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Protein Wnt-5a

 WNT5A_HUMAN             Reviewed;         380 AA.
P41221; A8K4A4; Q6P278;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
04-NOV-2008, sequence version 2.
05-DEC-2018, entry version 169.
RecName: Full=Protein Wnt-5a;
Flags: Precursor;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
PubMed=8288227; DOI=10.1006/geno.1993.1463;
Clark C.C., Cohen I.R., Eichstetter I., Cannizarro L.A.,
McPherson J.D., Wasmuth J.J., Iozzo R.V.;
"Molecular cloning of the human proto-oncogene Wnt-5A and mapping of
the gene (WNT5A) to chromosome 3p14-p21.";
Genomics 18:249-260(1993).
TISSUE=Mesangial cell, and Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
Nat. Genet. 36:40-45(2004).
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
PubMed=14610063; DOI=10.1083/jcb.200302152;
De Cat B., Muyldermans S.Y., Coomans C., Degeest G.,
Vanderschueren B., Creemers J., Biemar F., Peers B., David G.;
"Processing by proprotein convertases is required for glypican-3
modulation of cell survival, Wnt signaling, and gastrulation
J. Cell Biol. 163:625-635(2003).
PubMed=15735754; DOI=10.1038/sj.onc.1208370;
Kremenevskaja N., von Wasielewski R., Rao A.S., Schoefl C.,
Andersson T., Brabant G.;
"Wnt-5a has tumor suppressor activity in thyroid carcinoma.";
Oncogene 24:2144-2154(2005).
PubMed=17426020; DOI=10.1074/jbc.M700075200;
Dissanayake S.K., Wade M., Johnson C.E., O'Connell M.P.,
Leotlela P.D., French A.D., Shah K.V., Hewitt K.J., Rosenthal D.T.,
Indig F.E., Jiang Y., Nickoloff B.J., Taub D.D., Trent J.M.,
Moon R.T., Bittner M., Weeraratna A.T.;
"The Wnt5A/protein kinase C pathway mediates motility in melanoma
cells via the inhibition of metastasis suppressors and initiation of
an epithelial to mesenchymal transition.";
J. Biol. Chem. 282:17259-17271(2007).
PubMed=26902720; DOI=10.7554/eLife.11621;
Mihara E., Hirai H., Yamamoto H., Tamura-Kawakami K., Matano M.,
Kikuchi A., Sato T., Takagi J.;
"Active and water-soluble form of lipidated Wnt protein is maintained
by a serum glycoprotein afamin/alpha-albumin.";
Elife 5:0-0(2016).
PubMed=27214281; DOI=10.1038/ncb3363;
Kim S., Nie H., Nesin V., Tran U., Outeda P., Bai C.X., Keeling J.,
Maskey D., Watnick T., Wessely O., Tsiokas L.;
"The polycystin complex mediates Wnt/Ca(2+) signalling.";
Nat. Cell Biol. 18:752-764(2016).
DRS1 SER-83 AND ARG-182.
PubMed=19918918; DOI=10.1002/dvdy.22156;
Person A.D., Beiraghi S., Sieben C.M., Hermanson S., Neumann A.N.,
Robu M.E., Schleiffarth J.R., Billington C.J. Jr., van Bokhoven H.,
Hoogeboom J.M., Mazzeu J.F., Petryk A., Schimmenti L.A., Brunner H.G.,
Ekker S.C., Lohr J.L.;
"WNT5A mutations in patients with autosomal dominant Robinow
Dev. Dyn. 239:327-337(2010).
-!- FUNCTION: Ligand for members of the frizzled family of seven
transmembrane receptors. Can activate or inhibit canonical Wnt
signaling, depending on receptor context. In the presence of FZD4,
activates beta-catenin signaling. In the presence of ROR2,
inhibits the canonical Wnt pathway by promoting beta-catenin
degradation through a GSK3-independent pathway which involves
down-regulation of beta-catenin-induced reporter gene expression
(By similarity). Suppression of the canonical pathway allows
chondrogenesis to occur and inhibits tumor formation. Stimulates
cell migration. Decreases proliferation, migration, invasiveness
and clonogenicity of carcinoma cells and may act as a tumor
suppressor (PubMed:15735754). Mediates motility of melanoma cells
(PubMed:17426020). Required during embryogenesis for extension of
the primary anterior-posterior axis and for outgrowth of limbs and
the genital tubercle. Inhibits type II collagen expression in
chondrocytes (By similarity). {ECO:0000250|UniProtKB:P22725,
ECO:0000250|UniProtKB:Q27Q52, ECO:0000269|PubMed:15735754,
-!- SUBUNIT: Forms a soluble 1:1 complex with AFM; this prevents
oligomerization and is required for prolonged biological activity
(PubMed:26902720). The complex with AFM may represent the
physiological form in body fluids (PubMed:26902720). Homooligomer;
disulfide-linked, leading to inactivation (in vitro). Interacts
with PORCN. Interacts with WLS (By similarity). Interacts with
glypican GCP3 (PubMed:14610063). Interacts with PKD1 (via
extracellular domain) (PubMed:27214281).
{ECO:0000250|UniProtKB:P22725, ECO:0000269|PubMed:14610063,
ECO:0000269|PubMed:26902720, ECO:0000269|PubMed:27214281}.
Q9Y5W5:WIF1; NbExp=2; IntAct=EBI-6594545, EBI-3922719;
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000305}. Secreted {ECO:0000269|PubMed:26902720}.
Event=Alternative splicing; Named isoforms=2;
IsoId=P41221-1; Sequence=Displayed;
IsoId=P41221-2; Sequence=VSP_035594;
-!- TISSUE SPECIFICITY: Expression is increased in differentiated
thyroid carcinomas compared to normal thyroid tissue and
anaplastic thyroid tumors where expression is low or undetectable.
Expression is found in thyrocytes but not in stromal cells (at
protein level) (PubMed:15735754). Detected in neonate heart and
lung (PubMed:8288227). {ECO:0000269|PubMed:15735754,
-!- PTM: Glycosylation is necessary for secretion but not for
activity. {ECO:0000250|UniProtKB:P22725}.
-!- PTM: Palmitoleoylation is required for efficient binding to
frizzled receptors. Depalmitoleoylation leads to Wnt signaling
pathway inhibition. {ECO:0000250|UniProtKB:P27467,
-!- PTM: Proteolytic processing by TIKI1 and TIKI2 promotes oxidation
and formation of large disulfide-bond oligomers, leading to
inactivation of WNT5A. {ECO:0000250|UniProtKB:P22725}.
-!- DISEASE: Robinow syndrome, autosomal dominant 1 (DRS1)
[MIM:180700]: A disease characterized by short-limb dwarfism,
costovertebral segmentation defects and abnormalities of the head,
face and external genitalia. The clinical signs are generally
milder in dominant cases. {ECO:0000269|PubMed:19918918}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the Wnt family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
EMBL; L20861; AAA16842.1; -; mRNA.
EMBL; AK290375; BAF83064.1; -; mRNA.
EMBL; AK290869; BAF83558.1; -; mRNA.
EMBL; CH471055; EAW65310.1; -; Genomic_DNA.
EMBL; BC064694; AAH64694.1; -; mRNA.
CCDS; CCDS46850.1; -. [P41221-1]
CCDS; CCDS58835.1; -. [P41221-2]
PIR; A48914; A48914.
RefSeq; NP_001243034.1; NM_001256105.1. [P41221-2]
RefSeq; NP_003383.2; NM_003392.4. [P41221-1]
RefSeq; XP_006713387.1; XM_006713324.1. [P41221-2]
RefSeq; XP_011532387.1; XM_011534085.2. [P41221-2]
RefSeq; XP_011532388.1; XM_011534086.2. [P41221-2]
RefSeq; XP_011532389.1; XM_011534087.2. [P41221-2]
RefSeq; XP_011532390.1; XM_011534088.2. [P41221-2]
RefSeq; XP_011532391.1; XM_011534089.1. [P41221-2]
RefSeq; XP_016862617.1; XM_017007128.1. [P41221-2]
UniGene; Hs.643085; -.
ProteinModelPortal; P41221; -.
SMR; P41221; -.
BioGrid; 113311; 28.
DIP; DIP-29735N; -.
IntAct; P41221; 5.
MINT; P41221; -.
STRING; 9606.ENSP00000264634; -.
GlyConnect; 1672; -.
iPTMnet; P41221; -.
PhosphoSitePlus; P41221; -.
BioMuta; WNT5A; -.
DMDM; 212276478; -.
MaxQB; P41221; -.
PaxDb; P41221; -.
PeptideAtlas; P41221; -.
PRIDE; P41221; -.
ProteomicsDB; 55429; -.
ProteomicsDB; 55430; -. [P41221-2]
DNASU; 7474; -.
Ensembl; ENST00000264634; ENSP00000264634; ENSG00000114251. [P41221-1]
Ensembl; ENST00000474267; ENSP00000417310; ENSG00000114251. [P41221-1]
Ensembl; ENST00000497027; ENSP00000420104; ENSG00000114251. [P41221-2]
GeneID; 7474; -.
KEGG; hsa:7474; -.
UCSC; uc003dhn.5; human. [P41221-1]
CTD; 7474; -.
DisGeNET; 7474; -.
EuPathDB; HostDB:ENSG00000114251.13; -.
GeneCards; WNT5A; -.
GeneReviews; WNT5A; -.
HGNC; HGNC:12784; WNT5A.
MalaCards; WNT5A; -.
MIM; 164975; gene.
MIM; 180700; phenotype.
neXtProt; NX_P41221; -.
OpenTargets; ENSG00000114251; -.
Orphanet; 3107; Autosomal dominant Robinow syndrome.
PharmGKB; PA37385; -.
eggNOG; KOG3913; Eukaryota.
GeneTree; ENSGT00940000158894; -.
HOVERGEN; HBG001595; -.
InParanoid; P41221; -.
KO; K00444; -.
OrthoDB; EOG091G0OFF; -.
PhylomeDB; P41221; -.
TreeFam; TF105310; -.
Reactome; R-HSA-201681; TCF dependent signaling in response to WNT.
Reactome; R-HSA-3238698; WNT ligand biogenesis and trafficking.
Reactome; R-HSA-373080; Class B/2 (Secretin family receptors).
Reactome; R-HSA-3772470; Negative regulation of TCF-dependent signaling by WNT ligand antagonists.
Reactome; R-HSA-4086398; Ca2+ pathway.
Reactome; R-HSA-4086400; PCP/CE pathway.
Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
Reactome; R-HSA-5099900; WNT5A-dependent internalization of FZD4.
Reactome; R-HSA-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
SignaLink; P41221; -.
SIGNOR; P41221; -.
ChiTaRS; WNT5A; human.
GeneWiki; WNT5A; -.
GenomeRNAi; 7474; -.
PRO; PR:P41221; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000114251; Expressed in 199 organ(s), highest expression level in endometrium.
CleanEx; HS_WNT5A; -.
ExpressionAtlas; P41221; baseline and differential.
Genevisible; P41221; HS.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
GO; GO:0030665; C:clathrin-coated vesicle membrane; TAS:Reactome.
GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; TAS:Reactome.
GO; GO:0031012; C:extracellular matrix; IEA:Ensembl.
GO; GO:0005576; C:extracellular region; TAS:ARUK-UCL.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0098794; C:postsynapse; IEA:GOC.
GO; GO:1902379; F:chemoattractant activity involved in axon guidance; IEA:Ensembl.
GO; GO:0005125; F:cytokine activity; IEA:Ensembl.
GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:UniProtKB.
GO; GO:0005109; F:frizzled binding; IPI:UniProtKB.
GO; GO:0005543; F:phospholipid binding; TAS:ARUK-UCL.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0048018; F:receptor ligand activity; IC:BHF-UCL.
GO; GO:0005115; F:receptor tyrosine kinase-like orphan receptor binding; IPI:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0090630; P:activation of GTPase activity; IEA:Ensembl.
GO; GO:0007257; P:activation of JUN kinase activity; IDA:BHF-UCL.
GO; GO:0000187; P:activation of MAPK activity; IDA:BHF-UCL.
GO; GO:0032148; P:activation of protein kinase B activity; IDA:BHF-UCL.
GO; GO:0008595; P:anterior/posterior axis specification, embryo; IEA:Ensembl.
GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
GO; GO:0051216; P:cartilage development; IEA:UniProtKB-KW.
GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
GO; GO:0034613; P:cellular protein localization; IDA:UniProtKB.
GO; GO:0071277; P:cellular response to calcium ion; IEP:UniProtKB.
GO; GO:0071346; P:cellular response to interferon-gamma; IEP:UniProtKB.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:UniProtKB.
GO; GO:0071300; P:cellular response to retinoic acid; ISS:UniProtKB.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEP:UniProtKB.
GO; GO:0060067; P:cervix development; IEA:Ensembl.
GO; GO:0036517; P:chemoattraction of serotonergic neuron axon; IEA:Ensembl.
GO; GO:0036518; P:chemorepulsion of dopaminergic neuron axon; IEA:Ensembl.
GO; GO:0090103; P:cochlea morphogenesis; IEA:Ensembl.
GO; GO:0060028; P:convergent extension involved in axis elongation; IEA:Ensembl.
GO; GO:0060029; P:convergent extension involved in organogenesis; IEA:Ensembl.
GO; GO:0042733; P:embryonic digit morphogenesis; IEA:Ensembl.
GO; GO:0048706; P:embryonic skeletal system development; IMP:BHF-UCL.
GO; GO:0060750; P:epithelial cell proliferation involved in mammary gland duct elongation; IEA:Ensembl.
GO; GO:0001837; P:epithelial to mesenchymal transition; IEP:UniProtKB.
GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; IEA:Ensembl.
GO; GO:0001736; P:establishment of planar polarity; IEA:Ensembl.
GO; GO:1904861; P:excitatory synapse assembly; TAS:ParkinsonsUK-UCL.
GO; GO:0060324; P:face development; IMP:BHF-UCL.
GO; GO:0048806; P:genitalia development; IMP:BHF-UCL.
GO; GO:0001947; P:heart looping; IEA:Ensembl.
GO; GO:0071425; P:hematopoietic stem cell proliferation; IDA:BHF-UCL.
GO; GO:0007442; P:hindgut morphogenesis; IEA:Ensembl.
GO; GO:0048850; P:hypophysis morphogenesis; IEA:Ensembl.
GO; GO:1904862; P:inhibitory synapse assembly; TAS:ParkinsonsUK-UCL.
GO; GO:0030216; P:keratinocyte differentiation; IEP:BHF-UCL.
GO; GO:0060599; P:lateral sprouting involved in mammary gland duct morphogenesis; IEA:Ensembl.
GO; GO:0002088; P:lens development in camera-type eye; ISS:BHF-UCL.
GO; GO:0030324; P:lung development; IEA:Ensembl.
GO; GO:0008584; P:male gonad development; IEP:UniProtKB.
GO; GO:0060744; P:mammary gland branching involved in thelarche; IEA:Ensembl.
GO; GO:0097325; P:melanocyte proliferation; IEA:Ensembl.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0060638; P:mesenchymal-epithelial cell signaling; IEA:Ensembl.
GO; GO:0060809; P:mesodermal to mesenchymal transition involved in gastrulation; IEA:Ensembl.
GO; GO:0007494; P:midgut development; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0048843; P:negative regulation of axon extension involved in axon guidance; IEA:Ensembl.
GO; GO:0030514; P:negative regulation of BMP signaling pathway; IEA:Ensembl.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IGI:MGI.
GO; GO:1904934; P:negative regulation of cell proliferation in midbrain; NAS:ParkinsonsUK-UCL.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl.
GO; GO:0045599; P:negative regulation of fat cell differentiation; IMP:BHF-UCL.
GO; GO:0040037; P:negative regulation of fibroblast growth factor receptor signaling pathway; IEA:Ensembl.
GO; GO:0048022; P:negative regulation of melanin biosynthetic process; IEA:Ensembl.
GO; GO:0072201; P:negative regulation of mesenchymal cell proliferation; IDA:UniProtKB.
GO; GO:0060686; P:negative regulation of prostatic bud formation; IEA:Ensembl.
GO; GO:0051964; P:negative regulation of synapse assembly; IEA:Ensembl.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0030182; P:neuron differentiation; ISS:UniProtKB.
GO; GO:0035567; P:non-canonical Wnt signaling pathway; TAS:ParkinsonsUK-UCL.
GO; GO:0038031; P:non-canonical Wnt signaling pathway via JNK cascade; IEA:Ensembl.
GO; GO:0048570; P:notochord morphogenesis; IEA:Ensembl.
GO; GO:0021891; P:olfactory bulb interneuron development; ISS:UniProtKB.
GO; GO:0003408; P:optic cup formation involved in camera-type eye development; ISS:BHF-UCL.
GO; GO:0048341; P:paraxial mesoderm formation; IEA:Ensembl.
GO; GO:0003402; P:planar cell polarity pathway involved in axis elongation; IEA:Ensembl.
GO; GO:1904938; P:planar cell polarity pathway involved in axon guidance; IEA:Ensembl.
GO; GO:0061350; P:planar cell polarity pathway involved in cardiac muscle tissue morphogenesis; IEA:Ensembl.
GO; GO:0061349; P:planar cell polarity pathway involved in cardiac right atrium morphogenesis; IEA:Ensembl.
GO; GO:0060775; P:planar cell polarity pathway involved in gastrula mediolateral intercalation; IEA:Ensembl.
GO; GO:1904955; P:planar cell polarity pathway involved in midbrain dopaminergic neuron differentiation; TAS:ParkinsonsUK-UCL.
GO; GO:0090179; P:planar cell polarity pathway involved in neural tube closure; IEA:Ensembl.
GO; GO:0061347; P:planar cell polarity pathway involved in outflow tract morphogenesis; IEA:Ensembl.
GO; GO:0061354; P:planar cell polarity pathway involved in pericardium morphogenesis; IEA:Ensembl.
GO; GO:0061348; P:planar cell polarity pathway involved in ventricular septum morphogenesis; IEA:Ensembl.
GO; GO:0045766; P:positive regulation of angiogenesis; IMP:UniProtKB.
GO; GO:0061036; P:positive regulation of cartilage development; IEA:Ensembl.
GO; GO:2000049; P:positive regulation of cell-cell adhesion mediated by cadherin; IEA:Ensembl.
GO; GO:0045080; P:positive regulation of chemokine biosynthetic process; IMP:UniProtKB.
GO; GO:0002741; P:positive regulation of cytokine secretion involved in immune response; IMP:UniProtKB.
GO; GO:0045807; P:positive regulation of endocytosis; IEA:Ensembl.
GO; GO:0010595; P:positive regulation of endothelial cell migration; IMP:UniProtKB.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IMP:UniProtKB.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IDA:UniProtKB.
GO; GO:0045745; P:positive regulation of G protein-coupled receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; ISS:ARUK-UCL.
GO; GO:0050729; P:positive regulation of inflammatory response; IMP:BHF-UCL.
GO; GO:0032729; P:positive regulation of interferon-gamma production; IEA:Ensembl.
GO; GO:0050718; P:positive regulation of interleukin-1 beta secretion; IMP:BHF-UCL.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:BHF-UCL.
GO; GO:2000484; P:positive regulation of interleukin-8 secretion; IEA:Ensembl.
GO; GO:0043032; P:positive regulation of macrophage activation; IMP:BHF-UCL.
GO; GO:0060907; P:positive regulation of macrophage cytokine production; IMP:UniProtKB.
GO; GO:0045836; P:positive regulation of meiotic nuclear division; IEA:Ensembl.
GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IEA:Ensembl.
GO; GO:1901216; P:positive regulation of neuron death; ISS:ARUK-UCL.
GO; GO:0150012; P:positive regulation of neuron projection arborization; ISS:ARUK-UCL.
GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:2000052; P:positive regulation of non-canonical Wnt signaling pathway; IEA:Ensembl.
GO; GO:0045778; P:positive regulation of ossification; IMP:BHF-UCL.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IEA:Ensembl.
GO; GO:0032092; P:positive regulation of protein binding; IEA:Ensembl.
GO; GO:0045732; P:positive regulation of protein catabolic process; IGI:MGI.
GO; GO:1900020; P:positive regulation of protein kinase C activity; IMP:CACAO.
GO; GO:0090037; P:positive regulation of protein kinase C signaling; IMP:UniProtKB.
GO; GO:1902474; P:positive regulation of protein localization to synapse; TAS:ParkinsonsUK-UCL.
GO; GO:0060760; P:positive regulation of response to cytokine stimulus; IDA:UniProtKB.
GO; GO:0010820; P:positive regulation of T cell chemotaxis; IMP:UniProtKB.
GO; GO:0070245; P:positive regulation of thymocyte apoptotic process; IEA:Ensembl.
GO; GO:0051885; P:positive regulation of timing of anagen; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:1904469; P:positive regulation of tumor necrosis factor secretion; ISS:ARUK-UCL.
GO; GO:0060340; P:positive regulation of type I interferon-mediated signaling pathway; IDA:BHF-UCL.
GO; GO:0036342; P:post-anal tail morphogenesis; IEA:Ensembl.
GO; GO:0099068; P:postsynapse assembly; TAS:ParkinsonsUK-UCL.
GO; GO:0099054; P:presynapse assembly; TAS:ParkinsonsUK-UCL.
GO; GO:0090009; P:primitive streak formation; IEA:Ensembl.
GO; GO:0060762; P:regulation of branching involved in mammary gland duct morphogenesis; IEA:Ensembl.
GO; GO:1903827; P:regulation of cellular protein localization; IEA:Ensembl.
GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; ISS:ARUK-UCL.
GO; GO:0050727; P:regulation of inflammatory response; NAS:ARUK-UCL.
GO; GO:0099175; P:regulation of postsynapse organization; IDA:SynGO.
GO; GO:0099566; P:regulation of postsynaptic cytosolic calcium ion concentration; IDA:SynGO.
GO; GO:0050807; P:regulation of synapse organization; IDA:SynGO.
GO; GO:0010033; P:response to organic substance; IEP:UniProtKB.
GO; GO:0062009; P:secondary palate development; IMP:BHF-UCL.
GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
GO; GO:0003323; P:type B pancreatic cell development; IEA:Ensembl.
GO; GO:0060157; P:urinary bladder development; IEA:Ensembl.
GO; GO:0060065; P:uterus development; IEA:Ensembl.
GO; GO:0060068; P:vagina development; IEA:Ensembl.
GO; GO:0016055; P:Wnt signaling pathway; IDA:BHF-UCL.
GO; GO:1904953; P:Wnt signaling pathway involved in midbrain dopaminergic neuron differentiation; NAS:ParkinsonsUK-UCL.
GO; GO:0007223; P:Wnt signaling pathway, calcium modulating pathway; IDA:BHF-UCL.
GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:ParkinsonsUK-UCL.
GO; GO:0042060; P:wound healing; IDA:UniProtKB.
InterPro; IPR005817; Wnt.
InterPro; IPR026538; Wnt5a.
InterPro; IPR018161; Wnt_CS.
PANTHER; PTHR12027; PTHR12027; 1.
PANTHER; PTHR12027:SF33; PTHR12027:SF33; 1.
Pfam; PF00110; wnt; 1.
SMART; SM00097; WNT1; 1.
PROSITE; PS00246; WNT1; 1.
1: Evidence at protein level;
Alternative splicing; Chondrogenesis; Complete proteome;
Developmental protein; Differentiation; Disease mutation;
Disulfide bond; Dwarfism; Extracellular matrix; Glycoprotein;
Lipoprotein; Reference proteome; Secreted; Signal;
Wnt signaling pathway.
SIGNAL 1 35 {ECO:0000255}.
PROPEP 36 61 {ECO:0000250}.
CHAIN 62 380 Protein Wnt-5a.
LIPID 244 244 O-palmitoleoyl serine; by PORCN.
CARBOHYD 114 114 N-linked (GlcNAc...) asparagine.
CARBOHYD 120 120 N-linked (GlcNAc...) asparagine.
CARBOHYD 312 312 N-linked (GlcNAc...) asparagine.
CARBOHYD 326 326 N-linked (GlcNAc...) asparagine.
DISULFID 104 115 {ECO:0000250|UniProtKB:P28026}.
DISULFID 154 162 {ECO:0000250|UniProtKB:P28026}.
DISULFID 164 182 {ECO:0000250|UniProtKB:P28026}.
DISULFID 238 252 {ECO:0000250|UniProtKB:P28026}.
DISULFID 240 247 {ECO:0000250|UniProtKB:P28026}.
DISULFID 309 340 {ECO:0000250|UniProtKB:P28026}.
DISULFID 325 335 {ECO:0000250|UniProtKB:P28026}.
DISULFID 339 379 {ECO:0000250|UniProtKB:P28026}.
DISULFID 355 370 {ECO:0000250|UniProtKB:P28026}.
DISULFID 357 367 {ECO:0000250|UniProtKB:P28026}.
DISULFID 362 363 {ECO:0000250|UniProtKB:P28026}.
VAR_SEQ 1 15 Missing (in isoform 2).
VARIANT 83 83 C -> S (in DRS1; hypomorphic mutation;
VARIANT 182 182 C -> R (in DRS1; hypomorphic mutation;
SEQUENCE 380 AA; 42339 MW; 50E73AC7FE96C7B5 CRC64;

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