WNT16_HUMAN
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 03-AUG-2022, entry version 164.
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}.
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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; 12.
DR STRING; 9606.ENSP00000222462; -.
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; Q9UBV4; -.
DR PeptideAtlas; Q9UBV4; -.
DR PRIDE; Q9UBV4; -.
DR ProteomicsDB; 84079; -. [Q9UBV4-1]
DR ProteomicsDB; 84080; -. [Q9UBV4-2]
DR Antibodypedia; 17566; 216 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 CTD; 51384; -.
DR DisGeNET; 51384; -.
DR GeneCards; WNT16; -.
DR HGNC; HGNC:16267; WNT16.
DR HPA; ENSG00000002745; Tissue enhanced (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; RGRECNR; -.
DR OrthoDB; 745245at2759; -.
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 1067 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 skin of hip and 93 other tissues.
DR ExpressionAtlas; Q9UBV4; baseline and differential.
DR Genevisible; Q9UBV4; HS.
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:0060548; P:negative regulation of cell death; 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:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IMP:BHF-UCL.
DR GO; GO:0090399; P:replicative senescence; IMP:BHF-UCL.
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; PTHR12027; 1.
DR Pfam; PF00110; wnt; 1.
DR PRINTS; PR01895; WNT16PROTEIN.
DR PRINTS; PR01349; WNTPROTEIN.
DR SMART; SM00097; WNT1; 1.
DR PROSITE; PS00246; WNT1; 1.
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
