeneMm.6256.

3D structure databases

ProteinModelPortalQ9R216.
SMRQ9R216. Positions 40-156.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000053551.

Protein family/group databases

MEROPSI93.001.
GPCRDBSearch...

PTM databases

PhosphoSiteQ9R216.

Proteomic databases

PRIDEQ9R216.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000062572; ENSMUSP00000053551; ENSMUSG00000049551.
GeneID14371.
KEGGmmu:14371.
UCSCuc008zya.2. mouse.

Organism-specific databases

CTD8326.
MGIMGI:1313278. Fzd9.

Phylogenomic databases

eggNOGNOG257258.
GeneTreeENSGT00750000117488.
HOGENOMHOG000233236.
HOVERGENHBG006977.
InParanoidQ9R216.
KOK02842.
OMANALCMEA.
OrthoDBEOG7M3J01.
PhylomeDBQ9R216.
TreeFamTF317907.

Gene expression databases

BgeeQ9R216.
CleanExMM_FZD3.
MM_FZD9.
GenevestigatorQ9R216.

Family and domain databases

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

NextBio285857.
PROQ9R216.
SOURCESearch...

Entry information

Entry nameFZD9_MOUSE
AccessionPrimary (citable) accession number: Q9R216
Secondary accession number(s): O35494, Q9CX16, Q9R2B3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 114 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

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