WNT5A_MOUSE
ID WNT5A_MOUSE Reviewed; 380 AA.
AC P22725; Q8BM17; Q8BMF9; Q8VCV6;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Protein Wnt-5a;
DE Flags: Precursor;
GN Name=Wnt5a; Synonyms=Wnt-5a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Embryo;
RX PubMed=2279700; DOI=10.1101/gad.4.12b.2319;
RA Gavin B.J., McMahon J.A., McMahon A.P.;
RT "Expression of multiple novel Wnt-1/int-1-related genes during fetal and
RT adult mouse development.";
RL Genes Dev. 4:2319-2332(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Testis, and Vagina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Mammary tumor;
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 PROTEIN SEQUENCE OF 62-82, AND FUNCTION.
RX PubMed=16602827; DOI=10.1371/journal.pbio.0040115;
RA Mikels A.J., Nusse R.;
RT "Purified Wnt5a protein activates or inhibits beta-catenin-TCF signaling
RT depending on receptor context.";
RL PLoS Biol. 4:E115-E115(2006).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=10021340; DOI=10.1242/dev.126.6.1211;
RA Yamaguchi T.P., Bradley A., McMahon A.P., Jones S.;
RT "A Wnt5a pathway underlies outgrowth of multiple structures in the
RT vertebrate embryo.";
RL Development 126:1211-1223(1999).
RN [7]
RP INTERACTION WITH PORCN.
RX PubMed=10866835; DOI=10.1046/j.1432-1033.2000.01478.x;
RA Tanaka K., Okabayashi H., Asashima M., Perrimon N., Kadowaki T.;
RT "The evolutionarily conserved porcupine gene family is involved in the
RT processing of the Wnt family.";
RL Eur. J. Biochem. 267:4300-4311(2000).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12952940; DOI=10.1083/jcb.200303158;
RA Topol L., Jiang X., Choi H., Garrett-Beal L., Carolan P.J., Yang Y.;
RT "Wnt-5a inhibits the canonical Wnt pathway by promoting GSK-3-independent
RT beta-catenin degradation.";
RL J. Cell Biol. 162:899-908(2003).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, PRELIMINARY CYSTEINE PALMITOYLATION,
RP GLYCOSYLATION AT ASN-114; ASN-120; ASN-312 AND ASN-326, AND MUTAGENESIS OF
RP CYS-104; ASN-114; ASN-120; ASN-312 AND ASN-326.
RX PubMed=17117926; DOI=10.1042/bj20061476;
RA Kurayoshi M., Yamamoto H., Izumi S., Kikuchi A.;
RT "Post-translational palmitoylation and glycosylation of Wnt-5a are
RT necessary for its signalling.";
RL Biochem. J. 402:515-523(2007).
RN [10]
RP INTERACTION WITH WLS.
RX PubMed=19841259; DOI=10.1073/pnas.0904894106;
RA Fu J., Jiang M., Mirando A.J., Yu H.-M., Hsu W.;
RT "Reciprocal regulation of Wnt and Gpr177/mouse Wntless is required for
RT embryonic axis formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:18598-18603(2009).
RN [11]
RP PROTEOLYTIC PROCESSING BY TIKI1 AND TIKI2, DISULFIDE BONDS, AND SUBUNIT.
RX PubMed=22726442; DOI=10.1016/j.cell.2012.04.039;
RA Zhang X., Abreu J.G., Yokota C., Macdonald B.T., Singh S., Coburn K.L.,
RA Cheong S.M., Zhang M.M., Ye Q.Z., Hang H.C., Steen H., He X.;
RT "Tiki1 is required for head formation via Wnt cleavage-oxidation and
RT inactivation.";
RL Cell 149:1565-1577(2012).
RN [12]
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).
CC -!- FUNCTION: Ligand for members of the frizzled family of seven
CC transmembrane receptors (PubMed:17117926). Can activate or inhibit
CC canonical Wnt signaling, depending on receptor context
CC (PubMed:16602827). In the presence of FZD4, activates beta-catenin
CC signaling. In the presence of ROR2, inhibits the canonical Wnt pathway
CC by promoting beta-catenin degradation through a GSK3-independent
CC pathway which involves down-regulation of beta-catenin-induced reporter
CC gene expression (PubMed:16602827). Suppression of the canonical pathway
CC allows chondrogenesis to occur and inhibits tumor formation. Stimulates
CC cell migration (PubMed:17117926). Decreases proliferation, migration,
CC invasiveness and clonogenicity of carcinoma cells and may act as a
CC tumor suppressor. Mediates motility of melanoma cells (By similarity).
CC Required during embryogenesis for extension of the primary anterior-
CC posterior axis and for outgrowth of limbs and the genital tubercle
CC (PubMed:10021340). Inhibits type II collagen expression in chondrocytes
CC (By similarity). {ECO:0000250|UniProtKB:P41221,
CC ECO:0000250|UniProtKB:Q27Q52, ECO:0000269|PubMed:10021340,
CC ECO:0000269|PubMed:12952940, ECO:0000269|PubMed:16602827,
CC ECO:0000269|PubMed:17117926}.
CC -!- SUBUNIT: Forms a soluble 1:1 complex with AFM; this prevents
CC oligomerization and is required for prolonged biological activity. The
CC complex with AFM may represent the physiological form in body fluids
CC (By similarity). Homooligomer; disulfide-linked, leading to
CC inactivation (PubMed:22726442). Interacts with PORCN (PubMed:10866835).
CC Interacts with WLS (PubMed:19841259). Interacts with glypican GCP3 (By
CC similarity). Interacts with PKD1 (via extracellular domain)
CC (PubMed:27214281). {ECO:0000250|UniProtKB:P41221,
CC ECO:0000269|PubMed:10866835, ECO:0000269|PubMed:19841259,
CC ECO:0000269|PubMed:22726442, ECO:0000269|PubMed:27214281}.
CC -!- INTERACTION:
CC P22725; O35082: Kl; NbExp=2; IntAct=EBI-1570983, EBI-1570828;
CC P22725; Q9Y5W5: WIF1; Xeno; NbExp=7; IntAct=EBI-1570983, EBI-3922719;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000305}. Secreted {ECO:0000269|PubMed:17117926}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P22725-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P22725-2; Sequence=VSP_035595;
CC -!- TISSUE SPECIFICITY: Expressed in a gradient at the caudal end of the
CC embryo during gastrulation and later in the distal-most aspect of
CC several structures that extend from the body such as the limbs and
CC genital tubercle. {ECO:0000269|PubMed:10021340}.
CC -!- PTM: Glycosylation is necessary for secretion but not for activity.
CC {ECO:0000269|PubMed:17117926}.
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:0000269|PubMed:22726442}.
CC -!- DISRUPTION PHENOTYPE: Mice display perinatal lethality and display
CC gross morphological defects in outgrowing tissues. They are truncated
CC caudally, displaying loss of the tail and a significant shortening of
CC the anterior-posterior axis. The shape of the head is abnormal with
CC truncated snout, mandible and tongue and reduced outgrowth of the
CC external ear. Fore- and hindlimbs lack digits, the genital tubercle is
CC missing and chondrocyte differentiation is inhibited.
CC {ECO:0000269|PubMed:10021340, ECO:0000269|PubMed:12952940}.
CC -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000305}.
CC -!- CAUTION: A palmitoylation site was proposed at Cys-104, but it was
CC later shown that this cysteine is engaged in a disulfide bond.
CC {ECO:0000305}.
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DR EMBL; M89798; AAA40567.1; -; mRNA.
DR EMBL; AK031512; BAC27430.1; -; mRNA.
DR EMBL; AK031597; BAC27468.1; -; mRNA.
DR EMBL; AK036824; BAC29593.1; -; mRNA.
DR EMBL; CT025649; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC018425; AAH18425.1; -; mRNA.
DR CCDS; CCDS26888.1; -. [P22725-1]
DR CCDS; CCDS56946.1; -. [P22725-2]
DR PIR; D36470; D36470.
DR RefSeq; NP_001243153.1; NM_001256224.1. [P22725-2]
DR RefSeq; NP_033550.2; NM_009524.3. [P22725-1]
DR RefSeq; XP_006518987.1; XM_006518924.2. [P22725-2]
DR RefSeq; XP_006518988.1; XM_006518925.3.
DR AlphaFoldDB; P22725; -.
DR SMR; P22725; -.
DR BioGRID; 204577; 7.
DR CORUM; P22725; -.
DR DIP; DIP-39893N; -.
DR IntAct; P22725; 8.
DR MINT; P22725; -.
DR STRING; 10090.ENSMUSP00000064878; -.
DR GlyGen; P22725; 4 sites.
DR iPTMnet; P22725; -.
DR PhosphoSitePlus; P22725; -.
DR SwissPalm; P22725; -.
DR MaxQB; P22725; -.
DR PaxDb; P22725; -.
DR PeptideAtlas; P22725; -.
DR PRIDE; P22725; -.
DR ProteomicsDB; 299772; -. [P22725-1]
DR ProteomicsDB; 299773; -. [P22725-2]
DR Antibodypedia; 31456; 592 antibodies from 39 providers.
DR DNASU; 22418; -.
DR Ensembl; ENSMUST00000063465; ENSMUSP00000064878; ENSMUSG00000021994. [P22725-1]
DR Ensembl; ENSMUST00000112272; ENSMUSP00000107891; ENSMUSG00000021994. [P22725-2]
DR GeneID; 22418; -.
DR KEGG; mmu:22418; -.
DR UCSC; uc007sug.2; mouse. [P22725-1]
DR CTD; 7474; -.
DR MGI; MGI:98958; Wnt5a.
DR VEuPathDB; HostDB:ENSMUSG00000021994; -.
DR eggNOG; KOG3913; Eukaryota.
DR GeneTree; ENSGT00940000158894; -.
DR HOGENOM; CLU_033039_0_1_1; -.
DR InParanoid; P22725; -.
DR OMA; EGELNSC; -.
DR OrthoDB; 695671at2759; -.
DR PhylomeDB; P22725; -.
DR TreeFam; TF105310; -.
DR Reactome; R-MMU-201681; TCF dependent signaling in response to WNT.
DR Reactome; R-MMU-3238698; WNT ligand biogenesis and trafficking.
DR Reactome; R-MMU-4086398; Ca2+ pathway.
DR Reactome; R-MMU-4086400; PCP/CE pathway.
DR Reactome; R-MMU-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-MMU-5099900; WNT5A-dependent internalization of FZD4.
DR Reactome; R-MMU-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 22418; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Wnt5a; mouse.
DR PRO; PR:P22725; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P22725; protein.
DR Bgee; ENSMUSG00000021994; Expressed in embryonic post-anal tail and 335 other tissues.
DR Genevisible; P22725; MM.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:1902379; F:chemoattractant activity involved in axon guidance; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005125; F:cytokine activity; IDA:BHF-UCL.
DR GO; GO:0005109; F:frizzled binding; IDA:MGI.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0005115; F:receptor tyrosine kinase-like orphan receptor binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0090630; P:activation of GTPase activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0032148; P:activation of protein kinase B activity; ISO:MGI.
DR GO; GO:0009887; P:animal organ morphogenesis; TAS:MGI.
DR GO; GO:0008595; P:anterior/posterior axis specification, embryo; IDA:BHF-UCL.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
DR GO; GO:0003283; P:atrial septum development; IGI:CACAO.
DR GO; GO:0003401; P:axis elongation; IMP:MGI.
DR GO; GO:0048846; P:axon extension involved in axon guidance; IGI:MGI.
DR GO; GO:0007411; P:axon guidance; IDA:UniProtKB.
DR GO; GO:0007413; P:axonal fasciculation; TAS:ParkinsonsUK-UCL.
DR GO; GO:0007409; P:axonogenesis; IDA:ParkinsonsUK-UCL.
DR GO; GO:0030509; P:BMP signaling pathway; IMP:MGI.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:BHF-UCL.
DR GO; GO:0051216; P:cartilage development; IEA:UniProtKB-KW.
DR GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IGI:MGI.
DR GO; GO:0008283; P:cell population proliferation; IDA:MGI.
DR GO; GO:0007267; P:cell-cell signaling; TAS:MGI.
DR GO; GO:0071277; P:cellular response to calcium ion; IEA:Ensembl.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0071219; P:cellular response to molecule of bacterial origin; IDA:BHF-UCL.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
DR GO; GO:0060067; P:cervix development; IMP:MGI.
DR GO; GO:0036517; P:chemoattraction of serotonergic neuron axon; IDA:ParkinsonsUK-UCL.
DR GO; GO:0036518; P:chemorepulsion of dopaminergic neuron axon; IDA:ParkinsonsUK-UCL.
DR GO; GO:0090103; P:cochlea morphogenesis; IMP:MGI.
DR GO; GO:0060026; P:convergent extension; IMP:MGI.
DR GO; GO:0060028; P:convergent extension involved in axis elongation; IMP:MGI.
DR GO; GO:0060029; P:convergent extension involved in organogenesis; IGI:MGI.
DR GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
DR GO; GO:0046546; P:development of primary male sexual characteristics; IMP:MGI.
DR GO; GO:0048546; P:digestive tract morphogenesis; IMP:MGI.
DR GO; GO:0071542; P:dopaminergic neuron differentiation; IDA:CACAO.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IMP:MGI.
DR GO; GO:0030326; P:embryonic limb morphogenesis; IMP:MGI.
DR GO; GO:0048706; P:embryonic skeletal system development; ISO:MGI.
DR GO; GO:0010631; P:epithelial cell migration; IMP:MGI.
DR GO; GO:0050673; P:epithelial cell proliferation; IDA:MGI.
DR GO; GO:0060750; P:epithelial cell proliferation involved in mammary gland duct elongation; IDA:MGI.
DR GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; IGI:MGI.
DR GO; GO:0001736; P:establishment of planar polarity; IMP:MGI.
DR GO; GO:0060324; P:face development; ISO:MGI.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IMP:MGI.
DR GO; GO:0048806; P:genitalia development; ISO:MGI.
DR GO; GO:0001947; P:heart looping; IGI:MGI.
DR GO; GO:0071425; P:hematopoietic stem cell proliferation; IDA:MGI.
DR GO; GO:0007442; P:hindgut morphogenesis; IMP:MGI.
DR GO; GO:0048850; P:hypophysis morphogenesis; IMP:MGI.
DR GO; GO:0042472; P:inner ear morphogenesis; IDA:MGI.
DR GO; GO:0007254; P:JNK cascade; IDA:MGI.
DR GO; GO:0030216; P:keratinocyte differentiation; IEA:Ensembl.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0060599; P:lateral sprouting involved in mammary gland duct morphogenesis; IDA:MGI.
DR GO; GO:0035108; P:limb morphogenesis; IMP:MGI.
DR GO; GO:0030324; P:lung development; IMP:MGI.
DR GO; GO:0008584; P:male gonad development; IMP:MGI.
DR GO; GO:0060744; P:mammary gland branching involved in thelarche; IDA:MGI.
DR GO; GO:0140013; P:meiotic nuclear division; IGI:MGI.
DR GO; GO:0097325; P:melanocyte proliferation; IDA:CACAO.
DR GO; GO:0010463; P:mesenchymal cell proliferation; IMP:MGI.
DR GO; GO:0060638; P:mesenchymal-epithelial cell signaling; IMP:MGI.
DR GO; GO:0060809; P:mesodermal to mesenchymal transition involved in gastrulation; IGI:MGI.
DR GO; GO:0030901; P:midbrain development; IDA:ParkinsonsUK-UCL.
DR GO; GO:1904948; P:midbrain dopaminergic neuron differentiation; IDA:ParkinsonsUK-UCL.
DR GO; GO:0007494; P:midgut development; IMP:MGI.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IMP:MGI.
DR GO; GO:0050919; P:negative chemotaxis; IGI:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0048843; P:negative regulation of axon extension involved in axon guidance; IGI:MGI.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IMP:MGI.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:ParkinsonsUK-UCL.
DR GO; GO:1904934; P:negative regulation of cell proliferation in midbrain; IMP:ParkinsonsUK-UCL.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IDA:MGI.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; ISO:MGI.
DR GO; GO:0040037; P:negative regulation of fibroblast growth factor receptor signaling pathway; IMP:MGI.
DR GO; GO:0048022; P:negative regulation of melanin biosynthetic process; IDA:CACAO.
DR GO; GO:0072201; P:negative regulation of mesenchymal cell proliferation; ISO:MGI.
DR GO; GO:0060686; P:negative regulation of prostatic bud formation; IMP:MGI.
DR GO; GO:0051964; P:negative regulation of synapse assembly; IDA:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0001843; P:neural tube closure; IGI:MGI.
DR GO; GO:0021915; P:neural tube development; IGI:MGI.
DR GO; GO:0022008; P:neurogenesis; IDA:ParkinsonsUK-UCL.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0048812; P:neuron projection morphogenesis; IDA:UniProtKB.
DR GO; GO:0035567; P:non-canonical Wnt signaling pathway; IDA:ParkinsonsUK-UCL.
DR GO; GO:0038031; P:non-canonical Wnt signaling pathway via JNK cascade; IMP:BHF-UCL.
DR GO; GO:0048570; P:notochord morphogenesis; IGI:MGI.
DR GO; GO:0021891; P:olfactory bulb interneuron development; IMP:UniProtKB.
DR GO; GO:0048341; P:paraxial mesoderm formation; IGI:MGI.
DR GO; GO:0003344; P:pericardium morphogenesis; IGI:MGI.
DR GO; GO:0003402; P:planar cell polarity pathway involved in axis elongation; IMP:MGI.
DR GO; GO:1904938; P:planar cell polarity pathway involved in axon guidance; IDA:ParkinsonsUK-UCL.
DR GO; GO:0061350; P:planar cell polarity pathway involved in cardiac muscle tissue morphogenesis; IMP:MGI.
DR GO; GO:0061349; P:planar cell polarity pathway involved in cardiac right atrium morphogenesis; IMP:MGI.
DR GO; GO:0060775; P:planar cell polarity pathway involved in gastrula mediolateral intercalation; IGI:MGI.
DR GO; GO:0090179; P:planar cell polarity pathway involved in neural tube closure; IMP:MGI.
DR GO; GO:0061347; P:planar cell polarity pathway involved in outflow tract morphogenesis; IMP:MGI.
DR GO; GO:0061354; P:planar cell polarity pathway involved in pericardium morphogenesis; IMP:MGI.
DR GO; GO:0061348; P:planar cell polarity pathway involved in ventricular septum morphogenesis; IMP:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:0061036; P:positive regulation of cartilage development; IDA:MGI.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; ISO:MGI.
DR GO; GO:2000049; P:positive regulation of cell-cell adhesion mediated by cadherin; IDA:MGI.
DR GO; GO:0032722; P:positive regulation of chemokine production; ISO:MGI.
DR GO; GO:0001819; P:positive regulation of cytokine production; IDA:MGI.
DR GO; GO:0002720; P:positive regulation of cytokine production involved in immune response; ISO:MGI.
DR GO; GO:0045807; P:positive regulation of endocytosis; IDA:MGI.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:MGI.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:MGI.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IMP:MGI.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0090082; P:positive regulation of heart induction by negative regulation of canonical Wnt signaling pathway; IGI:CACAO.
DR GO; GO:1902035; P:positive regulation of hematopoietic stem cell proliferation; IDA:MGI.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISO:MGI.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IMP:BHF-UCL.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IDA:BHF-UCL.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:BHF-UCL.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IDA:BHF-UCL.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IMP:BHF-UCL.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; IDA:MGI.
DR GO; GO:0043032; P:positive regulation of macrophage activation; ISO:MGI.
DR GO; GO:0060907; P:positive regulation of macrophage cytokine production; ISO:MGI.
DR GO; GO:0045836; P:positive regulation of meiotic nuclear division; IGI:MGI.
DR GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IMP:MGI.
DR GO; GO:1901216; P:positive regulation of neuron death; IDA:ARUK-UCL.
DR GO; GO:0150012; P:positive regulation of neuron projection arborization; IGI:ARUK-UCL.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IDA:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:2000052; P:positive regulation of non-canonical Wnt signaling pathway; IDA:CACAO.
DR GO; GO:0045778; P:positive regulation of ossification; ISO:MGI.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IGI:MGI.
DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IGI:MGI.
DR GO; GO:0032092; P:positive regulation of protein binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:MGI.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:1900020; P:positive regulation of protein kinase C activity; ISO:MGI.
DR GO; GO:0090037; P:positive regulation of protein kinase C signaling; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:ParkinsonsUK-UCL.
DR GO; GO:0060760; P:positive regulation of response to cytokine stimulus; ISO:MGI.
DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IMP:MGI.
DR GO; GO:0010820; P:positive regulation of T cell chemotaxis; ISO:MGI.
DR GO; GO:0070245; P:positive regulation of thymocyte apoptotic process; IMP:MGI.
DR GO; GO:0051885; P:positive regulation of timing of anagen; IDA:CAFA.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:ARUK-UCL.
DR GO; GO:0060340; P:positive regulation of type I interferon-mediated signaling pathway; ISO:MGI.
DR GO; GO:0036342; P:post-anal tail morphogenesis; IMP:MGI.
DR GO; GO:0003138; P:primary heart field specification; IGI:CACAO.
DR GO; GO:0090009; P:primitive streak formation; IGI:MGI.
DR GO; GO:0008104; P:protein localization; IMP:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IGI:MGI.
DR GO; GO:0060762; P:regulation of branching involved in mammary gland duct morphogenesis; IDA:MGI.
DR GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IMP:ARUK-UCL.
DR GO; GO:0099175; P:regulation of postsynapse organization; ISO:MGI.
DR GO; GO:0099566; P:regulation of postsynaptic cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0032880; P:regulation of protein localization; IDA:ParkinsonsUK-UCL.
DR GO; GO:0050807; P:regulation of synapse organization; ISO:MGI.
DR GO; GO:0003139; P:secondary heart field specification; IGI:CACAO.
DR GO; GO:0062009; P:secondary palate development; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; TAS:MGI.
DR GO; GO:0061053; P:somite development; IGI:MGI.
DR GO; GO:0001756; P:somitogenesis; IGI:MGI.
DR GO; GO:0072089; P:stem cell proliferation; IMP:MGI.
DR GO; GO:0070242; P:thymocyte apoptotic process; IMP:MGI.
DR GO; GO:0060606; P:tube closure; IMP:MGI.
DR GO; GO:0003323; P:type B pancreatic cell development; IMP:MGI.
DR GO; GO:0060157; P:urinary bladder development; IMP:MGI.
DR GO; GO:0060065; P:uterus development; IMP:MGI.
DR GO; GO:0060068; P:vagina development; IMP:MGI.
DR GO; GO:0003281; P:ventricular septum development; IGI:CACAO.
DR GO; GO:0016055; P:Wnt signaling pathway; IGI:MGI.
DR GO; GO:1904953; P:Wnt signaling pathway involved in midbrain dopaminergic neuron differentiation; IDA:ParkinsonsUK-UCL.
DR GO; GO:0007223; P:Wnt signaling pathway, calcium modulating pathway; IDA:BHF-UCL.
DR GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; IDA:MGI.
DR GO; GO:0042060; P:wound healing; ISO:MGI.
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; Direct protein sequencing; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Lipoprotein; Reference proteome;
KW Secreted; Signal; Wnt signaling pathway.
FT SIGNAL 1..37
FT /evidence="ECO:0000255"
FT PROPEP 38..61
FT /evidence="ECO:0000269|PubMed:16602827"
FT /id="PRO_0000352797"
FT CHAIN 62..380
FT /note="Protein Wnt-5a"
FT /id="PRO_0000041428"
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:0000269|PubMed:17117926"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17117926"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17117926"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17117926"
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..20
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_035595"
FT MUTAGEN 104
FT /note="C->A: No effect on secretion."
FT /evidence="ECO:0000269|PubMed:17117926"
FT MUTAGEN 114
FT /note="N->Q: Abolishes glycosylation; when associated with
FT Q-120, Q-312 and Q-326."
FT /evidence="ECO:0000269|PubMed:17117926"
FT MUTAGEN 120
FT /note="N->Q: Abolishes glycosylation; when associated with
FT Q-114, Q-312 and Q-326."
FT /evidence="ECO:0000269|PubMed:17117926"
FT MUTAGEN 312
FT /note="N->Q: Abolishes glycosylation; when associated with
FT Q-114, Q-120 and Q-326."
FT /evidence="ECO:0000269|PubMed:17117926"
FT MUTAGEN 326
FT /note="N->Q: Abolishes glycosylation; when associated with
FT Q-114, Q-120 and Q-312."
FT /evidence="ECO:0000269|PubMed:17117926"
FT CONFLICT 168
FT /note="Missing (in Ref. 1; AAA40567)"
FT /evidence="ECO:0000305"
FT CONFLICT 190..191
FT /note="YR -> HP (in Ref. 1; AAA40567)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="F -> L (in Ref. 2; BAC27430)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 380 AA; 42309 MW; 64CA36C516D22D8A CRC64;
MKKPIGILSP GVALGTAGGA MSSKFFLMAL ATFFSFAQVV 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
