WNT3_EVATR
ID WNT3_EVATR Reviewed; 124 AA.
AC P28090;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Protein Wnt-3;
DE Flags: Fragment;
GN Name=WNT-3;
OS Evasterias troschelii (Mottled sea star) (Asterias troschelii).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Asterozoa; Asteroidea;
OC Forcipulatacea; Forcipulatida; Asteriidae; Evasterias.
OX NCBI_TaxID=7616;
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 (By similarity). Functions in the canonical Wnt
CC signaling pathway that results in activation of transcription factors
CC of the TCF/LEF family (By similarity). Required for normal embryonic
CC development (By similarity). {ECO:0000250|UniProtKB:P17553,
CC ECO:0000250|UniProtKB:P56703}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:P56703}. Secreted
CC {ECO:0000250|UniProtKB:P56703}.
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; M91273; AAA29131.1; -; Genomic_DNA.
DR AlphaFoldDB; P28090; -.
DR SMR; P28090; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 3.30.2460.20; -; 1.
DR InterPro; IPR005817; Wnt.
DR InterPro; IPR043158; Wnt_C.
DR PANTHER; PTHR12027; PTHR12027; 1.
DR Pfam; PF00110; wnt; 1.
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..>124
FT /note="Protein Wnt-3"
FT /id="PRO_0000200610"
FT REGION 40..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1
FT /note="O-palmitoleoyl serine; by PORCN"
FT /evidence="ECO:0000250|UniProtKB:P56704"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 90..105
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT NON_TER 1
FT NON_TER 124
SQ SEQUENCE 124 AA; 14040 MW; 9C2A6756BC431C1A CRC64;
SGSCEVKTCW MQTPHFKEVG DRLLVKYQNA KRVVARNSIG GGLGLANVPK KKRKRAPPPP
EDQLVFLEDS PNFCNPDGEI GIFGTKDRYC NRTSDGADRC DTMCCGRGYN IKLERRTEWC
YCQF