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Protein

Protein Wnt

Gene

Wnt3a

Organism
Rattus norvegicus (Rat)
Status
Unreviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

Functioni

Ligand for members of the frizzled family of seven transmembrane receptors.UniRule annotation

GO - Molecular functioni

  1. frizzled binding Source: GO_Central
  2. transcription coactivator activity Source: Ensembl

GO - Biological processi

  1. axis elongation involved in somitogenesis Source: Ensembl
  2. axon guidance Source: Ensembl
  3. canonical Wnt signaling pathway involved in cardiac muscle cell fate commitment Source: Ensembl
  4. cell fate commitment Source: GO_Central
  5. cell proliferation in forebrain Source: Ensembl
  6. cellular protein localization Source: Ensembl
  7. COP9 signalosome assembly Source: Ensembl
  8. dorsal/ventral neural tube patterning Source: Ensembl
  9. extracellular matrix organization Source: Ensembl
  10. heart looping Source: Ensembl
  11. hemopoiesis Source: Ensembl
  12. hippocampus development Source: Ensembl
  13. inner ear morphogenesis Source: Ensembl
  14. in utero embryonic development Source: Ensembl
  15. mammary gland development Source: Ensembl
  16. negative regulation of axon extension involved in axon guidance Source: Ensembl
  17. negative regulation of fat cell differentiation Source: Ensembl
  18. negative regulation of heart induction by canonical Wnt signaling pathway Source: Ensembl
  19. neuron differentiation Source: GO_Central
  20. osteoblast differentiation Source: Ensembl
  21. palate development Source: Ensembl
  22. paraxial mesodermal cell fate commitment Source: Ensembl
  23. platelet aggregation Source: Ensembl
  24. positive regulation of B cell proliferation Source: Ensembl
  25. positive regulation of canonical Wnt signaling pathway involved in controlling type B pancreatic cell proliferation Source: Ensembl
  26. positive regulation of cardiac muscle cell differentiation Source: Ensembl
  27. positive regulation of catenin import into nucleus Source: Ensembl
  28. positive regulation of cell-cell adhesion mediated by cadherin Source: Ensembl
  29. positive regulation of collateral sprouting in absence of injury Source: Ensembl
  30. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
  31. positive regulation of dermatome development Source: Ensembl
  32. positive regulation of mesodermal cell fate specification Source: Ensembl
  33. positive regulation of neural precursor cell proliferation Source: Ensembl
  34. positive regulation of peptidyl-serine phosphorylation Source: Ensembl
  35. positive regulation of protein binding Source: Ensembl
  36. positive regulation of protein tyrosine kinase activity Source: Ensembl
  37. positive regulation of receptor internalization Source: Ensembl
  38. positive regulation of sequence-specific DNA binding transcription factor activity Source: Ensembl
  39. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  40. post-anal tail morphogenesis Source: Ensembl
  41. regulation of cell differentiation Source: RGD
  42. regulation of cell growth Source: RGD
  43. regulation of microtubule cytoskeleton organization Source: Ensembl
  44. skeletal muscle cell differentiation Source: Ensembl
  45. spinal cord association neuron differentiation Source: Ensembl
  46. Wnt signaling pathway Source: GO_Central
  47. Wnt signaling pathway involved in forebrain neuroblast division Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Developmental proteinUniRule annotationSAAS annotation

Keywords - Biological processi

Wnt signaling pathwayUniRule annotationSAAS annotation

Enzyme and pathway databases

ReactomeiREACT_276957. RNF mutants show enhanced WNT signaling and proliferation.
REACT_292827. TCF dependent signaling in response to WNT.
REACT_314668. WNT ligand biogenesis and trafficking.
REACT_318736. regulation of FZD by ubiquitination.
REACT_323768. Class B/2 (Secretin family receptors).
REACT_336108. negative regulation of TCF-dependent signaling by WNT ligand antagonists.
REACT_341833. disassembly of the destruction complex and recruitment of AXIN to the membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein WntUniRule annotation
Gene namesi
Name:Wnt3aImported
Synonyms:Wnt3Imported
OrganismiRattus norvegicus (Rat)Imported
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi3972. Wnt3.
1308057. Wnt3a.

Subcellular locationi

Secretedextracellular spaceextracellular matrix UniRule annotation

GO - Cellular componenti

  1. cell surface Source: Ensembl
  2. cytoplasm Source: RGD
  3. extracellular space Source: GO_Central
  4. proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrixSAAS annotation, Secreted

PTM / Processingi

Keywords - PTMi

Disulfide bondSAAS annotation

Interactioni

Structurei

3D structure databases

ProteinModelPortaliF1M077.
SMRiF1M077. Positions 57-351.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Wnt family.UniRule annotation

Phylogenomic databases

GeneTreeiENSGT00760000118943.
KOiK00312.
OMAiCTTVNDS.
OrthoDBiEOG7C8GJ8.

Family and domain databases

InterProiIPR005817. Wnt.
IPR009141. Wnt3.
IPR018161. Wnt_CS.
[Graphical view]
PANTHERiPTHR12027. PTHR12027. 1 hit.
PfamiPF00110. wnt. 1 hit.
[Graphical view]
PRINTSiPR01843. WNT3PROTEIN.
PR01349. WNTPROTEIN.
SMARTiSM00097. WNT1. 1 hit.
[Graphical view]
PROSITEiPS00246. WNT1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

F1M077-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPLGYLLVL CSLKQALGSY PIWWSLAVGP QYSSLSTQPI LCASIPGLVP
60 70 80 90 100
KQLRFCRNYV EIMPSVAEGV KAGIQECQHQ FRGRRWNCTT VSNSLAIFGP
110 120 130 140 150
VLDKATRESA FVHAIASAGV AFAVTRSCAE GSAAICGCSS RLQGSPGEGW
160 170 180 190 200
KWGGCSEDIE FGGMVSREFA DARENRPDAR SAMNRHNNEA GRQAIASHMH
210 220 230 240 250
LKCKCHGLSG SCEVKTCWWS QPDFRTIGDF LKDKYDSASE MVVEKHRESR
260 270 280 290 300
GWVETLRPRY TYFKVPTERD LVYYEASPNF CEPNPETGSF GTRDRTCNVS
310 320 330 340 350
SHGIDGCDLL CCGRGHNART ERRREKCHCV FHWCCYVSCQ ECTRVYDVHT

CK
Length:352
Mass (Da):39,258
Last modified:April 3, 2013 - v2
Checksum:i7ADFC5B38A8EFF63
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06064066 Genomic DNA. No translation available.
RefSeqiXP_006246549.1. XM_006246487.2.
UniGeneiRn.234269.

Genome annotation databases

EnsembliENSRNOT00000064505; ENSRNOP00000063833; ENSRNOG00000003039.
GeneIDi303181.
KEGGirno:303181.
UCSCiRGD:3972. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06064066 Genomic DNA. No translation available.
RefSeqiXP_006246549.1. XM_006246487.2.
UniGeneiRn.234269.

3D structure databases

ProteinModelPortaliF1M077.
SMRiF1M077. Positions 57-351.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiF1M077.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000064505; ENSRNOP00000063833; ENSRNOG00000003039.
GeneIDi303181.
KEGGirno:303181.
UCSCiRGD:3972. rat.

Organism-specific databases

CTDi89780.
RGDi3972. Wnt3.
1308057. Wnt3a.

Phylogenomic databases

GeneTreeiENSGT00760000118943.
KOiK00312.
OMAiCTTVNDS.
OrthoDBiEOG7C8GJ8.

Enzyme and pathway databases

ReactomeiREACT_276957. RNF mutants show enhanced WNT signaling and proliferation.
REACT_292827. TCF dependent signaling in response to WNT.
REACT_314668. WNT ligand biogenesis and trafficking.
REACT_318736. regulation of FZD by ubiquitination.
REACT_323768. Class B/2 (Secretin family receptors).
REACT_336108. negative regulation of TCF-dependent signaling by WNT ligand antagonists.
REACT_341833. disassembly of the destruction complex and recruitment of AXIN to the membrane.

Miscellaneous databases

NextBioi35579744.

Family and domain databases

InterProiIPR005817. Wnt.
IPR009141. Wnt3.
IPR018161. Wnt_CS.
[Graphical view]
PANTHERiPTHR12027. PTHR12027. 1 hit.
PfamiPF00110. wnt. 1 hit.
[Graphical view]
PRINTSiPR01843. WNT3PROTEIN.
PR01349. WNTPROTEIN.
SMARTiSM00097. WNT1. 1 hit.
[Graphical view]
PROSITEiPS00246. WNT1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Rat Genome Sequencing Project Consortium
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown NorwayImported.
  2. Ensembl
    Submitted (JUN-2011) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.

Entry informationi

Entry nameiF1M077_RAT
AccessioniPrimary (citable) accession number: F1M077
Entry historyi
Integrated into UniProtKB/TrEMBL: May 3, 2011
Last sequence update: April 3, 2013
Last modified: April 1, 2015
This is version 37 of the entry and version 2 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Caution

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.