ID   WNT9A_HUMAN             Reviewed;         365 AA.
AC   O14904; A6NLW2; Q2M2J3; Q5VWU0; Q96S50;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2002, sequence version 2.
DT   13-FEB-2019, entry version 160.
DE   RecName: Full=Protein Wnt-9a;
DE   AltName: Full=Protein Wnt-14;
DE   Flags: Precursor;
GN   Name=WNT9A; Synonyms=WNT14;
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].
RX   PubMed=11414706; DOI=10.1006/bbrc.2001.5105;
RA   Saitoh T., Hirai M., Katoh M.;
RT   "Molecular cloning and characterization of WNT3a and WNT14 clustered
RT   in human chromosome 1q42 region.";
RL   Biochem. Biophys. Res. Commun. 284:1168-1175(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 221-343.
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   [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).
CC   -!- FUNCTION: Ligand for members of the frizzled family of seven
CC       transmembrane receptors. Functions in the canonical Wnt/beta-
CC       catenin signaling pathway. Required for normal timing of IHH
CC       expression during embryonic bone development, normal chondrocyte
CC       maturation and for normal bone mineralization during embryonic
CC       bone development. Plays a redundant role in maintaining joint
CC       integrity. {ECO:0000250|UniProtKB:O42280,
CC       ECO:0000250|UniProtKB:Q8R5M2}.
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).
CC       {ECO:0000269|PubMed:26902720}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000305}. Secreted {ECO:0000269|PubMed:26902720}.
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; AB060283; BAB61051.1; -; mRNA.
DR   EMBL; AL360269; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471098; EAW69821.1; -; Genomic_DNA.
DR   EMBL; BC111960; AAI11961.1; -; mRNA.
DR   EMBL; BC113431; AAI13432.1; -; mRNA.
DR   EMBL; AF028702; AAC39550.1; -; Genomic_DNA.
DR   CCDS; CCDS31045.1; -.
DR   RefSeq; NP_003386.1; NM_003395.2.
DR   UniGene; Hs.149504; -.
DR   ProteinModelPortal; O14904; -.
DR   SMR; O14904; -.
DR   IntAct; O14904; 1.
DR   STRING; 9606.ENSP00000272164; -.
DR   PhosphoSitePlus; O14904; -.
DR   BioMuta; WNT9A; -.
DR   PaxDb; O14904; -.
DR   PeptideAtlas; O14904; -.
DR   PRIDE; O14904; -.
DR   ProteomicsDB; 48289; -.
DR   DNASU; 7483; -.
DR   Ensembl; ENST00000272164; ENSP00000272164; ENSG00000143816.
DR   GeneID; 7483; -.
DR   KEGG; hsa:7483; -.
DR   UCSC; uc001hri.3; human.
DR   CTD; 7483; -.
DR   DisGeNET; 7483; -.
DR   EuPathDB; HostDB:ENSG00000143816.7; -.
DR   GeneCards; WNT9A; -.
DR   HGNC; HGNC:12778; WNT9A.
DR   MIM; 602863; gene.
DR   neXtProt; NX_O14904; -.
DR   OpenTargets; ENSG00000143816; -.
DR   PharmGKB; PA37379; -.
DR   eggNOG; KOG3913; Eukaryota.
DR   eggNOG; ENOG410XQZ1; LUCA.
DR   GeneTree; ENSGT00940000159618; -.
DR   HOGENOM; HOG000039529; -.
DR   HOVERGEN; HBG001595; -.
DR   InParanoid; O14904; -.
DR   KO; K01064; -.
DR   OMA; VECKQCT; -.
DR   OrthoDB; 866763at2759; -.
DR   PhylomeDB; O14904; -.
DR   TreeFam; TF105310; -.
DR   Reactome; R-HSA-201681; TCF dependent signaling in response to WNT.
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-3772470; Negative regulation of TCF-dependent signaling by WNT ligand antagonists.
DR   SIGNOR; O14904; -.
DR   ChiTaRS; WNT9A; human.
DR   GeneWiki; WNT9A; -.
DR   GenomeRNAi; 7483; -.
DR   PRO; PR:O14904; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   Bgee; ENSG00000143816; Expressed in 159 organ(s), highest expression level in esophagogastric junction muscularis propria.
DR   ExpressionAtlas; O14904; baseline and differential.
DR   Genevisible; O14904; HS.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; 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: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:0061303; P:cornea development in camera-type eye; ISS:BHF-UCL.
DR   GO; GO:0035115; P:embryonic forelimb morphogenesis; IEA:Ensembl.
DR   GO; GO:0072498; P:embryonic skeletal joint development; ISS:BHF-UCL.
DR   GO; GO:0048704; P:embryonic skeletal system morphogenesis; IEA:Ensembl.
DR   GO; GO:0061072; P:iris morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0007093; P:mitotic cell cycle checkpoint; IMP:BHF-UCL.
DR   GO; GO:0007275; P:multicellular organism development; NAS:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:BHF-UCL.
DR   GO; GO:0032331; P:negative regulation of chondrocyte differentiation; ISS:BHF-UCL.
DR   GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
DR   GO; GO:0030182; P:neuron differentiation; ISS:UniProtKB.
DR   GO; GO:0045597; P:positive regulation of cell differentiation; IEA:Ensembl.
DR   GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IEA:Ensembl.
DR   GO; GO:0016055; P:Wnt signaling pathway; IBA:GO_Central.
DR   InterPro; IPR005817; Wnt.
DR   InterPro; IPR013303; Wnt9a.
DR   InterPro; IPR018161; Wnt_CS.
DR   PANTHER; PTHR12027; PTHR12027; 1.
DR   PANTHER; PTHR12027:SF75; PTHR12027:SF75; 1.
DR   Pfam; PF00110; wnt; 1.
DR   PRINTS; PR01894; WNT14PROTEIN.
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     29       {ECO:0000255}.
FT   CHAIN        30    365       Protein Wnt-9a.
FT                                /FTId=PRO_0000041455.
FT   LIPID       221    221       O-palmitoleoyl serine; by PORCN.
FT                                {ECO:0000250|UniProtKB:P56704}.
FT   CARBOHYD    103    103       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     93    104       {ECO:0000250|UniProtKB:P28026}.
FT   DISULFID    141    149       {ECO:0000250|UniProtKB:P28026}.
FT   DISULFID    151    168       {ECO:0000250|UniProtKB:P28026}.
FT   DISULFID    215    229       {ECO:0000250|UniProtKB:P28026}.
FT   DISULFID    217    224       {ECO:0000250|UniProtKB:P28026}.
FT   DISULFID    299    324       {ECO:0000250|UniProtKB:P28026}.
FT   DISULFID    313    319       {ECO:0000250|UniProtKB:P28026}.
FT   DISULFID    323    363       {ECO:0000250|UniProtKB:P28026}.
FT   DISULFID    339    354       {ECO:0000250|UniProtKB:P28026}.
FT   DISULFID    341    351       {ECO:0000250|UniProtKB:P28026}.
FT   DISULFID    346    347       {ECO:0000250|UniProtKB:P28026}.
FT   VARIANT     260    260       A -> T (in dbSNP:rs8192633).
FT                                /FTId=VAR_052956.
SQ   SEQUENCE   365 AA;  40320 MW;  1E1284D744C6A9B2 CRC64;
     MLDGSPLARW LAAAFGLTLL LAALRPSAAY FGLTGSEPLT ILPLTLEPEA AAQAHYKACD
     RLKLERKQRR MCRRDPGVAE TLVEAVSMSA LECQFQFRFE RWNCTLEGRY RASLLKRGFK
     ETAFLYAISS AGLTHALAKA CSAGRMERCT CDEAPDLENR EAWQWGGCGD NLKYSSKFVK
     EFLGRRSSKD LRARVDFHNN LVGVKVIKAG VETTCKCHGV SGSCTVRTCW RQLAPFHEVG
     KHLKHKYETA LKVGSTTNEA AGEAGAISPP RGRASGAGGS DPLPRTPELV HLDDSPSFCL
     AGRFSPGTAG RRCHREKNCE SICCGRGHNT QSRVVTRPCQ CQVRWCCYVE CRQCTQREEV
     YTCKG
//