WNT8_THUTH
ID WNT8_THUTH Reviewed; 128 AA.
AC P28146;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Protein Wnt-8;
DE Flags: Fragment;
GN Name=wnt8;
OS Thunnus thynnus (Atlantic bluefin tuna) (Scomber thynnus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Pelagiaria; Scombriformes; Scombridae; Thunnus.
OX NCBI_TaxID=8237;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1534411; DOI=10.1073/pnas.89.11.5098;
RA Sidow A.;
RT "Diversification of the Wnt gene family on the ancestral lineage of
RT vertebrates.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:5098-5102(1992).
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.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
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; M91308; AAA49625.1; -; Genomic_DNA.
DR AlphaFoldDB; P28146; -.
DR SMR; P28146; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
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 PANTHER; PTHR12027; PTHR12027; 1.
DR PANTHER; PTHR12027:SF94; PTHR12027:SF94; 1.
DR Pfam; PF00110; wnt; 1.
DR PRINTS; PR01892; WNT8PROTEIN.
DR SMART; SM00097; WNT1; 1.
PE 3: Inferred from homology;
KW Developmental protein; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Lipoprotein; Secreted; Wnt signaling pathway.
FT CHAIN <1..>128
FT /note="Protein Wnt-8"
FT /id="PRO_0000200659"
FT LIPID 1
FT /note="O-palmitoleoyl serine"
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 71..109
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 87..102
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT NON_TER 1
FT NON_TER 128
SQ SEQUENCE 128 AA; 14293 MW; 849134882DE8C6B9 CRC64;
SGSCTTQTCW LQLPEFREVG NYLKEKYHRA LKVDLLRGAG NSAASRGAIA ETFSSISRKE
LVHLEDSPDY CLENRTLGLP GTEGRECLKK GKNLSKWEKR SCKRLCGECG LAVEERKAEM
VSSCNCKF