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   27-MAR-2024, entry version 182.
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   GlyCosmos; Q9H1J7; 4 sites, No reported glycans.
DR   GlyGen; Q9H1J7; 6 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q9H1J7; -.
DR   PhosphoSitePlus; Q9H1J7; -.
DR   BioMuta; WNT5B; -.
DR   DMDM; 20532427; -.
DR   jPOST; Q9H1J7; -.
DR   MassIVE; Q9H1J7; -.
DR   MaxQB; Q9H1J7; -.
DR   PaxDb; 9606-ENSP00000380379; -.
DR   PeptideAtlas; Q9H1J7; -.
DR   ProteomicsDB; 80420; -.
DR   Pumba; Q9H1J7; -.
DR   Antibodypedia; 10357; 276 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   AGR; HGNC:16265; -.
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; RSKVTCK; -.
DR   OrthoDB; 2874082at2759; -.
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; 23 hits in 1159 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 114 other cell types or tissues.
DR   ExpressionAtlas; Q9H1J7; baseline and differential.
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   CDD; cd19348; Wnt_Wnt5b; 1.
DR   Gene3D; 3.30.2460.20; -; 1.
DR   InterPro; IPR005817; Wnt.
DR   InterPro; IPR043158; Wnt_C.
DR   InterPro; IPR018161; Wnt_CS.
DR   PANTHER; PTHR12027:SF87; PROTEIN WNT-5B; 1.
DR   PANTHER; PTHR12027; WNT RELATED; 1.
DR   Pfam; PF00110; wnt; 1.
DR   PRINTS; PR01349; WNTPROTEIN.
DR   SMART; SM00097; WNT1; 1.
DR   PROSITE; PS00246; WNT1; 1.
DR   Genevisible; Q9H1J7; HS.
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
//