ID   WNT3A_XENLA             Reviewed;         352 AA.
AC   P31285;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Protein Wnt-3a;
DE            Short=XWnt-3a;
DE   Flags: Precursor;
GN   Name=wnt3a;
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].
RX   PubMed=8416844; DOI=10.1006/dbio.1993.1005;
RA   Wolda S.L., Moody C.J., Moon R.T.;
RT   "Overlapping expression of Xwnt-3A and Xwnt-1 in neural tissue of Xenopus
RT   laevis embryos.";
RL   Dev. Biol. 155:46-57(1993).
CC   -!- FUNCTION: Ligand for members of the frizzled family of seven
CC       transmembrane receptors. Functions in the canonical Wnt signaling
CC       pathway that results in activation of transcription factors of the
CC       TCF/LEF family. Required for normal embryonic mesoderm development and
CC       formation of caudal somites. Required for normal morphogenesis of the
CC       developing neural tube. {ECO:0000250|UniProtKB:P27467,
CC       ECO:0000250|UniProtKB:P56704}.
CC   -!- INTERACTION:
CC       P31285; Q6PA07: ptk7.L; NbExp=2; IntAct=EBI-7036309, EBI-7036323;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250|UniProtKB:P27467}. Secreted
CC       {ECO:0000250|UniProtKB:P27467}.
CC   -!- TISSUE SPECIFICITY: At neurula in anterior neural fold; at tailbud in
CC       dorsal midline of midbrain.
CC   -!- DEVELOPMENTAL STAGE: Neurula onwards.
CC   -!- PTM: Disulfide bonds have critical and distinct roles in secretion and
CC       activity. Loss of each conserved cysteine results in high molecular
CC       weight oxidized Wnt oligomers, which are formed through inter-Wnt
CC       disulfide bonding. {ECO:0000250|UniProtKB:P27467}.
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; L07538; AAA50009.1; -; mRNA.
DR   PIR; A48828; A48828.
DR   RefSeq; NP_001079343.1; NM_001085874.1.
DR   AlphaFoldDB; P31285; -.
DR   SMR; P31285; -.
DR   IntAct; P31285; 3.
DR   MINT; P31285; -.
DR   PRIDE; P31285; -.
DR   GeneID; 378679; -.
DR   KEGG; xla:378679; -.
DR   CTD; 378679; -.
DR   Xenbase; XB-GENE-1217290; wnt3a.S.
DR   OrthoDB; 965867at2759; -.
DR   Proteomes; UP000186698; Chromosome 6S.
DR   Bgee; 378679; Expressed in zone of skin and 1 other tissue.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0014033; P:neural crest cell differentiation; IDA:BHF-UCL.
DR   GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:BHF-UCL.
DR   Gene3D; 3.30.2460.20; -; 1.
DR   InterPro; IPR005817; Wnt.
DR   InterPro; IPR009141; Wnt3.
DR   InterPro; IPR043158; Wnt_C.
DR   InterPro; IPR018161; Wnt_CS.
DR   PANTHER; PTHR12027; PTHR12027; 1.
DR   Pfam; PF00110; wnt; 1.
DR   PRINTS; PR01843; WNT3PROTEIN.
DR   PRINTS; PR01349; WNTPROTEIN.
DR   SMART; SM00097; WNT1; 1.
DR   PROSITE; PS00246; WNT1; 1.
PE   1: Evidence at protein level;
KW   Developmental protein; Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Lipoprotein; Reference proteome; Secreted; Signal; Wnt signaling pathway.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..352
FT                   /note="Protein Wnt-3a"
FT                   /id="PRO_0000041420"
FT   LIPID           209
FT                   /note="O-palmitoleoyl serine"
FT                   /evidence="ECO:0000250|UniProtKB:P56704"
FT   CARBOHYD        87
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        298
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        77..88
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        128..136
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        138..155
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        203..217
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        205..212
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        297..312
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        327..342
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        329..339
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        334..335
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
SQ   SEQUENCE   352 AA;  39715 MW;  4B5F93F5DF08D6C5 CRC64;
     MGCFGYLLLI IGLHQVLATY PIWWSLAVGQ QYSSLGTQPI PCGTIPGLVA KQMRFCRNYM
     EIMPSVAEGV KIGIQECQHQ FRGRRWNCTT VNDNLAIFGP VLDKATRESA FVHAIASAGV
     AFAVTRSCAE GSATICGCDT HHKGPPGEGW KWGGCSEDMD FGSMVSREFA DARENRPDAR
     SAMNRHNNEA GRTSILDHRH LKCKCHGLSG SCEVKTCWWS QPDFRVIGDY LKDKYDSASE
     MVVEKHRESR GWVETLRPKY TFFKPPIERD LIYYESSPNF CEPNPETGSF GTRDRECNVT
     SHGIDGCDLL CCGRGQNTRT EKRKEKCHCI FHWCCYVSCQ ECMRVYDVHT CK