ID WNT16_HUMAN Reviewed; 365 AA. AC Q9UBV4; Q2M3G1; Q9Y5C0; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 24-JAN-2024, entry version 172. DE RecName: Full=Protein Wnt-16; DE Flags: Precursor; GN Name=WNT16; 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] (ISOFORM WNT-16B). RX PubMed=10500199; DOI=10.1073/pnas.96.20.11464; RA McWhirter J.R., Neuteboom S.T., Wancewicz E.V., Monia B.P., Downing J.R., RA Murre C.; RT "Oncogenic homeodomain transcription factor E2A-Pbx1 activates a novel WNT RT gene in pre-B acute lymphoblastoid leukemia."; RL Proc. Natl. Acad. Sci. U.S.A. 96:11464-11469(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM WNT-16A), AND VARIANTS ARG-82 AND RP ILE-263. RC TISSUE=Placenta; RX PubMed=11095990; DOI=10.1006/bbrc.2000.3852; RA Fear M.W., Kelsell D.P., Spurr N.K., Barnes M.R.; RT "Wnt-16a, a novel Wnt-16 isoform, which shows differential expression in RT adult human tissues."; RL Biochem. Biophys. Res. Commun. 278:814-820(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM WNT-16B). 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). RN [5] RP VARIANT [LARGE SCALE ANALYSIS] MET-126. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). 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 -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Wnt-16b; CC IsoId=Q9UBV4-1; Sequence=Displayed; CC Name=Wnt-16a; CC IsoId=Q9UBV4-2; Sequence=VSP_006797; CC -!- TISSUE SPECIFICITY: Isoform Wnt-16b is expressed in peripheral lymphoid CC organs such as spleen, appendix, and lymph nodes, in kidney but not in CC bone marrow. Isoform Wnt-16a is expressed at significant levels only in CC the pancreas. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF169963; AAD49351.1; -; mRNA. DR EMBL; AF152584; AAD38052.1; -; mRNA. DR EMBL; AC006364; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC104919; AAI04920.1; -; mRNA. DR EMBL; BC104945; AAI04946.1; -; mRNA. DR CCDS; CCDS5781.1; -. [Q9UBV4-1] DR RefSeq; NP_057171.2; NM_016087.2. DR RefSeq; NP_476509.1; NM_057168.1. [Q9UBV4-1] DR AlphaFoldDB; Q9UBV4; -. DR SMR; Q9UBV4; -. DR BioGRID; 119514; 128. DR IntAct; Q9UBV4; 13. DR STRING; 9606.ENSP00000222462; -. DR GlyCosmos; Q9UBV4; 3 sites, No reported glycans. DR GlyGen; Q9UBV4; 4 sites, 1 O-linked glycan (1 site). DR iPTMnet; Q9UBV4; -. DR PhosphoSitePlus; Q9UBV4; -. DR SwissPalm; Q9UBV4; -. DR BioMuta; WNT16; -. DR DMDM; 12643875; -. DR jPOST; Q9UBV4; -. DR MassIVE; Q9UBV4; -. DR PaxDb; 9606-ENSP00000222462; -. DR PeptideAtlas; Q9UBV4; -. DR ProteomicsDB; 84079; -. [Q9UBV4-1] DR ProteomicsDB; 84080; -. [Q9UBV4-2] DR Antibodypedia; 17566; 252 antibodies from 31 providers. DR DNASU; 51384; -. DR Ensembl; ENST00000222462.3; ENSP00000222462.2; ENSG00000002745.13. [Q9UBV4-1] DR GeneID; 51384; -. DR KEGG; hsa:51384; -. DR MANE-Select; ENST00000222462.3; ENSP00000222462.2; NM_057168.2; NP_476509.1. DR UCSC; uc003vjw.4; human. [Q9UBV4-1] DR AGR; HGNC:16267; -. DR CTD; 51384; -. DR DisGeNET; 51384; -. DR GeneCards; WNT16; -. DR HGNC; HGNC:16267; WNT16. DR HPA; ENSG00000002745; Group enriched (cervix, skin). DR MIM; 606267; gene. DR neXtProt; NX_Q9UBV4; -. DR OpenTargets; ENSG00000002745; -. DR PharmGKB; PA38105; -. DR VEuPathDB; HostDB:ENSG00000002745; -. DR eggNOG; KOG3913; Eukaryota. DR GeneTree; ENSGT00940000157480; -. DR HOGENOM; CLU_033039_1_0_1; -. DR InParanoid; Q9UBV4; -. DR OMA; KFERWNC; -. DR OrthoDB; 2874082at2759; -. DR PhylomeDB; Q9UBV4; -. DR TreeFam; TF105310; -. DR PathwayCommons; Q9UBV4; -. DR Reactome; R-HSA-3238698; WNT ligand biogenesis and trafficking. DR Reactome; R-HSA-373080; Class B/2 (Secretin family receptors). DR SignaLink; Q9UBV4; -. DR SIGNOR; Q9UBV4; -. DR BioGRID-ORCS; 51384; 5 hits in 1147 CRISPR screens. DR GeneWiki; WNT16; -. DR GenomeRNAi; 51384; -. DR Pharos; Q9UBV4; Tbio. DR PRO; PR:Q9UBV4; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; Q9UBV4; Protein. DR Bgee; ENSG00000002745; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 93 other cell types or tissues. DR ExpressionAtlas; Q9UBV4; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL. DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central. DR GO; GO:0005109; F:frizzled binding; IBA:GO_Central. DR GO; GO:0046849; P:bone remodeling; IEA:Ensembl. DR GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central. DR GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; IEA:Ensembl. DR GO; GO:0045165; P:cell fate commitment; IBA:GO_Central. DR GO; GO:0030216; P:keratinocyte differentiation; IMP:BHF-UCL. DR GO; GO:0043616; P:keratinocyte proliferation; IMP:BHF-UCL. DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IMP:BHF-UCL. DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central. DR GO; GO:0003408; P:optic cup formation involved in camera-type eye development; ISS:BHF-UCL. DR GO; GO:0090403; P:oxidative stress-induced premature senescence; IMP:BHF-UCL. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL. DR GO; GO:0046330; P:positive regulation of JNK cascade; IMP:BHF-UCL. DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IMP:BHF-UCL. DR GO; GO:0090399; P:replicative senescence; IMP:BHF-UCL. DR GO; GO:0016055; P:Wnt signaling pathway; IMP:BHF-UCL. DR CDD; cd19344; Wnt_Wnt16; 1. DR Gene3D; 3.30.2460.20; -; 1. DR InterPro; IPR005817; Wnt. DR InterPro; IPR013304; Wnt16. DR InterPro; IPR043158; Wnt_C. DR InterPro; IPR018161; Wnt_CS. DR PANTHER; PTHR12027:SF70; PROTEIN WNT-16; 1. DR PANTHER; PTHR12027; WNT RELATED; 1. DR Pfam; PF00110; wnt; 1. DR PRINTS; PR01895; WNT16PROTEIN. DR PRINTS; PR01349; WNTPROTEIN. DR SMART; SM00097; WNT1; 1. DR PROSITE; PS00246; WNT1; 1. DR Genevisible; Q9UBV4; HS. PE 2: Evidence at transcript level; KW Alternative splicing; Developmental protein; Disulfide bond; KW Extracellular matrix; Glycoprotein; Lipoprotein; Reference proteome; KW Secreted; Signal; Wnt signaling pathway. FT SIGNAL 1..29 FT /evidence="ECO:0000255" FT CHAIN 30..365 FT /note="Protein Wnt-16" FT /id="PRO_0000041471" FT LIPID 227 FT /note="O-palmitoleoyl serine; by PORCN" FT /evidence="ECO:0000250|UniProtKB:P56704" FT CARBOHYD 143 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 189 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 311 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 81..92 FT /evidence="ECO:0000250|UniProtKB:P28026" FT DISULFID 139..147 FT /evidence="ECO:0000250|UniProtKB:P28026" FT DISULFID 149..168 FT /evidence="ECO:0000250|UniProtKB:P28026" FT DISULFID 221..235 FT /evidence="ECO:0000250|UniProtKB:P28026" FT DISULFID 223..230 FT /evidence="ECO:0000250|UniProtKB:P28026" FT DISULFID 294..325 FT /evidence="ECO:0000250|UniProtKB:P28026" FT DISULFID 310..320 FT /evidence="ECO:0000250|UniProtKB:P28026" FT DISULFID 324..364 FT /evidence="ECO:0000250|UniProtKB:P28026" FT DISULFID 340..355 FT /evidence="ECO:0000250|UniProtKB:P28026" FT DISULFID 342..352 FT /evidence="ECO:0000250|UniProtKB:P28026" FT DISULFID 347..348 FT /evidence="ECO:0000250|UniProtKB:P28026" FT VAR_SEQ 1..32 FT /note="MDRAALLGLARLCALWAALLVLFPYGAQGNWM -> MERHPPMQLTTCLRET FT LFTGASQKTSLW (in isoform Wnt-16a)" FT /evidence="ECO:0000303|PubMed:11095990" FT /id="VSP_006797" FT VARIANT 82 FT /note="G -> R (in dbSNP:rs2908004)" FT /evidence="ECO:0000269|PubMed:11095990" FT /id="VAR_052957" FT VARIANT 126 FT /note="V -> M (in a colorectal cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036289" FT VARIANT 263 FT /note="T -> I (in dbSNP:rs2707466)" FT /evidence="ECO:0000269|PubMed:11095990" FT /id="VAR_052958" SQ SEQUENCE 365 AA; 40690 MW; 313A26D8FFBCC56F CRC64; MDRAALLGLA RLCALWAALL VLFPYGAQGN WMWLGIASFG VPEKLGCANL PLNSRQKELC KRKPYLLPSI REGARLGIQE CGSQFRHERW NCMITAAATT APMGASPLFG YELSSGTKET AFIYAVMAAG LVHSVTRSCS AGNMTECSCD TTLQNGGSAS EGWHWGGCSD DVQYGMWFSR KFLDFPIGNT TGKENKVLLA MNLHNNEAGR QAVAKLMSVD CRCHGVSGSC AVKTCWKTMS SFEKIGHLLK DKYENSIQIS DKTKRKMRRR EKDQRKIPIH KDDLLYVNKS PNYCVEDKKL GIPGTQGREC NRTSEGADGC NLLCCGRGYN THVVRHVERC ECKFIWCCYV RCRRCESMTD VHTCK //