WNT8B_DANRE
ID WNT8B_DANRE Reviewed; 358 AA.
AC P51029;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Protein Wnt-8b;
DE Flags: Precursor;
GN Name=wnt8b; Synonyms=wnt-8b;
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].
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).
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. May play a
CC role in the establishment of polarity in the nervous system.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- TISSUE SPECIFICITY: Hindbrain r1, 2 and 5.
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}.
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DR EMBL; U10870; AAC59698.1; -; mRNA.
DR PIR; I50506; I50506.
DR RefSeq; NP_571034.1; NM_130959.2.
DR AlphaFoldDB; P51029; -.
DR SMR; P51029; -.
DR BioGRID; 78377; 2.
DR STRING; 7955.ENSDARP00000049623; -.
DR PaxDb; P51029; -.
DR PRIDE; P51029; -.
DR GeneID; 30144; -.
DR KEGG; dre:30144; -.
DR CTD; 7479; -.
DR ZFIN; ZDB-GENE-990415-279; wnt8b.
DR eggNOG; KOG3913; Eukaryota.
DR InParanoid; P51029; -.
DR OrthoDB; 618621at2759; -.
DR PhylomeDB; P51029; -.
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 SignaLink; P51029; -.
DR PRO; PR:P51029; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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:0060070; P:canonical Wnt signaling pathway; IGI:ZFIN.
DR GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR GO; GO:0071679; P:commissural neuron axon guidance; IMP:ZFIN.
DR GO; GO:0009880; P:embryonic pattern specification; IGI:ZFIN.
DR GO; GO:0001654; P:eye development; IDA:ZFIN.
DR GO; GO:0060898; P:eye field cell fate commitment involved in camera-type eye formation; IGI:ZFIN.
DR GO; GO:0030900; P:forebrain development; IDA:ZFIN.
DR GO; GO:0021879; P:forebrain neuron differentiation; IMP:ZFIN.
DR GO; GO:0021854; P:hypothalamus development; IMP:ZFIN.
DR GO; GO:0022002; P:negative regulation of anterior neural cell fate commitment of the neural plate by Wnt signaling pathway; IMP:ZFIN.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0043049; P:otic placode formation; IMP:ZFIN.
DR GO; GO:0070654; P:sensory epithelium regeneration; IEP:ZFIN.
DR Gene3D; 3.30.2460.20; -; 1.
DR InterPro; IPR034311; Protein_Wnt-8B.
DR InterPro; IPR005817; Wnt.
DR InterPro; IPR013301; Wnt8.
DR InterPro; IPR043158; Wnt_C.
DR InterPro; IPR018161; Wnt_CS.
DR PANTHER; PTHR12027; PTHR12027; 1.
DR PANTHER; PTHR12027:SF94; PTHR12027:SF94; 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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..358
FT /note="Protein Wnt-8b"
FT /id="PRO_0000041452"
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 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
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 257..295
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 273..288
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 292..334
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 310..325
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 312..322
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 317..318
FT /evidence="ECO:0000250|UniProtKB:P28026"
SQ SEQUENCE 358 AA; 40343 MW; 3CCB93B0772BF4A8 CRC64;
MFMHLEVYYY AFILMAHMKT CCGWSVNNFL MTGPKAYLIY SSSVAAGAQS GIEECKYQFA
WDRWKCPERA LQLSTHSGLR SANRETAFFH AISSAGVMYT LTRNCSLGDF DNCGCDDTRN
GQRGGQGWLW GGCSDNVGFG EVISKQFVDA LETGQDARAA MNLHNNEVGR KAVKGTMQRT
CKCHGVSGSC TTQTCWLQLP EFREVGNYLK EKYHRAVKVD LLRGAGNSAA SRGAIAETFN
SISRKELVHL EDSPDYCLEN RTLGLPGTEG RECLRKGKNL SKWEKRTCKR LCGDCGLAVE
ERRAETVSSC NCKFHWCCAV KCEQCRKTVT KYYCVKRSKR VKNDNASRRK SYRLKKKH
