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 13-FEB-2019, entry version 161. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=9284937; 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; RA Saitoh T., Kirikoshi H., Mine T., Katoh M.; RT "Proto-oncogene WNT10B is up-regulated by tumor necrosis factor alpha RT in 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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., RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., RA 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., RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., RA 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., RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., RA Kucherlapati R., Weinstock G., 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RT project: 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 RT human 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., RA Copeland N.G., Osborne M.P., Bowcock A.M., Brown A.M.C.; RT "Isolation of two novel WNT genes, WNT14 and WNT15, one of which RT (WNT15) is 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 RP BY 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 RT by a 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 RP VARIANT 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., RA Wong S.W., 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 CC thus triggers beta-catenin/LEF/TCF-mediated transcriptional CC programs. Involved in signaling networks controlling stemness, CC pluripotency and cell fate decisions. Acts in the immune system, CC mammary gland, adipose tissue, bone and skin. CC {ECO:0000305|PubMed:16477437, ECO:0000305|PubMed:21447090, CC 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 CC physiological form in body fluids (PubMed:26902720). 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 Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Detected in most adult tissues. Highest levels CC were found in heart and skeletal muscle. Low levels are found in CC brain. CC -!- DEVELOPMENTAL STAGE: Infant brain has higher levels of WNT10B than CC adult brain. CC -!- PTM: Palmitoleoylation is required for efficient binding to CC frizzled receptors. Depalmitoleoylation leads to Wnt signaling CC pathway inhibition. {ECO:0000250|UniProtKB:P27467, CC ECO:0000250|UniProtKB:P56704}. CC -!- DISEASE: Split-hand/foot malformation 6 (SHFM6) [MIM:225300]: A CC limb malformation involving the central rays of the autopod and CC presenting with syndactyly, median clefts of the hands and feet, CC and aplasia and/or hypoplasia of the phalanges, metacarpals, and CC metatarsals. Some patients have been found to have mental CC retardation, ectodermal and craniofacial findings, and orofacial CC clefting. {ECO:0000269|PubMed:18515319}. Note=The disease is CC caused by mutations affecting the gene represented in this entry. CC -!- DISEASE: Tooth agenesis, selective, 8 (STHAG8) [MIM:617073]: A CC form of selective tooth agenesis, a common anomaly characterized CC by the congenital absence of one or more teeth. Selective tooth CC agenesis without associated systemic disorders has sometimes been CC divided into 2 types: oligodontia, defined as agenesis of 6 or CC more permanent teeth, and hypodontia, defined as agenesis of less CC than 6 teeth. The number in both cases does not include absence of CC third molars (wisdom teeth). STHAG8 inheritance is autosomal CC dominant. {ECO:0000269|PubMed:27321946}. Note=The disease is CC caused by mutations affecting the gene represented in this entry. CC Potential genotype-phenotype correlation between variants and the CC positions of missing teeth. {ECO:0000269|PubMed:27321946}. 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; 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 UniGene; Hs.91985; -. DR ProteinModelPortal; O00744; -. DR BioGrid; 113317; 7. DR STRING; 9606.ENSP00000301061; -. DR iPTMnet; O00744; -. DR PhosphoSitePlus; O00744; -. DR SwissPalm; O00744; -. DR BioMuta; WNT10B; -. DR EPD; O00744; -. DR jPOST; O00744; -. DR PaxDb; O00744; -. DR PeptideAtlas; O00744; -. DR PRIDE; O00744; -. DR ProteomicsDB; 48012; -. DR DNASU; 7480; -. DR Ensembl; ENST00000301061; ENSP00000301061; ENSG00000169884. [O00744-1] DR Ensembl; ENST00000407467; ENSP00000384691; ENSG00000169884. [O00744-2] DR GeneID; 7480; -. DR KEGG; hsa:7480; -. DR UCSC; uc001rss.4; human. [O00744-1] DR CTD; 7480; -. DR DisGeNET; 7480; -. DR EuPathDB; HostDB:ENSG00000169884.13; -. DR GeneCards; WNT10B; -. DR HGNC; HGNC:12775; WNT10B. DR HPA; HPA055048; -. DR HPA; HPA062539; -. 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 eggNOG; KOG3913; Eukaryota. DR eggNOG; ENOG410XQZ1; LUCA. DR GeneTree; ENSGT00940000160653; -. DR HOGENOM; HOG000039528; -. DR HOVERGEN; HBG083446; -. DR InParanoid; O00744; -. DR KO; K01357; -. DR OMA; SYSTDSC; -. DR OrthoDB; 1241694at2759; -. DR PhylomeDB; O00744; -. DR TreeFam; TF105310; -. 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 GeneWiki; WNT10B; -. DR GenomeRNAi; 7480; -. DR PRO; PR:O00744; -. DR Proteomes; UP000005640; Chromosome 12. DR Bgee; ENSG00000169884; Expressed in 193 organ(s), highest expression level in cingulate cortex. 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: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:0007050; P:cell cycle arrest; IEA:Ensembl. 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: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: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: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:0008284; P:positive regulation of cell population proliferation; 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:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl. DR GO; GO:0045899; P:positive regulation of RNA polymerase II transcriptional preinitiation complex assembly; 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:0016055; P:Wnt signaling pathway; IBA:GO_Central. DR InterPro; IPR005817; Wnt. DR InterPro; IPR013302; Wnt10. 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; Complete proteome; Developmental protein; KW Disease mutation; Disulfide bond; Extracellular matrix; Glycoprotein; KW Lipoprotein; Phosphoprotein; Polymorphism; Reference proteome; KW Secreted; Signal; Wnt signaling pathway. FT SIGNAL 1 28 {ECO:0000255}. FT CHAIN 29 389 Protein Wnt-10b. FT /FTId=PRO_0000041463. FT MOD_RES 46 46 Phosphothreonine. FT {ECO:0000244|PubMed:18669648}. FT LIPID 253 253 O-palmitoleoyl serine; by PORCN. FT {ECO:0000250|UniProtKB:P56704}. FT CARBOHYD 93 93 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 335 335 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 83 94 {ECO:0000250|UniProtKB:P28026}. FT DISULFID 136 144 {ECO:0000250|UniProtKB:P28026}. FT DISULFID 146 199 {ECO:0000250|UniProtKB:P28026}. FT DISULFID 247 261 {ECO:0000250|UniProtKB:P28026}. FT DISULFID 249 256 {ECO:0000250|UniProtKB:P28026}. FT DISULFID 318 349 {ECO:0000250|UniProtKB:P28026}. FT DISULFID 334 344 {ECO:0000250|UniProtKB:P28026}. FT DISULFID 348 388 {ECO:0000250|UniProtKB:P28026}. FT DISULFID 364 379 {ECO:0000250|UniProtKB:P28026}. FT DISULFID 366 376 {ECO:0000250|UniProtKB:P28026}. FT DISULFID 371 372 {ECO:0000250|UniProtKB:P28026}. FT VAR_SEQ 172 191 SFPHSLPSPGPGSSPSPGPQ -> LPGTSRHECESTTTGWG FT ARW (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_056289. FT VAR_SEQ 192 389 Missing (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_056290. FT VARIANT 77 77 H -> Y (in dbSNP:rs151284263). FT {ECO:0000269|PubMed:16477437}. FT /FTId=VAR_062512. FT VARIANT 211 211 R -> Q (in STHAG8; reduced activation of FT Wnt signaling; reduced endothelial FT differentiation; dbSNP:rs779326570). FT {ECO:0000269|PubMed:27321946}. FT /FTId=VAR_076926. FT VARIANT 256 256 C -> Y (associated with obesity; FT abrogates the ability of WNT10B to FT activate canonical Wnt signaling and FT blocks adipogenesis). FT {ECO:0000269|PubMed:16477437}. FT /FTId=VAR_062513. FT VARIANT 285 285 I -> T (in dbSNP:rs146010731). FT {ECO:0000269|PubMed:16477437}. FT /FTId=VAR_062514. FT VARIANT 301 301 P -> S (in dbSNP:rs35034312). FT {ECO:0000269|PubMed:16477437}. FT /FTId=VAR_062515. FT VARIANT 332 332 R -> W (in SHFM6; dbSNP:rs121918349). FT {ECO:0000269|PubMed:18515319}. FT /FTId=VAR_062516. FT CONFLICT 60 60 G -> D (in Ref. 1; AAB51685). FT {ECO:0000305}. FT CONFLICT 149 149 K -> R (in Ref. 7; CAA65769). FT {ECO:0000305}. FT CONFLICT 295 295 F -> S (in Ref. 7; CAA65769). FT {ECO:0000305}. FT CONFLICT 311 311 F -> L (in Ref. 7; CAA65769). FT {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 //