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Q8BKG4 (FZD10_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 89. 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-10

Short name=Fz-10
Alternative name(s):
CD_antigen=CD350
Gene names
Name:Fzd10
Synonyms:Fz10
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length582 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 By similarity.

Subunit structure

Interacts with MYOC By similarity.

Subcellular location

Cell membrane; Multi-pass membrane protein By similarity.

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_processWnt signaling pathway

Inferred from genetic interaction PubMed 15923619. 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

negative regulation of Rho GTPase activity

Inferred from electronic annotation. Source: Ensembl

non-canonical Wnt signaling pathway via JNK cascade

Inferred from electronic annotation. Source: Ensembl

positive regulation of JUN kinase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of Rac GTPase activity

Inferred from electronic annotation. Source: Ensembl

regulation of actin cytoskeleton organization

Inferred from electronic annotation. Source: Ensembl

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 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

plasma 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 – 2121 Potential
Chain22 – 582561Frizzled-10
PRO_0000013006

Regions

Topological domain22 – 226205Extracellular Potential
Transmembrane227 – 24721Helical; Name=1; Potential
Topological domain248 – 26316Cytoplasmic Potential
Transmembrane264 – 28421Helical; Name=2; Potential
Topological domain285 – 31228Extracellular Potential
Transmembrane313 – 33321Helical; Name=3; Potential
Topological domain334 – 35219Cytoplasmic Potential
Transmembrane353 – 37321Helical; Name=4; Potential
Topological domain374 – 39421Extracellular Potential
Transmembrane395 – 41521Helical; Name=5; Potential
Topological domain416 – 44429Cytoplasmic Potential
Transmembrane445 – 46521Helical; Name=6; Potential
Topological domain466 – 50338Extracellular Potential
Transmembrane504 – 52421Helical; Name=7; Potential
Topological domain525 – 58258Cytoplasmic Potential
Domain30 – 151122FZ
Motif527 – 5326Lys-Thr-X-X-X-Trp motif, mediates interaction with the PDZ domain of Dvl family members By similarity
Motif580 – 5823PDZ-binding

Amino acid modifications

Glycosylation491N-linked (GlcNAc...) Potential
Glycosylation1541N-linked (GlcNAc...) Potential
Glycosylation4861N-linked (GlcNAc...) Potential
Disulfide bond35 ↔ 96 By similarity
Disulfide bond43 ↔ 89 By similarity
Disulfide bond80 ↔ 118 By similarity
Disulfide bond107 ↔ 148 By similarity
Disulfide bond111 ↔ 135 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8BKG4 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 3ED4F5340B1505E0

FASTA58265,318
        10         20         30         40         50         60 
MQHPGPRLWL VLQVMIGSCT AISSMDLERP GDGKCQPVEI PMCKDIGYNT TRMPNLMGHE 

        70         80         90        100        110        120 
NQREAAIQLH EFAPLVEYGC HSHLRFFLCS LYAPMCTEQV STPIPACRVM CEQARLKCSP 

       130        140        150        160        170        180 
IMEQFKFRWP DSLDCSKLPN KNDPNYLCME APNNGSDEPS RGSGMFPPLF RPQRPHSAQE 

       190        200        210        220        230        240 
HPLKDGGPGR AGCDNPGKFH HVEKSESCAP LCTPGVDVYW SRDDKRFAVV WLAIWSVLCF 

       250        260        270        280        290        300 
FSSAFTVLTF LIDPSRFRYP ERPIIFLSMC YCVYSVGYII RLFAGAESIA CDRDSGQLYV 

       310        320        330        340        350        360 
IQEGLESTGC TLVFLVLYYF GMASSLWWVV LTLTWFLAAG KKWGHEAIEA NSSYFHLAAW 

       370        380        390        400        410        420 
AIPAVKTILI LVMRRVAGDE LTGVCYVGSM DVNALTGFVL VPLACYLVIG TSFILSGFVA 

       430        440        450        460        470        480 
LFHIRRVMKT GGENTDKLEK LMVRIGVFSL LYTVPATCVI ACYFYERLNM DYWKMLATQH 

       490        500        510        520        530        540 
KCKMNNQTKT PDCLMTTSIP AVEVFMVKVS MLLVVGITSG VWVWTSKTLQ SWQHVCSRGL 

       550        560        570        580 
KRKSRRKPAS VVTSAGIYKK AQHPQKPHLG KYELPAQPSA CV 

« Hide

References

« Hide 'large scale' references
[1]"Analysis of Fz10 expression in mouse embryos."
Nunnally A.P., Parr B.A.
Dev. Genes Evol. 214:144-148(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: CD-1.
[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: Head.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY509002 mRNA. Translation: AAR92468.1.
AK052950 mRNA. Translation: BAC35217.1.
RefSeqNP_780493.1. NM_175284.3.
UniGeneMm.197628.

3D structure databases

ProteinModelPortalQ8BKG4.
SMRQ8BKG4. Positions 35-151, 194-538.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid220362. 2 interactions.
STRING10090.ENSMUSP00000114114.

Protein family/group databases

MEROPSI93.001.
GPCRDBSearch...

Proteomic databases

PRIDEQ8BKG4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000117102; ENSMUSP00000114114; ENSMUSG00000081683.
GeneID93897.
KEGGmmu:93897.
UCSCuc008zsh.1. mouse.

Organism-specific databases

CTD11211.
MGIMGI:2136761. Fzd10.

Phylogenomic databases

eggNOGNOG257258.
GeneTreeENSGT00750000117488.
HOVERGENHBG006977.
InParanoidQ8BKG4.
KOK02842.
OMAEYGCHGH.
OrthoDBEOG7M3J01.
TreeFamTF317907.

Gene expression databases

ArrayExpressQ8BKG4.
BgeeQ8BKG4.
CleanExMM_FZD10.
GenevestigatorQ8BKG4.

Family and domain databases

Gene3D1.10.2000.10. 1 hit.
InterProIPR000539. Frizzled.
IPR015526. Frizzled/SFRP.
IPR020067. Frizzled_dom.
IPR026549. FZD10.
IPR017981. GPCR_2-like.
[Graphical view]
PANTHERPTHR11309. PTHR11309. 1 hit.
PTHR11309:SF24. PTHR11309:SF24. 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

NextBio351851.
PROQ8BKG4.
SOURCESearch...

Entry information

Entry nameFZD10_MOUSE
AccessionPrimary (citable) accession number: Q8BKG4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: March 1, 2003
Last modified: April 16, 2014
This is version 89 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