WNT3_XENLA
ID WNT3_XENLA Reviewed; 137 AA.
AC P31284;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Protein Wnt-3;
DE Short=XWnt-3;
DE Flags: Fragment;
GN Name=wnt3;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=1991549; DOI=10.1016/0012-1606(91)90073-c;
RA Christian J.L., Gavin B.J., McMahon A.P., Moon R.T.;
RT "Isolation of cDNAs partially encoding four Xenopus Wnt-1/int-1-related
RT proteins and characterization of their transient expression during
RT embryonic development.";
RL Dev. Biol. 143:230-234(1991).
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 -!- DEVELOPMENTAL STAGE: Detected at neurula and tadpole stage.
CC {ECO:0000269|PubMed:1991549}.
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; M55054; AAA50010.1; -; mRNA.
DR AlphaFoldDB; P31284; -.
DR SMR; P31284; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
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 InterPro; IPR018161; Wnt_CS.
DR PANTHER; PTHR12027; PTHR12027; 1.
DR Pfam; PF00110; wnt; 1.
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; Wnt signaling pathway.
FT CHAIN <1..>137
FT /note="Protein Wnt-3"
FT /id="PRO_0000200612"
FT LIPID 9
FT /note="O-palmitoleoyl serine; by PORCN"
FT /evidence="ECO:0000250|UniProtKB:P56704"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 3..17
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 5..12
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 97..112
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 134..135
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT NON_TER 1
FT NON_TER 137
SQ SEQUENCE 137 AA; 15940 MW; FF4AB1A7827733B9 CRC64;
QECKCHGLSG SCEVKTCWWS QPDFRVIGDY LKDKYDSASE MVVEQHRESR GWVETLRPKY
TFFKPPTERD LIYYESSPNF CEPNPETGSF GTRDRVCNVS SHGIDGCDLL CCGRGHNTRT
EKRKEKCHCI FHWCCSR