WNT4_HUMAN
ID WNT4_HUMAN Reviewed; 351 AA.
AC P56705; B4DJF9; Q5TZQ0; Q96T81; Q9BXF5; Q9H1J8; Q9UJM2;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2002, sequence version 4.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Protein Wnt-4;
DE Flags: Precursor;
GN Name=WNT4; ORFNames=UNQ426/PRO864;
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 1).
RA Testa T.T., Mossakowska D.E., Carter P.S., Hu E., Zhu Y., Kelsell D.P.,
RA Murdock P.R., Herrity N.C., Lewis C.J., Cross D.A., Culbert A.A.,
RA Reith A.D., Barnes M.R.;
RT "Molecular cloning and characterization of six novel human WNT genes.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=11283799; DOI=10.1086/320125;
RA Jordan B.K., Mohammed M., Ching S.T., Delot E., Chen X.N., Dewing P.,
RA Swain A., Rao P.N., Elejalde B.R., Vilain E.;
RT "Up-regulation of wnt-4 signaling and dosage-sensitive sex reversal in
RT humans.";
RL Am. J. Hum. Genet. 68:1102-1109(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Subthalamic nucleus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 210-329 (ISOFORM 1/2).
RC TISSUE=Mammary gland;
RX PubMed=8168088;
RA Huguet E.L., McMahon J.A., McMahon A.P., Bicknell R., Harris A.L.;
RT "Differential expression of human Wnt genes 2, 3, 4, and 7B in human breast
RT cell lines and normal and disease states of human breast tissue.";
RL Cancer Res. 54:2615-2621(1994).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
RA Peltoketo H., Heikkila M., Vainio S.;
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
RA Sim U.E., Smith A., Szilagi E., Ioannou P., Lindsay M.H., Little M.H.;
RT "Expression of Wnt-4 can be regulated by the Wilms' tumor suppressor gene,
RT WT1.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [11]
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 [12]
RP VARIANT MULLAPL GLY-216, AND CHARACTERIZATION OF VARIANT MULLAPL GLY-216.
RX PubMed=15317892; DOI=10.1056/nejmoa040533;
RA Biason-Lauber A., Konrad D., Navratil F., Schoenle E.J.;
RT "A WNT4 mutation associated with Muellerian-duct regression and
RT virilization in a 46,XX woman.";
RL N. Engl. J. Med. 351:792-798(2004).
RN [13]
RP VARIANT MULLAPL CYS-83, AND CHARACTERIZATION OF VARIANT MULLAPL CYS-83.
RX PubMed=16959810; DOI=10.1093/humrep/del360;
RA Biason-Lauber A., De Filippo G., Konrad D., Scarano G., Nazzaro A.,
RA Schoenle E.J.;
RT "WNT4 deficiency-a clinical phenotype distinct from the classic Mayer-
RT Rokitansky-Kuster-Hauser syndrome: a case report.";
RL Hum. Reprod. 22:224-229(2007).
RN [14]
RP VARIANT SERKAL VAL-114, AND CHARACTERIZATION OF VARIANT SERKAL VAL-114.
RX PubMed=18179883; DOI=10.1016/j.ajhg.2007.08.005;
RA Mandel H., Shemer R., Borochowitz Z.U., Okopnik M., Knopf C., Indelman M.,
RA Drugan A., Tiosano D., Gershoni-Baruch R., Choder M., Sprecher E.;
RT "SERKAL syndrome: an autosomal-recessive disorder caused by a loss-of-
RT function mutation in WNT4.";
RL Am. J. Hum. Genet. 82:39-47(2008).
RN [15]
RP VARIANT MULLAPL PRO-12, AND CHARACTERIZATION OF VARIANT MULLAPL PRO-12.
RX PubMed=18182450; DOI=10.1210/jc.2007-2023;
RA Philibert P., Biason-Lauber A., Rouzier R., Pienkowski C., Paris F.,
RA Konrad D., Schoenle E., Sultan C.;
RT "Identification and functional analysis of a new WNT4 gene mutation among
RT 28 adolescent girls with primary amenorrhea and Muellerian duct
RT abnormalities: a French collaborative study.";
RL J. Clin. Endocrinol. Metab. 93:895-900(2008).
CC -!- FUNCTION: Ligand for members of the frizzled family of seven
CC transmembrane receptors (Probable). Plays an important role in the
CC embryonic development of the urogenital tract and the lung
CC (PubMed:15317892, PubMed:16959810, PubMed:18179883, PubMed:18182450).
CC Required for normal mesenchyme to epithelium transition during
CC embryonic kidney development. Required for the formation of early
CC epithelial renal vesicles during kidney development (By similarity).
CC Required for normal formation of the Mullerian duct in females, and
CC normal levels of oocytes in the ovaries (PubMed:15317892,
CC PubMed:16959810, PubMed:18182450). Required for normal down-regulation
CC of 3 beta-hydroxysteroid dehydrogenase in the ovary (PubMed:15317892,
CC PubMed:16959810, PubMed:18182450). Required for normal lung development
CC and for normal patterning of trachael cartilage rings (By similarity).
CC {ECO:0000250|UniProtKB:P22724, ECO:0000269|PubMed:15317892,
CC ECO:0000269|PubMed:16959810, ECO:0000269|PubMed:18179883,
CC ECO:0000269|PubMed:18182450, ECO:0000305}.
CC -!- SUBUNIT: Interacts with PORCN (By similarity). Interacts with PKD1
CC (PubMed:27214281). {ECO:0000250|UniProtKB:P22724,
CC ECO:0000269|PubMed:27214281}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P56705-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P56705-2; Sequence=VSP_054017;
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 -!- DISEASE: 46,XX sex reversal with dysgenesis of kidneys, adrenals, and
CC lungs (SERKAL) [MIM:611812]: A disease characterized by the association
CC of female-to-male sex reversal with dysgenesis of kidneys, adrenals,
CC and lungs. {ECO:0000269|PubMed:18179883}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- DISEASE: Mullerian aplasia and hyperandrogenism (MULLAPL) [MIM:158330]:
CC A disorder of sex development. Affected females manifest dysgenesis of
CC Mullerian duct derivatives absent or rudimentary uterus and vagina,
CC functional ovaries, primary amenorrhea, hyperandrogenism and hirsutism.
CC {ECO:0000269|PubMed:15317892, ECO:0000269|PubMed:16959810,
CC ECO:0000269|PubMed:18182450}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY009398; AAG38658.1; -; mRNA.
DR EMBL; AF316543; AAK51699.1; -; mRNA.
DR EMBL; AY358947; AAQ89306.1; -; mRNA.
DR EMBL; AK296058; BAG58821.1; -; mRNA.
DR EMBL; BT020125; AAV38928.1; -; mRNA.
DR EMBL; AL031281; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL445253; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC057781; AAH57781.1; -; mRNA.
DR EMBL; AF335591; AAK25765.1; -; Genomic_DNA.
DR EMBL; AH010731; AAK50427.1; -; Genomic_DNA.
DR CCDS; CCDS223.1; -. [P56705-1]
DR RefSeq; NP_110388.2; NM_030761.4. [P56705-1]
DR RefSeq; XP_011539900.1; XM_011541598.2. [P56705-2]
DR AlphaFoldDB; P56705; -.
DR SMR; P56705; -.
DR BioGRID; 119939; 85.
DR IntAct; P56705; 15.
DR STRING; 9606.ENSP00000290167; -.
DR GlyGen; P56705; 2 sites.
DR iPTMnet; P56705; -.
DR PhosphoSitePlus; P56705; -.
DR BioMuta; WNT4; -.
DR DMDM; 20532425; -.
DR MassIVE; P56705; -.
DR PaxDb; P56705; -.
DR PeptideAtlas; P56705; -.
DR PRIDE; P56705; -.
DR ProteomicsDB; 4376; -.
DR ProteomicsDB; 56938; -. [P56705-1]
DR Antibodypedia; 2555; 498 antibodies from 36 providers.
DR DNASU; 54361; -.
DR Ensembl; ENST00000290167.11; ENSP00000290167.5; ENSG00000162552.15. [P56705-1]
DR GeneID; 54361; -.
DR KEGG; hsa:54361; -.
DR MANE-Select; ENST00000290167.11; ENSP00000290167.5; NM_030761.5; NP_110388.2.
DR UCSC; uc001bfs.5; human. [P56705-1]
DR CTD; 54361; -.
DR DisGeNET; 54361; -.
DR GeneCards; WNT4; -.
DR HGNC; HGNC:12783; WNT4.
DR HPA; ENSG00000162552; Tissue enhanced (skin).
DR MalaCards; WNT4; -.
DR MIM; 158330; phenotype.
DR MIM; 603490; gene.
DR MIM; 611812; phenotype.
DR neXtProt; NX_P56705; -.
DR OpenTargets; ENSG00000162552; -.
DR Orphanet; 247768; Muellerian aplasia and hyperandrogenism.
DR Orphanet; 139466; SERKAL syndrome.
DR PharmGKB; PA37384; -.
DR VEuPathDB; HostDB:ENSG00000162552; -.
DR eggNOG; KOG3913; Eukaryota.
DR GeneTree; ENSGT00940000159654; -.
DR HOGENOM; CLU_033039_1_0_1; -.
DR InParanoid; P56705; -.
DR OMA; CWRAMPP; -.
DR OrthoDB; 745245at2759; -.
DR PhylomeDB; P56705; -.
DR TreeFam; TF105310; -.
DR PathwayCommons; P56705; -.
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-4086400; PCP/CE pathway.
DR SignaLink; P56705; -.
DR SIGNOR; P56705; -.
DR BioGRID-ORCS; 54361; 11 hits in 1069 CRISPR screens.
DR ChiTaRS; WNT4; human.
DR GeneWiki; WNT4; -.
DR GenomeRNAi; 54361; -.
DR Pharos; P56705; Tbio.
DR PRO; PR:P56705; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P56705; protein.
DR Bgee; ENSG00000162552; Expressed in islet of Langerhans and 103 other tissues.
DR ExpressionAtlas; P56705; baseline and differential.
DR Genevisible; P56705; HS.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
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:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR GO; GO:0005109; F:frizzled binding; IBA:GO_Central.
DR GO; GO:0048018; F:receptor ligand activity; IDA:BHF-UCL.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR GO; GO:0030325; P:adrenal gland development; IEP:UniProtKB.
DR GO; GO:0097190; P:apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IEA:Ensembl.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:UniProtKB.
DR GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR GO; GO:0009267; P:cellular response to starvation; IEA:Ensembl.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEP:UniProtKB.
DR GO; GO:0001838; P:embryonic epithelial tube formation; IEA:Ensembl.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; IEP:UniProtKB.
DR GO; GO:0008585; P:female gonad development; IEA:Ensembl.
DR GO; GO:0030237; P:female sex determination; IMP:UniProtKB.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0042445; P:hormone metabolic process; IEA:Ensembl.
DR GO; GO:0033080; P:immature T cell proliferation in thymus; IEA:Ensembl.
DR GO; GO:0001822; P:kidney development; IEP:UniProtKB.
DR GO; GO:0001889; P:liver development; IEP:UniProtKB.
DR GO; GO:0008584; P:male gonad development; IMP:UniProtKB.
DR GO; GO:0061180; P:mammary gland epithelium development; IEP:UniProtKB.
DR GO; GO:0140013; P:meiotic nuclear division; IEA:Ensembl.
DR GO; GO:0060231; P:mesenchymal to epithelial transition; IEA:Ensembl.
DR GO; GO:0072162; P:metanephric mesenchymal cell differentiation; NAS:UniProtKB.
DR GO; GO:0072273; P:metanephric nephron morphogenesis; IEA:Ensembl.
DR GO; GO:0072174; P:metanephric tubule formation; IEA:Ensembl.
DR GO; GO:2000180; P:negative regulation of androgen biosynthetic process; IDA:UniProtKB.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0045596; P:negative regulation of cell differentiation; IEA:Ensembl.
DR GO; GO:0030336; P:negative regulation of cell migration; IEA:Ensembl.
DR GO; GO:0040037; P:negative regulation of fibroblast growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:UniProtKB.
DR GO; GO:2000019; P:negative regulation of male gonad development; IMP:UniProtKB.
DR GO; GO:0010894; P:negative regulation of steroid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0061369; P:negative regulation of testicular blood vessel morphogenesis; IMP:UniProtKB.
DR GO; GO:2000225; P:negative regulation of testosterone biosynthetic process; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0061045; P:negative regulation of wound healing; IEA:Ensembl.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0038030; P:non-canonical Wnt signaling pathway via MAPK cascade; IDA:BHF-UCL.
DR GO; GO:0048599; P:oocyte development; IEA:Ensembl.
DR GO; GO:0061205; P:paramesonephric duct development; IMP:UniProtKB.
DR GO; GO:1904238; P:pericyte cell differentiation; IEA:Ensembl.
DR GO; GO:0032349; P:positive regulation of aldosterone biosynthetic process; IDA:UniProtKB.
DR GO; GO:0030501; P:positive regulation of bone mineralization; IDA:BHF-UCL.
DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IDA:BHF-UCL.
DR GO; GO:2000066; P:positive regulation of cortisol biosynthetic process; IDA:UniProtKB.
DR GO; GO:0061184; P:positive regulation of dermatome development; IDA:BHF-UCL.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; IEA:Ensembl.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:Ensembl.
DR GO; GO:0045836; P:positive regulation of meiotic nuclear division; IEA:Ensembl.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IDA:BHF-UCL.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0022407; P:regulation of cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0072033; P:renal vesicle formation; IEA:Ensembl.
DR GO; GO:0072034; P:renal vesicle induction; IEA:Ensembl.
DR GO; GO:0060008; P:Sertoli cell differentiation; IEA:Ensembl.
DR GO; GO:0051145; P:smooth muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0060126; P:somatotropin secreting cell differentiation; IEA:Ensembl.
DR GO; GO:0060748; P:tertiary branching involved in mammary gland duct morphogenesis; IEA:Ensembl.
DR GO; GO:0060129; P:thyroid-stimulating hormone-secreting cell differentiation; IEA:Ensembl.
DR Gene3D; 3.30.2460.20; -; 1.
DR InterPro; IPR005817; Wnt.
DR InterPro; IPR009142; Wnt4.
DR InterPro; IPR043158; Wnt_C.
DR InterPro; IPR018161; Wnt_CS.
DR PANTHER; PTHR12027; PTHR12027; 1.
DR Pfam; PF00110; wnt; 1.
DR PRINTS; PR01844; WNT4PROTEIN.
DR PRINTS; PR01349; WNTPROTEIN.
DR SMART; SM00097; WNT1; 1.
DR PROSITE; PS00246; WNT1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Disease variant;
KW Disulfide bond; Extracellular matrix; Glycoprotein; Lipoprotein;
KW Reference proteome; Secreted; Signal; Wnt signaling pathway.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..351
FT /note="Protein Wnt-4"
FT /id="PRO_0000041421"
FT LIPID 212
FT /note="O-palmitoleoyl serine; by PORCN"
FT /evidence="ECO:0000250|UniProtKB:P56704"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 78..89
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 128..136
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 138..155
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 206..220
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 208..215
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 280..311
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 296..306
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 310..350
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 326..341
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 328..338
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 333..334
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT VAR_SEQ 1..55
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054017"
FT VARIANT 12
FT /note="L -> P (in MULLAPL; unable to suppress
FT steroidogenesis in an ovarian adenocarcinoma cell line
FT resulting in increased androgen production;
FT dbSNP:rs121908653)"
FT /evidence="ECO:0000269|PubMed:18182450"
FT /id="VAR_043497"
FT VARIANT 83
FT /note="R -> C (in MULLAPL; with androgen excess, normal
FT kidney size and location; unable to suppress expression of
FT steroidogenic enzymes in ovarian; impairs protein
FT secretion)"
FT /evidence="ECO:0000269|PubMed:16959810"
FT /id="VAR_043498"
FT VARIANT 114
FT /note="A -> V (in SERKAL; reduced transcript levels;
FT dbSNP:rs121908651)"
FT /evidence="ECO:0000269|PubMed:18179883"
FT /id="VAR_043499"
FT VARIANT 216
FT /note="E -> G (in MULLAPL; unable to suppress expression of
FT steroidogenic enzymes in ovarian and adrenal cell lines;
FT dbSNP:rs121908650)"
FT /evidence="ECO:0000269|PubMed:15317892"
FT /id="VAR_034703"
FT VARIANT 277
FT /note="P -> L (in dbSNP:rs34228276)"
FT /id="VAR_052955"
FT CONFLICT 106
FT /note="T -> I (in Ref. 1; AAG38658)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="F -> L (in Ref. 1; AAG38658)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 351 AA; 39052 MW; 465D08755C992DA8 CRC64;
MSPRSCLRSL RLLVFAVFSA AASNWLYLAK LSSVGSISEE ETCEKLKGLI QRQVQMCKRN
LEVMDSVRRG AQLAIEECQY QFRNRRWNCS TLDSLPVFGK VVTQGTREAA FVYAISSAGV
AFAVTRACSS GELEKCGCDR TVHGVSPQGF QWSGCSDNIA YGVAFSQSFV DVRERSKGAS
SSRALMNLHN NEAGRKAILT HMRVECKCHG VSGSCEVKTC WRAVPPFRQV GHALKEKFDG
ATEVEPRRVG SSRALVPRNA QFKPHTDEDL VYLEPSPDFC EQDMRSGVLG TRGRTCNKTS
KAIDGCELLC CGRGFHTAQV ELAERCSCKF HWCCFVKCRQ CQRLVELHTC R
