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   13-FEB-2019, entry version 146.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-106.
RX   PubMed=11604992;
RA   Kirikoshi H., Sekihara H., Katoh M.;
RT   "Molecular cloning and characterization of WNT14B, a novel member of
RT   the 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.,
RA   Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA   Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA   Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA   Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA   Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA   Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale
RT   effort to identify novel human secreted and transmembrane proteins: a
RT   bioinformatics 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.,
RA   Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA   Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA   Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA   Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA   Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA   Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA   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
RT   the 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.,
RA   Copeland N.G., Osborne M.P., Bowcock A.M., Brown A.M.C.;
RT   "Isolation of two novel WNT genes, WNT14 and WNT15, one of which
RT   (WNT15) is 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.,
RA   Costa M., 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
RT   by a 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
CC       tract, including uterus and part of the oviduct and the upper
CC       vagina in females, and epididymis and vas deferens in males.
CC       Activates a signaling cascade in the metanephric mesenchyme that
CC       induces tubulogenesis. Acts upstream of WNT4 in the signaling
CC       pathways that mediate development of kidney tubules and the
CC       Muellerian ducts. Plays a role in cranofacial development and is
CC       required for normal fusion of the palate during embryonic
CC       development (By similarity). {ECO:0000250|UniProtKB:O35468,
CC       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
CC       physiological form in body fluids (PubMed:26902720). Component of
CC       the Wnt-Fzd-LRP5-LRP6 signaling complex that contains a WNT
CC       protein, a FZD protein and LRP5 or LRP6. Interacts directly in the
CC       complex with LRP6 (PubMed:20093360). Interacts with PKD1 (via
CC       extracellular domain) (PubMed:27214281).
CC       {ECO:0000269|PubMed:20093360, ECO:0000269|PubMed:26902720,
CC       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
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}.
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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   UniGene; Hs.326420; -.
DR   ProteinModelPortal; O14905; -.
DR   BioGrid; 113321; 5.
DR   IntAct; O14905; 2.
DR   STRING; 9606.ENSP00000290015; -.
DR   iPTMnet; O14905; -.
DR   PhosphoSitePlus; O14905; -.
DR   BioMuta; WNT9B; -.
DR   PaxDb; O14905; -.
DR   PeptideAtlas; O14905; -.
DR   PRIDE; O14905; -.
DR   ProteomicsDB; 48290; -.
DR   Ensembl; ENST00000290015; ENSP00000290015; ENSG00000158955.
DR   Ensembl; ENST00000613753; ENSP00000482127; ENSG00000276799.
DR   GeneID; 7484; -.
DR   KEGG; hsa:7484; -.
DR   UCSC; uc002ikw.2; human.
DR   CTD; 7484; -.
DR   DisGeNET; 7484; -.
DR   EuPathDB; HostDB:ENSG00000158955.10; -.
DR   GeneCards; WNT9B; -.
DR   H-InvDB; HIX0027116; -.
DR   HGNC; HGNC:12779; WNT9B.
DR   HPA; HPA058361; -.
DR   HPA; HPA059572; -.
DR   MIM; 602864; gene.
DR   neXtProt; NX_O14905; -.
DR   OpenTargets; ENSG00000158955; -.
DR   PharmGKB; PA37380; -.
DR   eggNOG; KOG3913; Eukaryota.
DR   eggNOG; ENOG410XQZ1; LUCA.
DR   GeneTree; ENSGT00940000158599; -.
DR   HOGENOM; HOG000039529; -.
DR   HOVERGEN; HBG001595; -.
DR   InParanoid; O14905; -.
DR   KO; K01064; -.
DR   OMA; CAKDTSC; -.
DR   OrthoDB; 866763at2759; -.
DR   PhylomeDB; O14905; -.
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   SIGNOR; O14905; -.
DR   ChiTaRS; WNT9B; human.
DR   GenomeRNAi; 7484; -.
DR   PRO; PR:O14905; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   Bgee; ENSG00000158955; Expressed in 66 organ(s), highest expression level in kidney.
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: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:0007267; P:cell-cell signaling; NAS:UniProtKB.
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:0007275; P:multicellular organism development; NAS:UniProtKB.
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:0016055; P:Wnt signaling pathway; IBA:GO_Central.
DR   GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; IEA:Ensembl.
DR   InterPro; IPR005817; Wnt.
DR   InterPro; IPR026535; WNT9B.
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   Complete proteome; Developmental protein; Disulfide bond;
KW   Extracellular matrix; Glycoprotein; Lipoprotein; Polymorphism;
KW   Reference proteome; Secreted; Signal; Wnt signaling pathway.
FT   SIGNAL        1     22       {ECO:0000255}.
FT   CHAIN        23    357       Protein Wnt-9b.
FT                                /FTId=PRO_0000041458.
FT   LIPID       216    216       O-palmitoleoyl serine; by PORCN.
FT                                {ECO:0000250|UniProtKB:P56704}.
FT   CARBOHYD     99     99       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     89    100       {ECO:0000250|UniProtKB:P28026}.
FT   DISULFID    135    143       {ECO:0000250|UniProtKB:P28026}.
FT   DISULFID    145    162       {ECO:0000250|UniProtKB:P28026}.
FT   DISULFID    210    224       {ECO:0000250|UniProtKB:P28026}.
FT   DISULFID    212    219       {ECO:0000250|UniProtKB:P28026}.
FT   DISULFID    291    316       {ECO:0000250|UniProtKB:P28026}.
FT   DISULFID    305    311       {ECO:0000250|UniProtKB:P28026}.
FT   DISULFID    315    355       {ECO:0000250|UniProtKB:P28026}.
FT   DISULFID    331    346       {ECO:0000250|UniProtKB:P28026}.
FT   DISULFID    333    343       {ECO:0000250|UniProtKB:P28026}.
FT   DISULFID    338    339       {ECO:0000250|UniProtKB:P28026}.
FT   VARIANT     106    106       M -> T (in dbSNP:rs4968281).
FT                                {ECO:0000269|PubMed:11604992}.
FT                                /FTId=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
//