WNT11_HUMAN
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 03-AUG-2022, entry version 172.
DE RecName: Full=Protein Wnt-11;
DE Flags: Precursor;
GN Name=WNT11;
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 [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; DOI=10.3892/ijmm.8.6.651;
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., 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 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 project:
RT 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 regions of
CC tissues. Is likely to signal over only few cell diameters.
CC -!- INTERACTION:
CC O96014; O95273: CCNDBP1; NbExp=3; IntAct=EBI-8058160, EBI-748961;
CC O96014; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-8058160, EBI-3867333;
CC O96014; Q9BTY2: FUCA2; NbExp=3; IntAct=EBI-8058160, EBI-9050116;
CC O96014; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-8058160, EBI-11959885;
CC O96014; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-8058160, EBI-11749135;
CC O96014; Q9BYS1: KRTAP1-5; NbExp=3; IntAct=EBI-8058160, EBI-11741292;
CC O96014; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-8058160, EBI-10172290;
CC O96014; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-8058160, EBI-10171774;
CC O96014; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-8058160, EBI-10172052;
CC O96014; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-8058160, EBI-11953334;
CC O96014; Q9BYP8: KRTAP17-1; NbExp=5; IntAct=EBI-8058160, EBI-11988175;
CC O96014; Q6L8G8: KRTAP5-7; NbExp=3; IntAct=EBI-8058160, EBI-11987425;
CC O96014; O75690: KRTAP5-8; NbExp=3; IntAct=EBI-8058160, EBI-12134621;
CC O96014; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-8058160, EBI-3958099;
CC O96014; Q9BYQ3: KRTAP9-3; NbExp=3; IntAct=EBI-8058160, EBI-1043191;
CC O96014; Q99750: MDFI; NbExp=9; IntAct=EBI-8058160, EBI-724076;
CC O96014; A6NK89: RASSF10; NbExp=3; IntAct=EBI-8058160, EBI-6912267;
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. {ECO:0000269|PubMed:11712081}.
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 -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000305}.
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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 AlphaFoldDB; O96014; -.
DR SMR; O96014; -.
DR BioGRID; 113318; 28.
DR IntAct; O96014; 21.
DR MINT; O96014; -.
DR STRING; 9606.ENSP00000325526; -.
DR GlyGen; O96014; 5 sites.
DR iPTMnet; O96014; -.
DR PhosphoSitePlus; O96014; -.
DR BioMuta; WNT11; -.
DR jPOST; O96014; -.
DR MassIVE; O96014; -.
DR PaxDb; O96014; -.
DR PeptideAtlas; O96014; -.
DR PRIDE; O96014; -.
DR ProteomicsDB; 51196; -.
DR Antibodypedia; 31189; 143 antibodies from 31 providers.
DR DNASU; 7481; -.
DR Ensembl; ENST00000322563.8; ENSP00000325526.3; ENSG00000085741.14.
DR GeneID; 7481; -.
DR KEGG; hsa:7481; -.
DR MANE-Select; ENST00000322563.8; ENSP00000325526.3; NM_004626.3; NP_004617.2.
DR UCSC; uc001oxe.4; human.
DR CTD; 7481; -.
DR DisGeNET; 7481; -.
DR GeneCards; WNT11; -.
DR HGNC; HGNC:12776; WNT11.
DR HPA; ENSG00000085741; Tissue enhanced (adipose).
DR MIM; 603699; gene.
DR neXtProt; NX_O96014; -.
DR OpenTargets; ENSG00000085741; -.
DR PharmGKB; PA37378; -.
DR VEuPathDB; HostDB:ENSG00000085741; -.
DR eggNOG; KOG3913; Eukaryota.
DR GeneTree; ENSGT00940000158413; -.
DR HOGENOM; CLU_033039_1_0_1; -.
DR InParanoid; O96014; -.
DR OMA; CKLLPGM; -.
DR OrthoDB; 797177at2759; -.
DR PhylomeDB; O96014; -.
DR TreeFam; TF105310; -.
DR PathwayCommons; O96014; -.
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 SignaLink; O96014; -.
DR SIGNOR; O96014; -.
DR BioGRID-ORCS; 7481; 8 hits in 1068 CRISPR screens.
DR GeneWiki; WNT11; -.
DR GenomeRNAi; 7481; -.
DR Pharos; O96014; Tbio.
DR PRO; PR:O96014; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; O96014; protein.
DR Bgee; ENSG00000085741; Expressed in omental fat pad and 109 other tissues.
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:0005125; F:cytokine activity; 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:0030325; P:adrenal gland development; IEP:UniProtKB.
DR GO; GO:0048844; P:artery morphogenesis; IEA:Ensembl.
DR GO; GO:0003283; P:atrial septum development; 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; IBA:GO_Central.
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:1904019; P:epithelial cell apoptotic process; IEA:Ensembl.
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:0010463; P:mesenchymal cell proliferation; 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:2000647; P:negative regulation of stem 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:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
DR GO; GO:1904037; P:positive regulation of epithelial cell apoptotic process; IEA:Ensembl.
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:0090082; P:positive regulation of heart induction by negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
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:0003138; P:primary heart field specification; 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:0003139; P:secondary heart field specification; 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:0072089; P:stem cell proliferation; 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:0007223; P:Wnt signaling pathway, calcium modulating pathway; NAS:ParkinsonsUK-UCL.
DR GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; NAS:ParkinsonsUK-UCL.
DR Gene3D; 3.30.2460.20; -; 1.
DR InterPro; IPR005817; Wnt.
DR InterPro; IPR026536; Wnt-11.
DR InterPro; IPR043158; Wnt_C.
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 Developmental protein; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Lipoprotein; Reference proteome; Secreted; Signal; Wnt signaling pathway.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..354
FT /note="Protein Wnt-11"
FT /id="PRO_0000041465"
FT LIPID 215
FT /note="O-palmitoleoyl serine; by PORCN"
FT /evidence="ECO:0000250|UniProtKB:P56704"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 80..91
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 130..138
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 140..157
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 209..223
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 211..218
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 283..314
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 299..309
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 313..353
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 329..344
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 331..341
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 336..337
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT CONFLICT 121
FT /note="A -> T (in Ref. 1; CAA74159/CAA73223)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="G -> R (in Ref. 1; CAA74159/CAA73223)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="S -> W (in Ref. 1; CAA74159/CAA73223)"
FT /evidence="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
