ID   WNT8B_HUMAN             Reviewed;         351 AA.
AC   Q93098; O00771; Q5VX55; Q8WYK9;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 3.
DT   24-JAN-2024, entry version 182.
DE   RecName: Full=Protein Wnt-8b;
DE   Flags: Precursor;
GN   Name=WNT8B;
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 [GENOMIC DNA / MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=9536085; DOI=10.1093/hmg/7.5.813;
RA   Lako M., Lindsay S., Bullen P., Wilson D.I., Robson S.C., Strachan T.;
RT   "A novel mammalian Wnt gene, WNT8B, shows brain-restricted expression in
RT   early development, with sharply delimited expression boundaries in the
RT   developing forebrain.";
RL   Hum. Mol. Genet. 7:813-822(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Fetal brain;
RX   PubMed=11788899;
RA   Saitoh T., Mine T., Katoh M.;
RT   "Up-regulation of WNT8B mRNA in human gastric cancer.";
RL   Int. J. Oncol. 20:343-348(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA   Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA   Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA   Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA   Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA   Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA   Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA   Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA   McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA   Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA   Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA   Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA   Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA   Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA   Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA   Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 23-317.
RX   PubMed=8661156; DOI=10.1006/geno.1996.0374;
RA   Lako M., Strachan T., Curtis A.R.J., Lindsay S.;
RT   "Isolation and characterization of WNT8B, a novel human Wnt gene that maps
RT   to 10q24.";
RL   Genomics 35:386-388(1996).
RN   [5]
RP   VARIANT [LARGE SCALE ANALYSIS] GLN-53.
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. May play an important role in the development
CC       and differentiation of certain forebrain structures, notably the
CC       hippocampus. {ECO:0000269|PubMed:9536085}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix.
CC   -!- TISSUE SPECIFICITY: Expression is restricted to the brain, and more
CC       specifically to the forebrain. {ECO:0000269|PubMed:9536085}.
CC   -!- PTM: Palmitoleoylation is required for efficient binding to frizzled
CC       receptors (By similarity). Depalmitoleoylation leads to Wnt signaling
CC       pathway inhibition (By similarity). {ECO:0000250|UniProtKB:P28026,
CC       ECO:0000250|UniProtKB:P56704}.
CC   -!- PTM: Proteolytic processing by TIKI1 and TIKI2 promotes oxidation and
CC       formation of large disulfide-bond oligomers, leading to inactivation of
CC       WNT8B. {ECO:0000250|UniProtKB:P28026}.
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; Y11094; CAA71968.1; -; mRNA.
DR   EMBL; Y11108; CAA71994.1; -; Genomic_DNA.
DR   EMBL; AB073637; BAB83924.1; -; mRNA.
DR   EMBL; AL359759; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL133352; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; X91940; CAA63017.1; -; mRNA.
DR   CCDS; CCDS7494.1; -.
DR   RefSeq; NP_003384.2; NM_003393.3.
DR   AlphaFoldDB; Q93098; -.
DR   SMR; Q93098; -.
DR   BioGRID; 113316; 6.
DR   IntAct; Q93098; 2.
DR   STRING; 9606.ENSP00000340677; -.
DR   GlyCosmos; Q93098; 2 sites, No reported glycans.
DR   GlyGen; Q93098; 2 sites.
DR   iPTMnet; Q93098; -.
DR   PhosphoSitePlus; Q93098; -.
DR   BioMuta; WNT8B; -.
DR   DMDM; 66774217; -.
DR   MassIVE; Q93098; -.
DR   PaxDb; 9606-ENSP00000340677; -.
DR   PeptideAtlas; Q93098; -.
DR   ProteomicsDB; 75724; -.
DR   Antibodypedia; 17653; 251 antibodies from 31 providers.
DR   DNASU; 7479; -.
DR   Ensembl; ENST00000343737.6; ENSP00000340677.5; ENSG00000075290.8.
DR   GeneID; 7479; -.
DR   KEGG; hsa:7479; -.
DR   MANE-Select; ENST00000343737.6; ENSP00000340677.5; NM_003393.4; NP_003384.2.
DR   UCSC; uc001krb.4; human.
DR   AGR; HGNC:12789; -.
DR   CTD; 7479; -.
DR   DisGeNET; 7479; -.
DR   GeneCards; WNT8B; -.
DR   HGNC; HGNC:12789; WNT8B.
DR   HPA; ENSG00000075290; Tissue enhanced (parathyroid).
DR   MIM; 601396; gene.
DR   neXtProt; NX_Q93098; -.
DR   OpenTargets; ENSG00000075290; -.
DR   PharmGKB; PA37390; -.
DR   VEuPathDB; HostDB:ENSG00000075290; -.
DR   eggNOG; KOG3913; Eukaryota.
DR   GeneTree; ENSGT00940000160584; -.
DR   HOGENOM; CLU_033039_1_2_1; -.
DR   InParanoid; Q93098; -.
DR   OMA; FMHLEVF; -.
DR   OrthoDB; 2874082at2759; -.
DR   PhylomeDB; Q93098; -.
DR   TreeFam; TF105310; -.
DR   PathwayCommons; Q93098; -.
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-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR   SignaLink; Q93098; -.
DR   SIGNOR; Q93098; -.
DR   BioGRID-ORCS; 7479; 9 hits in 1148 CRISPR screens.
DR   GeneWiki; WNT8B; -.
DR   GenomeRNAi; 7479; -.
DR   Pharos; Q93098; Tbio.
DR   PRO; PR:Q93098; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; Q93098; Protein.
DR   Bgee; ENSG00000075290; Expressed in adult mammalian kidney and 25 other cell types or tissues.
DR   ExpressionAtlas; Q93098; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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: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:0048263; P:determination of dorsal identity; ISS:BHF-UCL.
DR   GO; GO:0007369; P:gastrulation; ISS:BHF-UCL.
DR   GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR   GO; GO:0030182; P:neuron differentiation; ISS:UniProtKB.
DR   GO; GO:0032355; P:response to estradiol; NAS:BHF-UCL.
DR   GO; GO:0032526; P:response to retinoic acid; NAS:BHF-UCL.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   Gene3D; 3.30.2460.20; -; 1.
DR   InterPro; IPR005817; Wnt.
DR   InterPro; IPR013301; Wnt8.
DR   InterPro; IPR043158; Wnt_C.
DR   InterPro; IPR018161; Wnt_CS.
DR   PANTHER; PTHR12027:SF94; PROTEIN WNT-8B; 1.
DR   PANTHER; PTHR12027; WNT RELATED; 1.
DR   Pfam; PF00110; wnt; 1.
DR   PRINTS; PR01892; WNT8PROTEIN.
DR   PRINTS; PR01349; WNTPROTEIN.
DR   SMART; SM00097; WNT1; 1.
DR   PROSITE; PS00246; WNT1; 1.
DR   Genevisible; Q93098; HS.
PE   2: Evidence at transcript 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..351
FT                   /note="Protein Wnt-8b"
FT                   /id="PRO_0000041450"
FT   LIPID           186
FT                   /note="O-palmitoleoyl serine"
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        259
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        54..65
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        104..112
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        114..132
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        180..194
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        182..189
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        256..294
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        272..287
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        291..333
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        309..324
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        311..321
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        316..317
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   VARIANT         11
FT                   /note="C -> S (in dbSNP:rs3793771)"
FT                   /id="VAR_020310"
FT   VARIANT         53
FT                   /note="E -> Q (in a colorectal cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036288"
FT   CONFLICT        230
FT                   /note="G -> A (in Ref. 1 and 4)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        284
FT                   /note="R -> L (in Ref. 1 and 4)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   351 AA;  38721 MW;  DD242070948813F8 CRC64;
     MFLSKPSVYI CLFTCVLQLS HSWSVNNFLM TGPKAYLIYS SSVAAGAQSG IEECKYQFAW
     DRWNCPERAL QLSSHGGLRS ANRETAFVHA ISSAGVMYTL TRNCSLGDFD NCGCDDSRNG
     QLGGQGWLWG GCSDNVGFGE AISKQFVDAL ETGQDARAAM NLHNNEAGRK AVKGTMKRTC
     KCHGVSGSCT TQTCWLQLPE FREVGAHLKE KYHAALKVDL LQGAGNSAAG RGAIADTFRS
     ISTRELVHLE DSPDYCLENK TLGLLGTEGR ECLRRGRALG RWERRSCRRL CGDCGLAVEE
     RRAETVSSCN CKFHWCCAVR CEQCRRRVTK YFCSRAERPR GGAAHKPGRK P
//