WN10B_HUMAN
ID WN10B_HUMAN Reviewed; 389 AA.
AC O00744; B2R7A5; O00747; Q4VAJ4; Q4VAJ5; Q8WZ97;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Protein Wnt-10b;
DE AltName: Full=Protein Wnt-12;
DE Flags: Precursor;
GN Name=WNT10B; Synonyms=WNT12;
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).
RX PubMed=9284937; DOI=10.1159/000134597;
RA Hardiman G., Kastelein R.A., Bazan J.F.;
RT "Isolation, characterization and chromosomal localization of human
RT WNT10B.";
RL Cytogenet. Cell Genet. 77:278-282(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=11713588; DOI=10.3892/ijo.19.6.1187;
RA Saitoh T., Kirikoshi H., Mine T., Katoh M.;
RT "Proto-oncogene WNT10B is up-regulated by tumor necrosis factor alpha in
RT human gastric cancer cell line MKN45.";
RL Int. J. Oncol. 19:1187-1192(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 45-347 (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=9121776; DOI=10.1038/sj.onc.1200936;
RA Bui T.D., Rankin J., Smith K., Huguet E.L., Ruben S., Strachan T.,
RA Harris A.L., Lindsay S.;
RT "A novel human Wnt gene, WNT10B, maps to 12q13 and is expressed in human
RT breast carcinomas.";
RL Oncogene 14:1249-1253(1997).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 253-368.
RC TISSUE=Placenta;
RX PubMed=9441749; DOI=10.1006/geno.1997.5041;
RA Bergstein I., Eisenberg L.M., Bhalerao J., Jenkins N.A., Copeland N.G.,
RA Osborne M.P., Bowcock A.M., Brown A.M.C.;
RT "Isolation of two novel WNT genes, WNT14 and WNT15, one of which (WNT15) is
RT closely linked to WNT3 on human chromosome 17q21.";
RL Genomics 46:450-458(1997).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-46, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP REVIEW ON FUNCTION.
RX PubMed=21447090; DOI=10.1111/j.1748-1716.2011.02296.x;
RA Wend P., Wend K., Krum S.A., Miranda-Carboni G.A.;
RT "The role of WNT10B in physiology and disease.";
RL Acta Physiol. 204:34-51(2012).
RN [11]
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 [12]
RP VARIANTS TYR-77; TYR-256; THR-285 AND SER-301, ASSOCIATION OF VARIANT
RP TYR-256 WITH OBESITY, AND FUNCTION.
RX PubMed=16477437; DOI=10.1007/s00125-006-0144-4;
RA Christodoulides C., Scarda A., Granzotto M., Milan G., Dalla Nora E.,
RA Keogh J., De Pergola G., Stirling H., Pannacciulli N., Sethi J.K.,
RA Federspil G., Vidal-Puig A., Farooqi I.S., O'Rahilly S., Vettor R.;
RT "WNT10B mutations in human obesity.";
RL Diabetologia 49:678-684(2006).
RN [13]
RP VARIANT SHFM6 TRP-332.
RX PubMed=18515319; DOI=10.1093/hmg/ddn164;
RA Ugur S.A., Tolun A.;
RT "Homozygous WNT10b mutation and complex inheritance in Split-Hand/Foot
RT Malformation.";
RL Hum. Mol. Genet. 17:2644-2653(2008).
RN [14]
RP INVOLVEMENT IN STHAG8, VARIANT STHAG8 GLN-211, CHARACTERIZATION OF VARIANT
RP STHAG8 GLN-211, AND FUNCTION.
RX PubMed=27321946; DOI=10.1016/j.ajhg.2016.05.012;
RA Yu P., Yang W., Han D., Wang X., Guo S., Li J., Li F., Zhang X., Wong S.W.,
RA Bai B., Liu Y., Du J., Sun Z.S., Shi S., Feng H., Cai T.;
RT "Mutations in WNT10B are identified in individuals with oligodontia.";
RL Am. J. Hum. Genet. 99:195-201(2016).
CC -!- FUNCTION: Member of the Wnt ligand gene family that encodes for
CC secreted proteins, which activate the Wnt signaling cascade.
CC Specifically activates canonical Wnt/beta-catenin signaling and thus
CC triggers beta-catenin/LEF/TCF-mediated transcriptional programs.
CC Involved in signaling networks controlling stemness, pluripotency and
CC cell fate decisions. Acts in the immune system, mammary gland, adipose
CC tissue, bone and skin. {ECO:0000305|PubMed:16477437,
CC ECO:0000305|PubMed:21447090, ECO:0000305|PubMed:27321946}.
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).
CC -!- INTERACTION:
CC O00744; P05067: APP; NbExp=3; IntAct=EBI-21797207, EBI-77613;
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=O00744-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O00744-2; Sequence=VSP_056289, VSP_056290;
CC -!- TISSUE SPECIFICITY: Detected in most adult tissues. Highest levels were
CC found in heart and skeletal muscle. Low levels are found in brain.
CC -!- DEVELOPMENTAL STAGE: Infant brain has higher levels of WNT10B than
CC adult brain.
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: Split-hand/foot malformation 6 (SHFM6) [MIM:225300]: A limb
CC malformation involving the central rays of the autopod and presenting
CC with syndactyly, median clefts of the hands and feet, and aplasia
CC and/or hypoplasia of the phalanges, metacarpals, and metatarsals. Some
CC patients have been found to have intellectual disability, ectodermal
CC and craniofacial findings, and orofacial clefting.
CC {ECO:0000269|PubMed:18515319}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Tooth agenesis, selective, 8 (STHAG8) [MIM:617073]: A form of
CC selective tooth agenesis, a common anomaly characterized by the
CC congenital absence of one or more teeth. Selective tooth agenesis
CC without associated systemic disorders has sometimes been divided into 2
CC types: oligodontia, defined as agenesis of 6 or more permanent teeth,
CC and hypodontia, defined as agenesis of less than 6 teeth. The number in
CC both cases does not include absence of third molars (wisdom teeth).
CC STHAG8 inheritance is autosomal dominant.
CC {ECO:0000269|PubMed:27321946}. Note=The disease is caused by variants
CC affecting the gene represented in this entry. Potential genotype-
CC phenotype correlation between variants and the positions of missing
CC teeth. {ECO:0000269|PubMed:27321946}.
CC -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000305}.
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DR EMBL; U81787; AAB51685.1; -; mRNA.
DR EMBL; AB070724; BAB72181.1; -; mRNA.
DR EMBL; AK312906; BAG35752.1; -; mRNA.
DR EMBL; AC073610; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471111; EAW58028.1; -; Genomic_DNA.
DR EMBL; BC096353; AAH96353.1; -; mRNA.
DR EMBL; BC096354; AAH96354.1; -; mRNA.
DR EMBL; BC096355; AAH96355.1; -; mRNA.
DR EMBL; BC096356; AAH96356.1; -; mRNA.
DR EMBL; X97057; CAA65769.1; -; mRNA.
DR EMBL; AF028700; AAC39549.1; -; Genomic_DNA.
DR CCDS; CCDS8775.1; -. [O00744-1]
DR RefSeq; NP_003385.2; NM_003394.3. [O00744-1]
DR AlphaFoldDB; O00744; -.
DR SMR; O00744; -.
DR BioGRID; 113317; 30.
DR IntAct; O00744; 7.
DR STRING; 9606.ENSP00000301061; -.
DR GlyGen; O00744; 2 sites.
DR iPTMnet; O00744; -.
DR PhosphoSitePlus; O00744; -.
DR SwissPalm; O00744; -.
DR BioMuta; WNT10B; -.
DR jPOST; O00744; -.
DR MassIVE; O00744; -.
DR PaxDb; O00744; -.
DR PeptideAtlas; O00744; -.
DR PRIDE; O00744; -.
DR ProteomicsDB; 48012; -. [O00744-1]
DR ProteomicsDB; 62286; -.
DR Antibodypedia; 25755; 238 antibodies from 34 providers.
DR DNASU; 7480; -.
DR Ensembl; ENST00000301061.9; ENSP00000301061.4; ENSG00000169884.14. [O00744-1]
DR Ensembl; ENST00000407467.5; ENSP00000384691.1; ENSG00000169884.14. [O00744-2]
DR GeneID; 7480; -.
DR KEGG; hsa:7480; -.
DR MANE-Select; ENST00000301061.9; ENSP00000301061.4; NM_003394.4; NP_003385.2.
DR UCSC; uc001rss.4; human. [O00744-1]
DR CTD; 7480; -.
DR DisGeNET; 7480; -.
DR GeneCards; WNT10B; -.
DR HGNC; HGNC:12775; WNT10B.
DR HPA; ENSG00000169884; Tissue enriched (brain).
DR MalaCards; WNT10B; -.
DR MIM; 225300; phenotype.
DR MIM; 601906; gene.
DR MIM; 617073; phenotype.
DR neXtProt; NX_O00744; -.
DR OpenTargets; ENSG00000169884; -.
DR Orphanet; 2440; Isolated split hand-split foot malformation.
DR Orphanet; 99798; Oligodontia.
DR PharmGKB; PA37377; -.
DR VEuPathDB; HostDB:ENSG00000169884; -.
DR eggNOG; KOG3913; Eukaryota.
DR GeneTree; ENSGT00940000160653; -.
DR HOGENOM; CLU_033039_1_3_1; -.
DR InParanoid; O00744; -.
DR OMA; GHNVLQQ; -.
DR OrthoDB; 1241694at2759; -.
DR PhylomeDB; O00744; -.
DR TreeFam; TF105310; -.
DR PathwayCommons; O00744; -.
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-381340; Transcriptional regulation of white adipocyte differentiation.
DR SignaLink; O00744; -.
DR SIGNOR; O00744; -.
DR BioGRID-ORCS; 7480; 7 hits in 1077 CRISPR screens.
DR GeneWiki; WNT10B; -.
DR GenomeRNAi; 7480; -.
DR Pharos; O00744; Tbio.
DR PRO; PR:O00744; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; O00744; protein.
DR Bgee; ENSG00000169884; Expressed in orbitofrontal cortex and 153 other tissues.
DR ExpressionAtlas; O00744; baseline and differential.
DR Genevisible; O00744; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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; IC:BHF-UCL.
DR GO; GO:0060346; P:bone trabecula formation; IEA:Ensembl.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:BHF-UCL.
DR GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
DR GO; GO:0071374; P:cellular response to parathyroid hormone stimulus; IEA:Ensembl.
DR GO; GO:0071300; P:cellular response to retinoic acid; ISS:UniProtKB.
DR GO; GO:0002062; P:chondrocyte differentiation; IEP:UniProtKB.
DR GO; GO:0030855; P:epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0045444; P:fat cell differentiation; IEA:Ensembl.
DR GO; GO:0061196; P:fungiform papilla development; IEA:Ensembl.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0071425; P:hematopoietic stem cell proliferation; IDA:BHF-UCL.
DR GO; GO:0006629; P:lipid metabolic process; IEA:Ensembl.
DR GO; GO:0048627; P:myoblast development; IEA:Ensembl.
DR GO; GO:0014835; P:myoblast differentiation involved in skeletal muscle regeneration; IEA:Ensembl.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IDA:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0030182; P:neuron differentiation; ISS:UniProtKB.
DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:BHF-UCL.
DR GO; GO:0030501; P:positive regulation of bone mineralization; IEA:Ensembl.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IEA:Ensembl.
DR GO; GO:0030858; P:positive regulation of epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:1902035; P:positive regulation of hematopoietic stem cell proliferation; IEA:Ensembl.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0045899; P:positive regulation of RNA polymerase II transcription preinitiation complex assembly; IEA:Ensembl.
DR GO; GO:0045582; P:positive regulation of T cell differentiation; IEA:Ensembl.
DR GO; GO:0051885; P:positive regulation of timing of anagen; IEA:Ensembl.
DR GO; GO:0050821; P:protein stabilization; IDA:BHF-UCL.
DR GO; GO:0032434; P:regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:0048641; P:regulation of skeletal muscle tissue development; IEA:Ensembl.
DR GO; GO:0050909; P:sensory perception of taste; IEA:Ensembl.
DR GO; GO:0048741; P:skeletal muscle fiber development; IEA:Ensembl.
DR GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl.
DR GO; GO:0030217; P:T cell differentiation; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR Gene3D; 3.30.2460.20; -; 1.
DR InterPro; IPR005817; Wnt.
DR InterPro; IPR013302; Wnt10.
DR InterPro; IPR043158; Wnt_C.
DR InterPro; IPR018161; Wnt_CS.
DR PANTHER; PTHR12027; PTHR12027; 1.
DR Pfam; PF00110; wnt; 1.
DR PRINTS; PR01893; WNT10PROTEIN.
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 Phosphoprotein; Reference proteome; Secreted; Signal;
KW Wnt signaling pathway.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..389
FT /note="Protein Wnt-10b"
FT /id="PRO_0000041463"
FT REGION 171..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 46
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT LIPID 253
FT /note="O-palmitoleoyl serine; by PORCN"
FT /evidence="ECO:0000250|UniProtKB:P56704"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 83..94
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 136..144
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 146..199
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 247..261
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 249..256
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 318..349
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 334..344
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 348..388
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 364..379
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 366..376
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 371..372
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT VAR_SEQ 172..191
FT /note="SFPHSLPSPGPGSSPSPGPQ -> LPGTSRHECESTTTGWGARW (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056289"
FT VAR_SEQ 192..389
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056290"
FT VARIANT 77
FT /note="H -> Y (in dbSNP:rs151284263)"
FT /evidence="ECO:0000269|PubMed:16477437"
FT /id="VAR_062512"
FT VARIANT 211
FT /note="R -> Q (in STHAG8; reduced activation of Wnt
FT signaling; reduced endothelial differentiation;
FT dbSNP:rs779326570)"
FT /evidence="ECO:0000269|PubMed:27321946"
FT /id="VAR_076926"
FT VARIANT 256
FT /note="C -> Y (associated with obesity; abrogates the
FT ability of WNT10B to activate canonical Wnt signaling and
FT blocks adipogenesis)"
FT /evidence="ECO:0000269|PubMed:16477437"
FT /id="VAR_062513"
FT VARIANT 285
FT /note="I -> T (in dbSNP:rs146010731)"
FT /evidence="ECO:0000269|PubMed:16477437"
FT /id="VAR_062514"
FT VARIANT 301
FT /note="P -> S (in dbSNP:rs35034312)"
FT /evidence="ECO:0000269|PubMed:16477437"
FT /id="VAR_062515"
FT VARIANT 332
FT /note="R -> W (in SHFM6; dbSNP:rs121918349)"
FT /evidence="ECO:0000269|PubMed:18515319"
FT /id="VAR_062516"
FT CONFLICT 60
FT /note="G -> D (in Ref. 1; AAB51685)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="K -> R (in Ref. 7; CAA65769)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="F -> S (in Ref. 7; CAA65769)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="F -> L (in Ref. 7; CAA65769)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 389 AA; 43000 MW; F973F2CA0DB115EF CRC64;
MLEEPRPRPP PSGLAGLLFL ALCSRALSNE ILGLKLPGEP PLTANTVCLT LSGLSKRQLG
LCLRNPDVTA SALQGLHIAV HECQHQLRDQ RWNCSALEGG GRLPHHSAIL KRGFRESAFS
FSMLAAGVMH AVATACSLGK LVSCGCGWKG SGEQDRLRAK LLQLQALSRG KSFPHSLPSP
GPGSSPSPGP QDTWEWGGCN HDMDFGEKFS RDFLDSREAP RDIQARMRIH NNRVGRQVVT
ENLKRKCKCH GTSGSCQFKT CWRAAPEFRA VGAALRERLG RAIFIDTHNR NSGAFQPRLR
PRRLSGELVY FEKSPDFCER DPTMGSPGTR GRACNKTSRL LDGCGSLCCG RGHNVLRQTR
VERCHCRFHW CCYVLCDECK VTEWVNVCK
