WNT9B_HUMAN
ID WNT9B_HUMAN Reviewed; 357 AA.
AC O14905; Q6UXT4; Q96Q09;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Protein Wnt-9b;
DE AltName: Full=Protein Wnt-14b;
DE AltName: Full=Protein Wnt-15;
DE Flags: Precursor;
GN Name=WNT9B; Synonyms=WNT14B {ECO:0000303|PubMed:11604992}, WNT15;
GN ORFNames=UNQ6973/PRO21956;
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], AND VARIANT THR-106.
RX PubMed=11604992; DOI=10.3892/ijo.19.5.947;
RA Kirikoshi H., Sekihara H., Katoh M.;
RT "Molecular cloning and characterization of WNT14B, a novel member of the
RT WNT gene family.";
RL Int. J. Oncol. 19:947-952(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 216-335.
RX PubMed=9441749; DOI=10.1006/geno.1997.5041;
RA Bergstein I., Eisenberg L.M., Bhalerao J., Jenkins N.A., Copeland N.G.,
RA Osborne M.P., Bowcock A.M., Brown A.M.C.;
RT "Isolation of two novel WNT genes, WNT14 and WNT15, one of which (WNT15) is
RT closely linked to WNT3 on human chromosome 17q21.";
RL Genomics 46:450-458(1997).
RN [5]
RP INTERACTION WITH LRP6 IN THE WNT/FZD/LRP6 COMPLEX, AND FUNCTION.
RX PubMed=20093360; DOI=10.1074/jbc.m109.092130;
RA Bourhis E., Tam C., Franke Y., Bazan J.F., Ernst J., Hwang J., Costa M.,
RA Cochran A.G., Hannoush R.N.;
RT "Reconstitution of a frizzled8.Wnt3a.LRP6 signaling complex reveals
RT multiple Wnt and Dkk1 binding sites on LRP6.";
RL J. Biol. Chem. 285:9172-9179(2010).
RN [6]
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 by a
RT serum glycoprotein afamin/alpha-albumin.";
RL Elife 5:0-0(2016).
RN [7]
RP INTERACTION WITH PKD1.
RX PubMed=27214281; DOI=10.1038/ncb3363;
RA Kim S., Nie H., Nesin V., Tran U., Outeda P., Bai C.X., Keeling J.,
RA Maskey D., Watnick T., Wessely O., Tsiokas L.;
RT "The polycystin complex mediates Wnt/Ca(2+) signalling.";
RL Nat. Cell Biol. 18:752-764(2016).
CC -!- FUNCTION: Ligand for members of the frizzled family of seven
CC transmembrane receptors (Probable). Functions in the canonical
CC Wnt/beta-catenin signaling pathway. Required for normal embryonic
CC kidney development, and for normal development of the urogenital tract,
CC including uterus and part of the oviduct and the upper vagina in
CC females, and epididymis and vas deferens in males. Activates a
CC signaling cascade in the metanephric mesenchyme that induces
CC tubulogenesis. Acts upstream of WNT4 in the signaling pathways that
CC mediate development of kidney tubules and the Muellerian ducts. Plays a
CC role in cranofacial development and is required for normal fusion of
CC the palate during embryonic development (By similarity).
CC {ECO:0000250|UniProtKB:O35468, ECO:0000305|PubMed:20093360}.
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 physiological
CC form in body fluids (PubMed:26902720). Component of the Wnt-Fzd-LRP5-
CC LRP6 signaling complex that contains a WNT protein, a FZD protein and
CC LRP5 or LRP6. Interacts directly in the complex with LRP6
CC (PubMed:20093360). Interacts with PKD1 (via extracellular domain)
CC (PubMed:27214281). {ECO:0000269|PubMed:20093360,
CC ECO:0000269|PubMed:26902720, ECO:0000269|PubMed:27214281}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000305}. Secreted {ECO:0000269|PubMed:26902720}.
CC -!- TISSUE SPECIFICITY: Moderately expressed in fetal kidney and adult
CC kidney. Also found in brain.
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; AB063483; BAB70499.1; -; mRNA.
DR EMBL; AY358217; AAQ88584.1; -; mRNA.
DR EMBL; AC015855; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF028703; AAC39551.1; -; Genomic_DNA.
DR CCDS; CCDS11506.1; -.
DR RefSeq; NP_003387.1; NM_003396.2.
DR AlphaFoldDB; O14905; -.
DR SMR; O14905; -.
DR BioGRID; 113321; 14.
DR IntAct; O14905; 4.
DR STRING; 9606.ENSP00000290015; -.
DR GlyGen; O14905; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; O14905; -.
DR PhosphoSitePlus; O14905; -.
DR BioMuta; WNT9B; -.
DR MassIVE; O14905; -.
DR PaxDb; O14905; -.
DR PeptideAtlas; O14905; -.
DR PRIDE; O14905; -.
DR Antibodypedia; 17705; 167 antibodies from 34 providers.
DR DNASU; 7484; -.
DR Ensembl; ENST00000290015.7; ENSP00000290015.2; ENSG00000158955.11.
DR Ensembl; ENST00000613753.2; ENSP00000482127.1; ENSG00000276799.2.
DR GeneID; 7484; -.
DR KEGG; hsa:7484; -.
DR MANE-Select; ENST00000290015.7; ENSP00000290015.2; NM_003396.3; NP_003387.1.
DR UCSC; uc002ikw.2; human.
DR CTD; 7484; -.
DR DisGeNET; 7484; -.
DR GeneCards; WNT9B; -.
DR HGNC; HGNC:12779; WNT9B.
DR HPA; ENSG00000158955; Group enriched (parathyroid gland, seminal vesicle).
DR MIM; 602864; gene.
DR neXtProt; NX_O14905; -.
DR OpenTargets; ENSG00000158955; -.
DR Orphanet; 1848; Renal agenesis, bilateral.
DR PharmGKB; PA37380; -.
DR VEuPathDB; HostDB:ENSG00000158955; -.
DR eggNOG; KOG3913; Eukaryota.
DR GeneTree; ENSGT00940000158599; -.
DR HOGENOM; CLU_033039_2_0_1; -.
DR InParanoid; O14905; -.
DR OMA; RLELWVP; -.
DR OrthoDB; 866763at2759; -.
DR PhylomeDB; O14905; -.
DR TreeFam; TF105310; -.
DR PathwayCommons; O14905; -.
DR Reactome; R-HSA-3238698; WNT ligand biogenesis and trafficking.
DR Reactome; R-HSA-373080; Class B/2 (Secretin family receptors).
DR SignaLink; O14905; -.
DR SIGNOR; O14905; -.
DR BioGRID-ORCS; 7484; 12 hits in 1066 CRISPR screens.
DR GenomeRNAi; 7484; -.
DR Pharos; O14905; Tbio.
DR PRO; PR:O14905; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O14905; protein.
DR Bgee; ENSG00000158955; Expressed in metanephros cortex and 82 other tissues.
DR ExpressionAtlas; O14905; baseline and differential.
DR Genevisible; O14905; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0039706; F:co-receptor binding; IEA:Ensembl.
DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR GO; GO:0005109; F:frizzled binding; IBA:GO_Central.
DR GO; GO:0048018; F:receptor ligand activity; IDA:WormBase.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IEA:Ensembl.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:WormBase.
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:0009267; P:cellular response to starvation; IEA:Ensembl.
DR GO; GO:0072044; P:collecting duct development; IEA:Ensembl.
DR GO; GO:0061303; P:cornea development in camera-type eye; ISS:BHF-UCL.
DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IEA:Ensembl.
DR GO; GO:0072046; P:establishment of planar polarity involved in nephron morphogenesis; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0072003; P:kidney rudiment formation; IEA:Ensembl.
DR GO; GO:0030539; P:male genitalia development; IEA:Ensembl.
DR GO; GO:0072038; P:mesenchymal stem cell maintenance involved in nephron morphogenesis; IEA:Ensembl.
DR GO; GO:0072181; P:mesonephric duct formation; IEA:Ensembl.
DR GO; GO:0072174; P:metanephric tubule formation; IEA:Ensembl.
DR GO; GO:1904948; P:midbrain dopaminergic neuron differentiation; IMP:ParkinsonsUK-UCL.
DR GO; GO:1902455; P:negative regulation of stem cell population maintenance; IMP:ParkinsonsUK-UCL.
DR GO; GO:0030182; P:neuron differentiation; ISS:UniProtKB.
DR GO; GO:1905438; P:non-canonical Wnt signaling pathway involved in midbrain dopaminergic neuron differentiation; IDA:ParkinsonsUK-UCL.
DR GO; GO:0043085; P:positive regulation of catalytic activity; IEA:Ensembl.
DR GO; GO:0009786; P:regulation of asymmetric cell division; IEA:Ensembl.
DR GO; GO:0003339; P:regulation of mesenchymal to epithelial transition involved in metanephros morphogenesis; IEA:Ensembl.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0035150; P:regulation of tube size; IEA:Ensembl.
DR GO; GO:0032526; P:response to retinoic acid; NAS:BHF-UCL.
DR GO; GO:0060021; P:roof of mouth development; IEA:Ensembl.
DR GO; GO:0061038; P:uterus morphogenesis; IEA:Ensembl.
DR GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; IEA:Ensembl.
DR Gene3D; 3.30.2460.20; -; 1.
DR InterPro; IPR005817; Wnt.
DR InterPro; IPR026535; WNT9B.
DR InterPro; IPR043158; Wnt_C.
DR InterPro; IPR018161; Wnt_CS.
DR PANTHER; PTHR12027; PTHR12027; 1.
DR PANTHER; PTHR12027:SF84; PTHR12027:SF84; 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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..357
FT /note="Protein Wnt-9b"
FT /id="PRO_0000041458"
FT LIPID 216
FT /note="O-palmitoleoyl serine; by PORCN"
FT /evidence="ECO:0000250|UniProtKB:P56704"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 89..100
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 135..143
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 145..162
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 210..224
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 212..219
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 291..316
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 305..311
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 315..355
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 331..346
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 333..343
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 338..339
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT VARIANT 106
FT /note="M -> T (in dbSNP:rs4968281)"
FT /evidence="ECO:0000269|PubMed:11604992"
FT /id="VAR_030839"
SQ SEQUENCE 357 AA; 39001 MW; CC22162F9D294CB8 CRC64;
MRPPPALALA GLCLLALPAA AASYFGLTGR EVLTPFPGLG TAAAPAQGGA HLKQCDLLKL
SRRQKQLCRR EPGLAETLRD AAHLGLLECQ FQFRHERWNC SLEGRMGLLK RGFKETAFLY
AVSSAALTHT LARACSAGRM ERCTCDDSPG LESRQAWQWG VCGDNLKYST KFLSNFLGSK
RGNKDLRARA DAHNTHVGIK AVKSGLRTTC KCHGVSGSCA VRTCWKQLSP FRETGQVLKL
RYDSAVKVSS ATNEALGRLE LWAPARQGSL TKGLAPRSGD LVYMEDSPSF CRPSKYSPGT
AGRVCSREAS CSSLCCGRGY DTQSRLVAFS CHCQVQWCCY VECQQCVQEE LVYTCKH
