WNT5B_HUMAN
ID WNT5B_HUMAN Reviewed; 359 AA.
AC Q9H1J7; A8K315; D3DUP9; Q96S49; Q9BV04;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Protein Wnt-5b;
DE Flags: Precursor;
GN Name=WNT5B;
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].
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].
RX PubMed=11445850; DOI=10.3892/ijo.19.2.347;
RA Saitoh T., Katoh M.;
RT "Molecular cloning and characterization of human WNT5B on chromosome
RT 12p13.3 region.";
RL Int. J. Oncol. 19:347-351(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 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle;
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PORCN. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
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; AY009399; AAG38659.1; -; mRNA.
DR EMBL; AB060966; BAB62039.1; -; mRNA.
DR EMBL; AK290430; BAF83119.1; -; mRNA.
DR EMBL; CH471116; EAW88925.1; -; Genomic_DNA.
DR EMBL; CH471116; EAW88927.1; -; Genomic_DNA.
DR EMBL; BC001749; AAH01749.1; -; mRNA.
DR CCDS; CCDS8510.1; -.
DR RefSeq; NP_110402.2; NM_030775.2.
DR RefSeq; NP_116031.1; NM_032642.2.
DR AlphaFoldDB; Q9H1J7; -.
DR SMR; Q9H1J7; -.
DR BioGRID; 123348; 3.
DR IntAct; Q9H1J7; 4.
DR STRING; 9606.ENSP00000380379; -.
DR GlyGen; Q9H1J7; 4 sites.
DR iPTMnet; Q9H1J7; -.
DR PhosphoSitePlus; Q9H1J7; -.
DR BioMuta; WNT5B; -.
DR DMDM; 20532427; -.
DR jPOST; Q9H1J7; -.
DR MassIVE; Q9H1J7; -.
DR MaxQB; Q9H1J7; -.
DR PaxDb; Q9H1J7; -.
DR PeptideAtlas; Q9H1J7; -.
DR PRIDE; Q9H1J7; -.
DR ProteomicsDB; 80420; -.
DR Antibodypedia; 10357; 249 antibodies from 30 providers.
DR DNASU; 81029; -.
DR Ensembl; ENST00000310594.7; ENSP00000308887.3; ENSG00000111186.13.
DR Ensembl; ENST00000397196.7; ENSP00000380379.2; ENSG00000111186.13.
DR Ensembl; ENST00000537031.5; ENSP00000439312.1; ENSG00000111186.13.
DR GeneID; 81029; -.
DR KEGG; hsa:81029; -.
DR MANE-Select; ENST00000397196.7; ENSP00000380379.2; NM_032642.3; NP_116031.1.
DR UCSC; uc001qjj.4; human.
DR CTD; 81029; -.
DR DisGeNET; 81029; -.
DR GeneCards; WNT5B; -.
DR HGNC; HGNC:16265; WNT5B.
DR HPA; ENSG00000111186; Tissue enhanced (prostate).
DR MIM; 606361; gene.
DR neXtProt; NX_Q9H1J7; -.
DR OpenTargets; ENSG00000111186; -.
DR PharmGKB; PA38104; -.
DR VEuPathDB; HostDB:ENSG00000111186; -.
DR eggNOG; KOG3913; Eukaryota.
DR GeneTree; ENSGT00940000157617; -.
DR HOGENOM; CLU_033039_0_1_1; -.
DR InParanoid; Q9H1J7; -.
DR OMA; EHARMLM; -.
DR OrthoDB; 695671at2759; -.
DR PhylomeDB; Q9H1J7; -.
DR TreeFam; TF105310; -.
DR PathwayCommons; Q9H1J7; -.
DR Reactome; R-HSA-3238698; WNT ligand biogenesis and trafficking.
DR Reactome; R-HSA-4086400; PCP/CE pathway.
DR SignaLink; Q9H1J7; -.
DR SIGNOR; Q9H1J7; -.
DR BioGRID-ORCS; 81029; 15 hits in 1079 CRISPR screens.
DR ChiTaRS; WNT5B; human.
DR GeneWiki; WNT5B; -.
DR GenomeRNAi; 81029; -.
DR Pharos; Q9H1J7; Tbio.
DR PRO; PR:Q9H1J7; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9H1J7; protein.
DR Bgee; ENSG00000111186; Expressed in stromal cell of endometrium and 112 other tissues.
DR ExpressionAtlas; Q9H1J7; baseline and differential.
DR Genevisible; Q9H1J7; HS.
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; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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:0005102; F:signaling receptor binding; IPI:UniProtKB.
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:0071300; P:cellular response to retinoic acid; ISS:UniProtKB.
DR GO; GO:0002062; P:chondrocyte differentiation; IEP:UniProtKB.
DR GO; GO:0045444; P:fat cell differentiation; NAS:UniProtKB.
DR GO; GO:0070307; P:lens fiber cell development; ISS:BHF-UCL.
DR GO; GO:0042692; P:muscle cell differentiation; ISS:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
DR GO; GO:1904105; P:positive regulation of convergent extension involved in gastrulation; ISS:UniProtKB.
DR GO; GO:2000052; P:positive regulation of non-canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR Gene3D; 3.30.2460.20; -; 1.
DR InterPro; IPR005817; Wnt.
DR InterPro; IPR026537; Wnt5b.
DR InterPro; IPR043158; Wnt_C.
DR InterPro; IPR018161; Wnt_CS.
DR PANTHER; PTHR12027; PTHR12027; 1.
DR PANTHER; PTHR12027:SF87; PTHR12027:SF87; 1.
DR Pfam; PF00110; wnt; 1.
DR PRINTS; PR01349; WNTPROTEIN.
DR SMART; SM00097; WNT1; 1.
DR PROSITE; PS00246; WNT1; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Lipoprotein; Reference proteome; Secreted; Signal; Wnt signaling pathway.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..359
FT /note="Protein Wnt-5b"
FT /id="PRO_0000041434"
FT LIPID 223
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 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 83..94
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 133..141
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 143..161
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 217..231
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 219..226
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 288..319
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 304..314
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 318..358
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 334..349
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 336..346
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 341..342
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT CONFLICT 73
FT /note="G -> R (in Ref. 1; AAG38659)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="R -> P (in Ref. 1; AAG38659)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="N -> K (in Ref. 1; AAG38659)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="R -> S (in Ref. 1; AAG38659)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="G -> R (in Ref. 1; AAG38659)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="S -> R (in Ref. 1; AAG38659)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 359 AA; 40323 MW; 6E35EE2B0AF1FD29 CRC64;
MPSLLLLFTA ALLSSWAQLL TDANSWWSLA LNPVQRPEMF IIGAQPVCSQ LPGLSPGQRK
LCQLYQEHMA YIGEGAKTGI KECQHQFRQR RWNCSTADNA SVFGRVMQIG SRETAFTHAV
SAAGVVNAIS RACREGELST CGCSRTARPK DLPRDWLWGG CGDNVEYGYR FAKEFVDARE
REKNFAKGSE EQGRVLMNLQ NNEAGRRAVY KMADVACKCH GVSGSCSLKT CWLQLAEFRK
VGDRLKEKYD SAAAMRVTRK GRLELVNSRF TQPTPEDLVY VDPSPDYCLR NESTGSLGTQ
GRLCNKTSEG MDGCELMCCG RGYNQFKSVQ VERCHCKFHW CCFVRCKKCT EIVDQYICK
