WNT5A_HUMAN
ID WNT5A_HUMAN Reviewed; 380 AA.
AC P41221; A8K4A4; Q6P278;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Protein Wnt-5a;
DE Flags: Precursor;
GN Name=WNT5A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RX PubMed=8288227; DOI=10.1006/geno.1993.1463;
RA Clark C.C., Cohen I.R., Eichstetter I., Cannizarro L.A., McPherson J.D.,
RA Wasmuth J.J., Iozzo R.V.;
RT "Molecular cloning of the human proto-oncogene Wnt-5A and mapping of the
RT gene (WNT5A) to chromosome 3p14-p21.";
RL Genomics 18:249-260(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Mesangial cell, and Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH GPC3.
RX PubMed=14610063; DOI=10.1083/jcb.200302152;
RA De Cat B., Muyldermans S.Y., Coomans C., Degeest G., Vanderschueren B.,
RA Creemers J., Biemar F., Peers B., David G.;
RT "Processing by proprotein convertases is required for glypican-3 modulation
RT of cell survival, Wnt signaling, and gastrulation movements.";
RL J. Cell Biol. 163:625-635(2003).
RN [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15735754; DOI=10.1038/sj.onc.1208370;
RA Kremenevskaja N., von Wasielewski R., Rao A.S., Schoefl C., Andersson T.,
RA Brabant G.;
RT "Wnt-5a has tumor suppressor activity in thyroid carcinoma.";
RL Oncogene 24:2144-2154(2005).
RN [7]
RP FUNCTION.
RX PubMed=17426020; DOI=10.1074/jbc.m700075200;
RA Dissanayake S.K., Wade M., Johnson C.E., O'Connell M.P., Leotlela P.D.,
RA French A.D., Shah K.V., Hewitt K.J., Rosenthal D.T., Indig F.E., Jiang Y.,
RA Nickoloff B.J., Taub D.D., Trent J.M., Moon R.T., Bittner M.,
RA Weeraratna A.T.;
RT "The Wnt5A/protein kinase C pathway mediates motility in melanoma cells via
RT the inhibition of metastasis suppressors and initiation of an epithelial to
RT mesenchymal transition.";
RL J. Biol. Chem. 282:17259-17271(2007).
RN [8]
RP INTERACTION WITH AFM, AND SUBCELLULAR LOCATION.
RX PubMed=26902720; DOI=10.7554/elife.11621;
RA Mihara E., Hirai H., Yamamoto H., Tamura-Kawakami K., Matano M.,
RA Kikuchi A., Sato T., Takagi J.;
RT "Active and water-soluble form of lipidated Wnt protein is maintained by a
RT serum glycoprotein afamin/alpha-albumin.";
RL Elife 5:0-0(2016).
RN [9]
RP INTERACTION WITH PKD1.
RX PubMed=27214281; DOI=10.1038/ncb3363;
RA Kim S., Nie H., Nesin V., Tran U., Outeda P., Bai C.X., Keeling J.,
RA Maskey D., Watnick T., Wessely O., Tsiokas L.;
RT "The polycystin complex mediates Wnt/Ca(2+) signalling.";
RL Nat. Cell Biol. 18:752-764(2016).
RN [10]
RP VARIANTS DRS1 SER-83 AND ARG-182, AND CHARACTERIZATION OF VARIANTS DRS1
RP SER-83 AND ARG-182.
RX PubMed=19918918; DOI=10.1002/dvdy.22156;
RA Person A.D., Beiraghi S., Sieben C.M., Hermanson S., Neumann A.N.,
RA Robu M.E., Schleiffarth J.R., Billington C.J. Jr., van Bokhoven H.,
RA Hoogeboom J.M., Mazzeu J.F., Petryk A., Schimmenti L.A., Brunner H.G.,
RA Ekker S.C., Lohr J.L.;
RT "WNT5A mutations in patients with autosomal dominant Robinow syndrome.";
RL Dev. Dyn. 239:327-337(2010).
RN [11]
RP VARIANTS DRS1 CYS-160 AND GLY-CYS-164 INS.
RX PubMed=29276006; DOI=10.1016/j.ajhg.2017.10.002;
RG Baylor-Hopkins Center for Mendelian Genomics;
RA White J.J., Mazzeu J.F., Coban-Akdemir Z., Bayram Y., Bahrambeigi V.,
RA Hoischen A., van Bon B.W.M., Gezdirici A., Gulec E.Y., Ramond F.,
RA Touraine R., Thevenon J., Shinawi M., Beaver E., Heeley J., Hoover-Fong J.,
RA Durmaz C.D., Karabulut H.G., Marzioglu-Ozdemir E., Cayir A., Duz M.B.,
RA Seven M., Price S., Ferreira B.M., Vianna-Morgante A.M., Ellard S.,
RA Parrish A., Stals K., Flores-Daboub J., Jhangiani S.N., Gibbs R.A.,
RA Brunner H.G., Sutton V.R., Lupski J.R., Carvalho C.M.B.;
RT "WNT signaling perturbations underlie the genetic heterogeneity of Robinow
RT syndrome.";
RL Am. J. Hum. Genet. 102:27-43(2018).
CC -!- FUNCTION: Ligand for members of the frizzled family of seven
CC transmembrane receptors. Can activate or inhibit canonical Wnt
CC signaling, depending on receptor context. In the presence of FZD4,
CC activates beta-catenin signaling. In the presence of ROR2, inhibits the
CC canonical Wnt pathway by promoting beta-catenin degradation through a
CC GSK3-independent pathway which involves down-regulation of beta-
CC catenin-induced reporter gene expression (By similarity). Suppression
CC of the canonical pathway allows chondrogenesis to occur and inhibits
CC tumor formation. Stimulates cell migration. Decreases proliferation,
CC migration, invasiveness and clonogenicity of carcinoma cells and may
CC act as a tumor suppressor (PubMed:15735754). Mediates motility of
CC melanoma cells (PubMed:17426020). Required during embryogenesis for
CC extension of the primary anterior-posterior axis and for outgrowth of
CC limbs and the genital tubercle. Inhibits type II collagen expression in
CC chondrocytes (By similarity). {ECO:0000250|UniProtKB:P22725,
CC ECO:0000250|UniProtKB:Q27Q52, ECO:0000269|PubMed:15735754,
CC ECO:0000269|PubMed:17426020}.
CC -!- SUBUNIT: Forms a soluble 1:1 complex with AFM; this prevents
CC oligomerization and is required for prolonged biological activity
CC (PubMed:26902720). The complex with AFM may represent the physiological
CC form in body fluids (PubMed:26902720). Homooligomer; disulfide-linked,
CC leading to inactivation (in vitro). Interacts with PORCN. Interacts
CC with WLS (By similarity). Interacts with glypican GCP3
CC (PubMed:14610063). Interacts with PKD1 (via extracellular domain)
CC (PubMed:27214281). {ECO:0000250|UniProtKB:P22725,
CC ECO:0000269|PubMed:14610063, ECO:0000269|PubMed:26902720,
CC ECO:0000269|PubMed:27214281}.
CC -!- INTERACTION:
CC P41221; Q9Y5W5: WIF1; NbExp=2; IntAct=EBI-6594545, EBI-3922719;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000305}. Secreted {ECO:0000269|PubMed:26902720}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P41221-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P41221-2; Sequence=VSP_035594;
CC -!- TISSUE SPECIFICITY: Expression is increased in differentiated thyroid
CC carcinomas compared to normal thyroid tissue and anaplastic thyroid
CC tumors where expression is low or undetectable. Expression is found in
CC thyrocytes but not in stromal cells (at protein level)
CC (PubMed:15735754). Detected in neonate heart and lung (PubMed:8288227).
CC {ECO:0000269|PubMed:15735754, ECO:0000269|PubMed:8288227}.
CC -!- PTM: Glycosylation is necessary for secretion but not for activity.
CC {ECO:0000250|UniProtKB:P22725}.
CC -!- PTM: Palmitoleoylation is required for efficient binding to frizzled
CC receptors. Depalmitoleoylation leads to Wnt signaling pathway
CC inhibition. {ECO:0000250|UniProtKB:P27467,
CC ECO:0000250|UniProtKB:P56704}.
CC -!- PTM: Proteolytic processing by TIKI1 and TIKI2 promotes oxidation and
CC formation of large disulfide-bond oligomers, leading to inactivation of
CC WNT5A. {ECO:0000250|UniProtKB:P22725}.
CC -!- DISEASE: Robinow syndrome, autosomal dominant 1 (DRS1) [MIM:180700]: A
CC disease characterized by short-limb dwarfism, costovertebral
CC segmentation defects and abnormalities of the head, face and external
CC genitalia. The clinical signs are generally milder in dominant cases.
CC {ECO:0000269|PubMed:19918918, ECO:0000269|PubMed:29276006}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/WNT5AID42825ch3p14.html";
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DR EMBL; L20861; AAA16842.1; -; mRNA.
DR EMBL; AK290375; BAF83064.1; -; mRNA.
DR EMBL; AK290869; BAF83558.1; -; mRNA.
DR EMBL; CH471055; EAW65310.1; -; Genomic_DNA.
DR EMBL; BC064694; AAH64694.1; -; mRNA.
DR CCDS; CCDS46850.1; -. [P41221-1]
DR CCDS; CCDS58835.1; -. [P41221-2]
DR PIR; A48914; A48914.
DR RefSeq; NP_001243034.1; NM_001256105.1. [P41221-2]
DR RefSeq; NP_003383.2; NM_003392.4. [P41221-1]
DR RefSeq; XP_006713387.1; XM_006713324.1.
DR RefSeq; XP_011532387.1; XM_011534085.2. [P41221-2]
DR RefSeq; XP_011532388.1; XM_011534086.2. [P41221-2]
DR RefSeq; XP_011532389.1; XM_011534087.2.
DR RefSeq; XP_011532390.1; XM_011534088.2. [P41221-2]
DR RefSeq; XP_011532391.1; XM_011534089.1. [P41221-2]
DR RefSeq; XP_016862617.1; XM_017007128.1. [P41221-2]
DR AlphaFoldDB; P41221; -.
DR SMR; P41221; -.
DR BioGRID; 113311; 67.
DR DIP; DIP-29735N; -.
DR IntAct; P41221; 24.
DR MINT; P41221; -.
DR STRING; 9606.ENSP00000264634; -.
DR GlyConnect; 1672; 2 N-Linked glycans (1 site).
DR GlyGen; P41221; 4 sites, 2 N-linked glycans (1 site).
DR iPTMnet; P41221; -.
DR PhosphoSitePlus; P41221; -.
DR BioMuta; WNT5A; -.
DR DMDM; 212276478; -.
DR EPD; P41221; -.
DR jPOST; P41221; -.
DR MassIVE; P41221; -.
DR MaxQB; P41221; -.
DR PaxDb; P41221; -.
DR PeptideAtlas; P41221; -.
DR PRIDE; P41221; -.
DR ProteomicsDB; 55429; -. [P41221-1]
DR ProteomicsDB; 55430; -. [P41221-2]
DR Antibodypedia; 31456; 592 antibodies from 39 providers.
DR DNASU; 7474; -.
DR Ensembl; ENST00000264634.9; ENSP00000264634.4; ENSG00000114251.15. [P41221-1]
DR Ensembl; ENST00000474267.5; ENSP00000417310.1; ENSG00000114251.15. [P41221-1]
DR Ensembl; ENST00000497027.5; ENSP00000420104.1; ENSG00000114251.15. [P41221-2]
DR GeneID; 7474; -.
DR KEGG; hsa:7474; -.
DR MANE-Select; ENST00000264634.9; ENSP00000264634.4; NM_003392.7; NP_003383.4.
DR UCSC; uc003dhn.5; human. [P41221-1]
DR CTD; 7474; -.
DR DisGeNET; 7474; -.
DR GeneCards; WNT5A; -.
DR GeneReviews; WNT5A; -.
DR HGNC; HGNC:12784; WNT5A.
DR HPA; ENSG00000114251; Tissue enhanced (endometrium, salivary gland).
DR MalaCards; WNT5A; -.
DR MIM; 164975; gene.
DR MIM; 180700; phenotype.
DR neXtProt; NX_P41221; -.
DR OpenTargets; ENSG00000114251; -.
DR Orphanet; 3107; Autosomal dominant Robinow syndrome.
DR PharmGKB; PA37385; -.
DR VEuPathDB; HostDB:ENSG00000114251; -.
DR eggNOG; KOG3913; Eukaryota.
DR GeneTree; ENSGT00940000158894; -.
DR HOGENOM; CLU_033039_0_1_1; -.
DR InParanoid; P41221; -.
DR OMA; EGELNSC; -.
DR OrthoDB; 695671at2759; -.
DR PhylomeDB; P41221; -.
DR TreeFam; TF105310; -.
DR PathwayCommons; P41221; -.
DR Reactome; R-HSA-201681; TCF dependent signaling in response to WNT.
DR Reactome; R-HSA-3238698; WNT ligand biogenesis and trafficking.
DR Reactome; R-HSA-373080; Class B/2 (Secretin family receptors).
DR Reactome; R-HSA-3772470; Negative regulation of TCF-dependent signaling by WNT ligand antagonists.
DR Reactome; R-HSA-4086398; Ca2+ pathway.
DR Reactome; R-HSA-4086400; PCP/CE pathway.
DR Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-HSA-5099900; WNT5A-dependent internalization of FZD4.
DR Reactome; R-HSA-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-HSA-9673324; WNT5:FZD7-mediated leishmania damping.
DR SignaLink; P41221; -.
DR SIGNOR; P41221; -.
DR BioGRID-ORCS; 7474; 6 hits in 1063 CRISPR screens.
DR ChiTaRS; WNT5A; human.
DR GeneWiki; WNT5A; -.
DR GenomeRNAi; 7474; -.
DR Pharos; P41221; Tbio.
DR PRO; PR:P41221; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P41221; protein.
DR Bgee; ENSG00000114251; Expressed in stromal cell of endometrium and 178 other tissues.
DR ExpressionAtlas; P41221; baseline and differential.
DR Genevisible; P41221; HS.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; TAS:Reactome.
DR GO; GO:0031012; C:extracellular matrix; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; TAS:ARUK-UCL.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:1902379; F:chemoattractant activity involved in axon guidance; IEA:Ensembl.
DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR GO; GO:0005109; F:frizzled binding; IPI:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; TAS:ARUK-UCL.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0048018; F:receptor ligand activity; IC:BHF-UCL.
DR GO; GO:0005115; F:receptor tyrosine kinase-like orphan receptor binding; IPI:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; IEA:Ensembl.
DR GO; GO:0032148; P:activation of protein kinase B activity; IDA:BHF-UCL.
DR GO; GO:0008595; P:anterior/posterior axis specification, embryo; IEA:Ensembl.
DR GO; GO:0003283; P:atrial septum development; IEA:Ensembl.
DR GO; GO:0048846; P:axon extension involved in axon guidance; IEA:Ensembl.
DR GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
DR GO; GO:0030509; P:BMP signaling pathway; IEA:Ensembl.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0051216; P:cartilage development; IEA:UniProtKB-KW.
DR GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR GO; GO:0071277; P:cellular response to calcium ion; IEP:UniProtKB.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IEP:UniProtKB.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:UniProtKB.
DR GO; GO:0071300; P:cellular response to retinoic acid; ISS:UniProtKB.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEP:UniProtKB.
DR GO; GO:0060067; P:cervix development; IEA:Ensembl.
DR GO; GO:0036517; P:chemoattraction of serotonergic neuron axon; IEA:Ensembl.
DR GO; GO:0036518; P:chemorepulsion of dopaminergic neuron axon; IEA:Ensembl.
DR GO; GO:0090103; P:cochlea morphogenesis; IEA:Ensembl.
DR GO; GO:0060028; P:convergent extension involved in axis elongation; IEA:Ensembl.
DR GO; GO:0060029; P:convergent extension involved in organogenesis; IEA:Ensembl.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IEA:Ensembl.
DR GO; GO:0048706; P:embryonic skeletal system development; IMP:BHF-UCL.
DR GO; GO:0010631; P:epithelial cell migration; IEA:Ensembl.
DR GO; GO:0060750; P:epithelial cell proliferation involved in mammary gland duct elongation; IEA:Ensembl.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; IEP:UniProtKB.
DR GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; IEA:Ensembl.
DR GO; GO:0001736; P:establishment of planar polarity; IEA:Ensembl.
DR GO; GO:1904861; P:excitatory synapse assembly; TAS:ParkinsonsUK-UCL.
DR GO; GO:0060324; P:face development; IMP:BHF-UCL.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0048806; P:genitalia development; IMP:BHF-UCL.
DR GO; GO:0001947; P:heart looping; IEA:Ensembl.
DR GO; GO:0071425; P:hematopoietic stem cell proliferation; IDA:BHF-UCL.
DR GO; GO:0007442; P:hindgut morphogenesis; IEA:Ensembl.
DR GO; GO:0048850; P:hypophysis morphogenesis; IEA:Ensembl.
DR GO; GO:1904862; P:inhibitory synapse assembly; TAS:ParkinsonsUK-UCL.
DR GO; GO:0007254; P:JNK cascade; IEA:Ensembl.
DR GO; GO:0030216; P:keratinocyte differentiation; IEP:BHF-UCL.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0060599; P:lateral sprouting involved in mammary gland duct morphogenesis; IEA:Ensembl.
DR GO; GO:0002088; P:lens development in camera-type eye; ISS:BHF-UCL.
DR GO; GO:0030324; P:lung development; IEA:Ensembl.
DR GO; GO:0008584; P:male gonad development; IEP:UniProtKB.
DR GO; GO:0060744; P:mammary gland branching involved in thelarche; IEA:Ensembl.
DR GO; GO:0140013; P:meiotic nuclear division; IEA:Ensembl.
DR GO; GO:0097325; P:melanocyte proliferation; IEA:Ensembl.
DR GO; GO:0010463; P:mesenchymal cell proliferation; IEA:Ensembl.
DR GO; GO:0060638; P:mesenchymal-epithelial cell signaling; IEA:Ensembl.
DR GO; GO:0060809; P:mesodermal to mesenchymal transition involved in gastrulation; IEA:Ensembl.
DR GO; GO:0007494; P:midgut development; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0048843; P:negative regulation of axon extension involved in axon guidance; IEA:Ensembl.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IEA:Ensembl.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IGI:MGI.
DR GO; GO:1904934; P:negative regulation of cell proliferation in midbrain; NAS:ParkinsonsUK-UCL.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IMP:BHF-UCL.
DR GO; GO:0040037; P:negative regulation of fibroblast growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0048022; P:negative regulation of melanin biosynthetic process; IEA:Ensembl.
DR GO; GO:0072201; P:negative regulation of mesenchymal cell proliferation; IDA:UniProtKB.
DR GO; GO:0060686; P:negative regulation of prostatic bud formation; IEA:Ensembl.
DR GO; GO:0051964; P:negative regulation of synapse assembly; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; ISS:UniProtKB.
DR GO; GO:0035567; P:non-canonical Wnt signaling pathway; TAS:ParkinsonsUK-UCL.
DR GO; GO:0038031; P:non-canonical Wnt signaling pathway via JNK cascade; IEA:Ensembl.
DR GO; GO:0048570; P:notochord morphogenesis; IEA:Ensembl.
DR GO; GO:0021891; P:olfactory bulb interneuron development; ISS:UniProtKB.
DR GO; GO:0003408; P:optic cup formation involved in camera-type eye development; ISS:BHF-UCL.
DR GO; GO:0048341; P:paraxial mesoderm formation; IEA:Ensembl.
DR GO; GO:0003402; P:planar cell polarity pathway involved in axis elongation; IEA:Ensembl.
DR GO; GO:1904938; P:planar cell polarity pathway involved in axon guidance; IEA:Ensembl.
DR GO; GO:0061350; P:planar cell polarity pathway involved in cardiac muscle tissue morphogenesis; IEA:Ensembl.
DR GO; GO:0061349; P:planar cell polarity pathway involved in cardiac right atrium morphogenesis; IEA:Ensembl.
DR GO; GO:0060775; P:planar cell polarity pathway involved in gastrula mediolateral intercalation; IEA:Ensembl.
DR GO; GO:1904955; P:planar cell polarity pathway involved in midbrain dopaminergic neuron differentiation; TAS:ParkinsonsUK-UCL.
DR GO; GO:0090179; P:planar cell polarity pathway involved in neural tube closure; IEA:Ensembl.
DR GO; GO:0061347; P:planar cell polarity pathway involved in outflow tract morphogenesis; IEA:Ensembl.
DR GO; GO:0061354; P:planar cell polarity pathway involved in pericardium morphogenesis; IEA:Ensembl.
DR GO; GO:0061348; P:planar cell polarity pathway involved in ventricular septum morphogenesis; IEA:Ensembl.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:UniProtKB.
DR GO; GO:0061036; P:positive regulation of cartilage development; IEA:Ensembl.
DR GO; GO:2000049; P:positive regulation of cell-cell adhesion mediated by cadherin; IEA:Ensembl.
DR GO; GO:0032722; P:positive regulation of chemokine production; IMP:UniProtKB.
DR GO; GO:0002720; P:positive regulation of cytokine production involved in immune response; IMP:UniProtKB.
DR GO; GO:0045807; P:positive regulation of endocytosis; IEA:Ensembl.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IMP:UniProtKB.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IMP:UniProtKB.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IDA:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:ARUK-UCL.
DR GO; GO:0090082; P:positive regulation of heart induction by negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:1902035; P:positive regulation of hematopoietic stem cell proliferation; IEA:Ensembl.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IMP:BHF-UCL.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IEA:Ensembl.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IMP:BHF-UCL.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:BHF-UCL.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IEA:Ensembl.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IEA:Ensembl.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; IDA:BHF-UCL.
DR GO; GO:0043032; P:positive regulation of macrophage activation; IMP:BHF-UCL.
DR GO; GO:0060907; P:positive regulation of macrophage cytokine production; IMP:UniProtKB.
DR GO; GO:0045836; P:positive regulation of meiotic nuclear division; IEA:Ensembl.
DR GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IEA:Ensembl.
DR GO; GO:1901216; P:positive regulation of neuron death; ISS:ARUK-UCL.
DR GO; GO:0150012; P:positive regulation of neuron projection arborization; ISS:ARUK-UCL.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
DR GO; GO:2000052; P:positive regulation of non-canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0045778; P:positive regulation of ossification; IMP:BHF-UCL.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IEA:Ensembl.
DR GO; GO:0032092; P:positive regulation of protein binding; IEA:Ensembl.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IGI:MGI.
DR GO; GO:1900020; P:positive regulation of protein kinase C activity; IMP:CACAO.
DR GO; GO:0090037; P:positive regulation of protein kinase C signaling; IMP:UniProtKB.
DR GO; GO:1902474; P:positive regulation of protein localization to synapse; TAS:ParkinsonsUK-UCL.
DR GO; GO:0060760; P:positive regulation of response to cytokine stimulus; IDA:UniProtKB.
DR GO; GO:0010820; P:positive regulation of T cell chemotaxis; IMP:UniProtKB.
DR GO; GO:0070245; P:positive regulation of thymocyte apoptotic process; IEA:Ensembl.
DR GO; GO:0051885; P:positive regulation of timing of anagen; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISS:ARUK-UCL.
DR GO; GO:0060340; P:positive regulation of type I interferon-mediated signaling pathway; IDA:BHF-UCL.
DR GO; GO:0036342; P:post-anal tail morphogenesis; IEA:Ensembl.
DR GO; GO:0099068; P:postsynapse assembly; TAS:ParkinsonsUK-UCL.
DR GO; GO:0099054; P:presynapse assembly; TAS:ParkinsonsUK-UCL.
DR GO; GO:0003138; P:primary heart field specification; IEA:Ensembl.
DR GO; GO:0090009; P:primitive streak formation; IEA:Ensembl.
DR GO; GO:0008104; P:protein localization; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
DR GO; GO:0060762; P:regulation of branching involved in mammary gland duct morphogenesis; IEA:Ensembl.
DR GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; ISS:ARUK-UCL.
DR GO; GO:0050727; P:regulation of inflammatory response; NAS:ARUK-UCL.
DR GO; GO:0099175; P:regulation of postsynapse organization; IDA:SynGO.
DR GO; GO:0099566; P:regulation of postsynaptic cytosolic calcium ion concentration; IDA:SynGO.
DR GO; GO:0050807; P:regulation of synapse organization; IDA:SynGO.
DR GO; GO:0010033; P:response to organic substance; IEP:UniProtKB.
DR GO; GO:0003139; P:secondary heart field specification; IEA:Ensembl.
DR GO; GO:0062009; P:secondary palate development; IMP:BHF-UCL.
DR GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
DR GO; GO:0070242; P:thymocyte apoptotic process; IEA:Ensembl.
DR GO; GO:0003323; P:type B pancreatic cell development; IEA:Ensembl.
DR GO; GO:0060157; P:urinary bladder development; IEA:Ensembl.
DR GO; GO:0060065; P:uterus development; IEA:Ensembl.
DR GO; GO:0060068; P:vagina development; IEA:Ensembl.
DR GO; GO:0016055; P:Wnt signaling pathway; IDA:BHF-UCL.
DR GO; GO:1904953; P:Wnt signaling pathway involved in midbrain dopaminergic neuron differentiation; NAS:ParkinsonsUK-UCL.
DR GO; GO:0007223; P:Wnt signaling pathway, calcium modulating pathway; IMP:UniProtKB.
DR GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:ParkinsonsUK-UCL.
DR GO; GO:0042060; P:wound healing; IDA:UniProtKB.
DR Gene3D; 3.30.2460.20; -; 1.
DR InterPro; IPR005817; Wnt.
DR InterPro; IPR026538; Wnt5a.
DR InterPro; IPR043158; Wnt_C.
DR InterPro; IPR018161; Wnt_CS.
DR PANTHER; PTHR12027; PTHR12027; 1.
DR PANTHER; PTHR12027:SF33; PTHR12027:SF33; 1.
DR Pfam; PF00110; wnt; 1.
DR PRINTS; PR01349; WNTPROTEIN.
DR SMART; SM00097; WNT1; 1.
DR PROSITE; PS00246; WNT1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chondrogenesis; Developmental protein;
KW Differentiation; Disease variant; Disulfide bond; Dwarfism;
KW Extracellular matrix; Glycoprotein; Lipoprotein; Reference proteome;
KW Secreted; Signal; Wnt signaling pathway.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT PROPEP 36..61
FT /evidence="ECO:0000250"
FT /id="PRO_0000352796"
FT CHAIN 62..380
FT /note="Protein Wnt-5a"
FT /id="PRO_0000041427"
FT LIPID 244
FT /note="O-palmitoleoyl serine; by PORCN"
FT /evidence="ECO:0000250|UniProtKB:P56704"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 104..115
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 154..162
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 164..182
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 238..252
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 240..247
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 309..340
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 325..335
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 339..379
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 355..370
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 357..367
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 362..363
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT VAR_SEQ 1..15
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:8288227"
FT /id="VSP_035594"
FT VARIANT 83
FT /note="C -> S (in DRS1; hypomorphic mutation;
FT dbSNP:rs786200925)"
FT /evidence="ECO:0000269|PubMed:19918918"
FT /id="VAR_066623"
FT VARIANT 160
FT /note="S -> C (in DRS1; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:29276006"
FT /id="VAR_083248"
FT VARIANT 164
FT /note="C -> CGC (in DRS1)"
FT /evidence="ECO:0000269|PubMed:29276006"
FT /id="VAR_083249"
FT VARIANT 182
FT /note="C -> R (in DRS1; hypomorphic mutation;
FT dbSNP:rs387906663)"
FT /evidence="ECO:0000269|PubMed:19918918"
FT /id="VAR_066629"
SQ SEQUENCE 380 AA; 42339 MW; 50E73AC7FE96C7B5 CRC64;
MKKSIGILSP GVALGMAGSA MSSKFFLVAL AIFFSFAQVV IEANSWWSLG MNNPVQMSEV
YIIGAQPLCS QLAGLSQGQK KLCHLYQDHM QYIGEGAKTG IKECQYQFRH RRWNCSTVDN
TSVFGRVMQI GSRETAFTYA VSAAGVVNAM SRACREGELS TCGCSRAARP KDLPRDWLWG
GCGDNIDYGY RFAKEFVDAR ERERIHAKGS YESARILMNL HNNEAGRRTV YNLADVACKC
HGVSGSCSLK TCWLQLADFR KVGDALKEKY DSAAAMRLNS RGKLVQVNSR FNSPTTQDLV
YIDPSPDYCV RNESTGSLGT QGRLCNKTSE GMDGCELMCC GRGYDQFKTV QTERCHCKFH
WCCYVKCKKC TEIVDQFVCK
