ID WNT11_HUMAN Reviewed; 354 AA. AC O96014; B2R8Z6; Q14DE8; Q8WZ98; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2002, sequence version 2. DT 13-FEB-2019, entry version 155. DE RecName: Full=Protein Wnt-11; DE Flags: Precursor; GN Name=WNT11; 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 [GENOMIC DNA / MRNA]. RX PubMed=9757009; DOI=10.1016/S0378-1119(98)00393-X; RA Lako M., Strachan T., Bullen P., Wilson D.I., Robson S.C., Lindsay S.; RT "Isolation, characterisation and embryonic expression of WNT11, a gene RT which maps to 11q13.5 and has possible roles in the development of RT skeleton, kidney and lung."; RL Gene 219:101-110(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RX PubMed=11712081; RA Kirikoshi H., Sekihara H., Katoh M.; RT "Molecular cloning and characterization of human WNT11."; RL Int. J. Mol. Med. 8:651-656(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 MRNA]. RC TISSUE=Colon, and Fetal brain; 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). CC -!- FUNCTION: Ligand for members of the frizzled family of seven CC transmembrane receptors. Probable developmental protein. May be a CC signaling molecule which affects the development of discrete CC regions of tissues. Is likely to signal over only few cell CC diameters. CC -!- INTERACTION: CC P60409:KRTAP10-7; NbExp=3; IntAct=EBI-8058160, EBI-10172290; CC P60411:KRTAP10-9; NbExp=3; IntAct=EBI-8058160, EBI-10172052; CC Q99750:MDFI; NbExp=5; IntAct=EBI-8058160, EBI-724076; CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix. CC -!- TISSUE SPECIFICITY: Expressed in fetal lung, kidney, adult heart, CC liver, skeletal muscle, and pancreas. CC {ECO:0000269|PubMed:11712081}. 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 -!- 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; Y13843; CAA74159.1; -; Genomic_DNA. DR EMBL; Y13844; CAA74159.1; JOINED; Genomic_DNA. DR EMBL; Y13845; CAA74159.1; JOINED; Genomic_DNA. DR EMBL; Y13846; CAA74159.1; JOINED; Genomic_DNA. DR EMBL; Y13847; CAA74159.1; JOINED; Genomic_DNA. DR EMBL; Y12692; CAA73223.1; -; mRNA. DR EMBL; AB070218; BAB72099.1; -; mRNA. DR EMBL; AK313570; BAG36343.1; -; mRNA. DR EMBL; BC074790; AAH74790.1; -; mRNA. DR EMBL; BC074791; AAH74791.1; -; mRNA. DR EMBL; BC113386; AAI13387.1; -; mRNA. DR EMBL; BC113388; AAI13389.1; -; mRNA. DR CCDS; CCDS8242.1; -. DR RefSeq; NP_004617.2; NM_004626.2. DR RefSeq; XP_005274288.1; XM_005274231.1. DR UniGene; Hs.108219; -. DR ProteinModelPortal; O96014; -. DR SMR; O96014; -. DR BioGrid; 113318; 9. DR IntAct; O96014; 17. DR MINT; O96014; -. DR STRING; 9606.ENSP00000325526; -. DR iPTMnet; O96014; -. DR PhosphoSitePlus; O96014; -. DR BioMuta; WNT11; -. DR jPOST; O96014; -. DR PaxDb; O96014; -. DR PeptideAtlas; O96014; -. DR PRIDE; O96014; -. DR ProteomicsDB; 51196; -. DR DNASU; 7481; -. DR Ensembl; ENST00000322563; ENSP00000325526; ENSG00000085741. DR GeneID; 7481; -. DR KEGG; hsa:7481; -. DR UCSC; uc001oxe.4; human. DR CTD; 7481; -. DR DisGeNET; 7481; -. DR EuPathDB; HostDB:ENSG00000085741.12; -. DR GeneCards; WNT11; -. DR HGNC; HGNC:12776; WNT11. DR HPA; HPA050101; -. DR HPA; HPA063569; -. DR MIM; 603699; gene. DR neXtProt; NX_O96014; -. DR OpenTargets; ENSG00000085741; -. DR PharmGKB; PA37378; -. DR eggNOG; KOG3913; Eukaryota. DR eggNOG; ENOG410XQZ1; LUCA. DR GeneTree; ENSGT00940000158413; -. DR HOGENOM; HOG000039529; -. DR HOVERGEN; HBG001595; -. DR InParanoid; O96014; -. DR KO; K01384; -. DR OMA; QCNKTSH; -. DR OrthoDB; 797177at2759; -. DR PhylomeDB; O96014; -. 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-4086398; Ca2+ pathway. DR Reactome; R-HSA-4086400; PCP/CE pathway. DR SIGNOR; O96014; -. DR GeneWiki; WNT11; -. DR GenomeRNAi; 7481; -. DR PRO; PR:O96014; -. DR Proteomes; UP000005640; Chromosome 11. DR Bgee; ENSG00000085741; Expressed in 122 organ(s), highest expression level in left adrenal gland. DR ExpressionAtlas; O96014; baseline and differential. DR Genevisible; O96014; HS. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. 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; IBA:GO_Central. DR GO; GO:0005109; F:frizzled binding; IBA:GO_Central. DR GO; GO:0005096; F:GTPase activator activity; IMP:UniProtKB. DR GO; GO:0030295; F:protein kinase activator activity; IMP:UniProtKB. DR GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB. DR GO; GO:0030325; P:adrenal gland development; IEP:UniProtKB. DR GO; GO:0048844; P:artery morphogenesis; IEA:Ensembl. DR GO; GO:0070830; P:bicellular tight junction assembly; IEA:Ensembl. DR GO; GO:0030282; P:bone mineralization; IEA:Ensembl. DR GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl. DR GO; GO:0045165; P:cell fate commitment; IBA:GO_Central. DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl. DR GO; GO:0071300; P:cellular response to retinoic acid; ISS:UniProtKB. DR GO; GO:0060197; P:cloacal septation; IEP:UniProtKB. DR GO; GO:0060028; P:convergent extension involved in axis elongation; IEA:Ensembl. DR GO; GO:0048706; P:embryonic skeletal system development; IEP:UniProtKB. DR GO; GO:0001837; P:epithelial to mesenchymal transition; IEA:Ensembl. DR GO; GO:0060484; P:lung-associated mesenchyme development; IEP:UniProtKB. DR GO; GO:0045199; P:maintenance of epithelial cell apical/basal polarity; IEA:Ensembl. DR GO; GO:0072177; P:mesonephric duct development; IEP:UniProtKB. DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB. DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:UniProtKB. DR GO; GO:0061037; P:negative regulation of cartilage development; NAS:UniProtKB. DR GO; GO:0060548; P:negative regulation of cell death; IMP:UniProtKB. DR GO; GO:0030308; P:negative regulation of cell growth; IMP:UniProtKB. DR GO; GO:0030336; P:negative regulation of cell migration; IMP:UniProtKB. DR GO; GO:0090272; P:negative regulation of fibroblast growth factor production; IEA:Ensembl. DR GO; GO:0072201; P:negative regulation of mesenchymal cell proliferation; IEA:Ensembl. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB. DR GO; GO:0061101; P:neuroendocrine cell differentiation; IMP:UniProtKB. DR GO; GO:0030182; P:neuron differentiation; ISS:UniProtKB. DR GO; GO:0048570; P:notochord morphogenesis; IEA:Ensembl. DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl. DR GO; GO:0003151; P:outflow tract morphogenesis; IEA:Ensembl. DR GO; GO:0048341; P:paraxial mesoderm formation; IEA:Ensembl. DR GO; GO:0003402; P:planar cell polarity pathway involved in axis elongation; IEA:Ensembl. DR GO; GO:0060775; P:planar cell polarity pathway involved in gastrula mediolateral intercalation; IEA:Ensembl. DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl. DR GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB. DR GO; GO:0043547; P:positive regulation of GTPase activity; IMP:UniProtKB. DR GO; GO:0090037; P:positive regulation of protein kinase C signaling; IMP:UniProtKB. DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IMP:UniProtKB. DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB. DR GO; GO:0032915; P:positive regulation of transforming growth factor beta2 production; IEA:Ensembl. DR GO; GO:0034394; P:protein localization to cell surface; IMP:UniProtKB. DR GO; GO:0006468; P:protein phosphorylation; IMP:UniProtKB. DR GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl. DR GO; GO:0062009; P:secondary palate development; IMP:BHF-UCL. DR GO; GO:0061053; P:somite development; IEA:Ensembl. DR GO; GO:0060675; P:ureteric bud morphogenesis; IEP:UniProtKB. DR GO; GO:0060412; P:ventricular septum morphogenesis; IEA:Ensembl. DR GO; GO:0016055; P:Wnt signaling pathway; IBA:GO_Central. DR GO; GO:0007223; P:Wnt signaling pathway, calcium modulating pathway; NAS:ParkinsonsUK-UCL. DR GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:Reactome. DR InterPro; IPR005817; Wnt. DR InterPro; IPR026536; Wnt-11. DR InterPro; IPR018161; Wnt_CS. DR PANTHER; PTHR12027; PTHR12027; 1. DR PANTHER; PTHR12027:SF7; PTHR12027:SF7; 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 Complete proteome; Developmental protein; Disulfide bond; KW Extracellular matrix; Glycoprotein; Lipoprotein; Reference proteome; KW Secreted; Signal; Wnt signaling pathway. FT SIGNAL 1 24 {ECO:0000255}. FT CHAIN 25 354 Protein Wnt-11. FT /FTId=PRO_0000041465. FT LIPID 215 215 O-palmitoleoyl serine; by PORCN. FT {ECO:0000250|UniProtKB:P56704}. FT CARBOHYD 40 40 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 90 90 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 160 160 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 300 300 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 304 304 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 80 91 {ECO:0000250|UniProtKB:P28026}. FT DISULFID 130 138 {ECO:0000250|UniProtKB:P28026}. FT DISULFID 140 157 {ECO:0000250|UniProtKB:P28026}. FT DISULFID 209 223 {ECO:0000250|UniProtKB:P28026}. FT DISULFID 211 218 {ECO:0000250|UniProtKB:P28026}. FT DISULFID 283 314 {ECO:0000250|UniProtKB:P28026}. FT DISULFID 299 309 {ECO:0000250|UniProtKB:P28026}. FT DISULFID 313 353 {ECO:0000250|UniProtKB:P28026}. FT DISULFID 329 344 {ECO:0000250|UniProtKB:P28026}. FT DISULFID 331 341 {ECO:0000250|UniProtKB:P28026}. FT DISULFID 336 337 {ECO:0000250|UniProtKB:P28026}. FT CONFLICT 121 121 A -> T (in Ref. 1; CAA74159/CAA73223). FT {ECO:0000305}. FT CONFLICT 156 156 G -> R (in Ref. 1; CAA74159/CAA73223). FT {ECO:0000305}. FT CONFLICT 271 271 S -> W (in Ref. 1; CAA74159/CAA73223). FT {ECO:0000305}. SQ SEQUENCE 354 AA; 39179 MW; 0E29717C98541DBB CRC64; MRARPQVCEA LLFALALQTG VCYGIKWLAL SKTPSALALN QTQHCKQLEG LVSAQVQLCR SNLELMHTVV HAAREVMKAC RRAFADMRWN CSSIELAPNY LLDLERGTRE SAFVYALSAA AISHAIARAC TSGDLPGCSC GPVPGEPPGP GNRWGGCADN LSYGLLMGAK FSDAPMKVKK TGSQANKLMR LHNSEVGRQA LRASLEMKCK CHGVSGSCSI RTCWKGLQEL QDVAADLKTR YLSATKVVHR PMGTRKHLVP KDLDIRPVKD SELVYLQSSP DFCMKNEKVG SHGTQDRQCN KTSNGSDSCD LMCCGRGYNP YTDRVVERCH CKYHWCCYVT CRRCERTVER YVCK //