WNT8A_DANRE
ID WNT8A_DANRE Reviewed; 359 AA.
AC P51028; Q7SXM4; Q90YL9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Protein Wnt-8a;
DE Flags: Precursor;
GN Name=wnt8a; Synonyms=wnt-8, wnt8;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Embryo;
RX PubMed=7600994; DOI=10.1242/dev.121.6.1787;
RA Kelly G.M., Erezyilmaz D.F., Greenstein P.E., Moon R.T.;
RT "Zebrafish wnt8 and wnt8b share a common activity but are involved in
RT distinct developmental pathways.";
RL Development 121:1787-1799(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION, DEVELOPMENTAL STAGE,
RP AND FUNCTION.
RX PubMed=11703928; DOI=10.1016/s1534-5807(01)00007-7;
RA Lekven A.C., Thorpe C.J., Waxman J.S., Moon R.T.;
RT "Zebrafish wnt8 encodes two wnt8 proteins on a bicistronic transcript and
RT is required for mesoderm and neurectoderm patterning.";
RL Dev. Cell 1:103-114(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=25371059; DOI=10.1038/ncomms6368;
RA Lu F.I., Sun Y.H., Wei C.Y., Thisse C., Thisse B.;
RT "Tissue-specific derepression of TCF/LEF controls the activity of the
RT Wnt/beta-catenin pathway.";
RL Nat. Commun. 5:5368-5368(2014).
CC -!- FUNCTION: Ligand for members of the frizzled family of seven
CC transmembrane receptors (Probable). Required for mesoderm and neural
CC ectoderm patterning during gastrulation (PubMed:11703928). Involved in
CC axis formation during embryonic development, via activation of
CC canonical Wnt/CTNNB1 signaling (PubMed:11703928, PubMed:25371059). May
CC be involved in the specification of the spatial patterns of expression
CC of Gsc and other regulatory genes leading to the establishment of the
CC embryonic axis (PubMed:7600994). {ECO:0000269|PubMed:11703928,
CC ECO:0000269|PubMed:25371059, ECO:0000269|PubMed:7600994, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:Q9H1J5}. Secreted
CC {ECO:0000250|UniProtKB:Q9H1J5}.
CC -!- TISSUE SPECIFICITY: Expressed in the margin of the pregastrula embryo
CC destined to be the future mesoderm. {ECO:0000269|PubMed:7600994}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the segmental plate and ventral
CC mesoderm during early gastrulation and early somitogenesis
CC (PubMed:25371059). Expressed in the marginal region and in a broad
CC domain in the ventral region after 75% epiboly (PubMed:11703928).
CC Expressed in the tailbud during the bud stage (PubMed:11703928).
CC {ECO:0000269|PubMed:11703928, ECO:0000269|PubMed:25371059}.
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 wnt8. {ECO:0000250|UniProtKB:P28026}.
CC -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000305}.
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DR EMBL; U10869; AAC59697.2; -; mRNA.
DR EMBL; AY032749; AAK70223.1; -; Genomic_DNA.
DR EMBL; BC055535; AAH55535.1; -; mRNA.
DR PIR; I50505; I50505.
DR RefSeq; NP_571021.3; NM_130946.3.
DR AlphaFoldDB; P51028; -.
DR SMR; P51028; -.
DR BioGRID; 78358; 12.
DR STRING; 7955.ENSDARP00000116057; -.
DR PaxDb; P51028; -.
DR GeneID; 30122; -.
DR KEGG; dre:30122; -.
DR CTD; 7478; -.
DR ZFIN; ZDB-GENE-980526-332; wnt8a.
DR eggNOG; KOG3913; Eukaryota.
DR InParanoid; P51028; -.
DR OrthoDB; 618621at2759; -.
DR PhylomeDB; P51028; -.
DR Reactome; R-DRE-3238698; WNT ligand biogenesis and trafficking.
DR Reactome; R-DRE-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR PRO; PR:P51028; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0097189; C:apoptotic body; IDA:ZFIN.
DR GO; GO:0009986; C:cell surface; IDA:ZFIN.
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:0009952; P:anterior/posterior pattern specification; IDA:ZFIN.
DR GO; GO:0035284; P:brain segmentation; IMP:ZFIN.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IMP:ZFIN.
DR GO; GO:0060823; P:canonical Wnt signaling pathway involved in neural plate anterior/posterior pattern formation; IMP:ZFIN.
DR GO; GO:0045165; P:cell fate commitment; IDA:ZFIN.
DR GO; GO:0042074; P:cell migration involved in gastrulation; IGI:ZFIN.
DR GO; GO:0039015; P:cell proliferation involved in pronephros development; IMP:ZFIN.
DR GO; GO:0007417; P:central nervous system development; IMP:ZFIN.
DR GO; GO:0048263; P:determination of dorsal identity; IMP:ZFIN.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:ZFIN.
DR GO; GO:0007398; P:ectoderm development; IMP:ZFIN.
DR GO; GO:0000578; P:embryonic axis specification; IMP:UniProtKB.
DR GO; GO:0007492; P:endoderm development; IMP:ZFIN.
DR GO; GO:0001654; P:eye development; IDA:ZFIN.
DR GO; GO:0030902; P:hindbrain development; IMP:ZFIN.
DR GO; GO:0007498; P:mesoderm development; IMP:ZFIN.
DR GO; GO:0001707; P:mesoderm formation; IMP:ZFIN.
DR GO; GO:0001710; P:mesodermal cell fate commitment; IGI:ZFIN.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IGI:ZFIN.
DR GO; GO:0014036; P:neural crest cell fate specification; IMP:ZFIN.
DR GO; GO:0021999; P:neural plate anterior/posterior regionalization; IGI:ZFIN.
DR GO; GO:0060896; P:neural plate pattern specification; IDA:ZFIN.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0030903; P:notochord development; IMP:ZFIN.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; IMP:ZFIN.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:ZFIN.
DR GO; GO:0036342; P:post-anal tail morphogenesis; IMP:ZFIN.
DR GO; GO:2000742; P:regulation of anterior head development; IGI:ZFIN.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:ZFIN.
DR GO; GO:0001756; P:somitogenesis; IGI:ZFIN.
DR GO; GO:0060061; P:Spemann organizer formation; IMP:ZFIN.
DR GO; GO:0021512; P:spinal cord anterior/posterior patterning; IMP:ZFIN.
DR GO; GO:0016055; P:Wnt signaling pathway; IGI:ZFIN.
DR GO; GO:0044332; P:Wnt signaling pathway involved in dorsal/ventral axis specification; IMP:BHF-UCL.
DR Gene3D; 3.30.2460.20; -; 1.
DR InterPro; IPR034312; Protein_Wnt-8A/8C.
DR InterPro; IPR005817; Wnt.
DR InterPro; IPR013301; Wnt8.
DR InterPro; IPR043158; Wnt_C.
DR InterPro; IPR018161; Wnt_CS.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR12027; PTHR12027; 1.
DR PANTHER; PTHR12027:SF92; PTHR12027:SF92; 1.
DR Pfam; PF00110; wnt; 1.
DR PRINTS; PR01892; WNT8PROTEIN.
DR PRINTS; PR01349; WNTPROTEIN.
DR SMART; SM00097; WNT1; 1.
DR PROSITE; PS00246; WNT1; 1.
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..25
FT /evidence="ECO:0000255"
FT CHAIN 26..359
FT /note="Protein Wnt-8a"
FT /id="PRO_0000041446"
FT LIPID 187
FT /note="O-palmitoleoyl serine"
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 55..66
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 105..113
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 115..133
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 181..195
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 183..190
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 260..298
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 276..291
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 295..337
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 313..328
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 315..325
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 320..321
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT CONFLICT 244
FT /note="A -> S (in Ref. 3; AAH55535)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="Q -> R (in Ref. 3; AAH55535)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 359 AA; 40289 MW; C192475B9D48C3C2 CRC64;
MNPCQIFASL VMSICCHILS STAWSVNNFL MTGPKAYLAY TSSVQAGAQS GIEECKHQFA
WDRWNCPESA LQLSTHKGLR SATRETAFVH AISAAGVMYT LTKNCSMGDF ENCGCDDSKI
GKMGGRGWVW GGCSDNVNFG DRIAKLFVDA LENGHDSRAA VNLHNNEAGR LAVKATLKRT
CKCHGLSGSC SIQTCWMQLA DFRDIGSYLK IKHDQARKLE MDKIRMRAGN SADNRGAIAD
TFSAVARTEL IFMEDSPDYC VKNLSMGLHG TEGRECLQSG KNLSQWERRS CRRLCHECGL
KVEERRIETV SSCNCKFHWC CTVKCETCTQ TVTRYFCAKR HRNRRPHNHS RKRQHTRRG
