ID   WNT3A_SCEOC             Reviewed;         123 AA.
AC   P28142;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Protein Wnt-3a;
DE   Flags: Fragment;
GN   Name=WNT-3A;
OS   Sceloporus occidentalis (Western fence lizard).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Iguania; Phrynosomatidae; Phrynosomatinae; Sceloporus.
OX   NCBI_TaxID=8519;
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. 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   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250|UniProtKB:P27467}. Secreted
CC       {ECO:0000250|UniProtKB:P27467}.
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; M91299; AAA49542.1; -; Genomic_DNA.
DR   AlphaFoldDB; P28142; -.
DR   SMR; P28142; -.
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; ISS:UniProtKB.
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..>123
FT                   /note="Protein Wnt-3a"
FT                   /id="PRO_0000200617"
FT   LIPID           1
FT                   /note="O-palmitoleoyl serine"
FT                   /evidence="ECO:0000250|UniProtKB:P56704"
FT   CARBOHYD        90
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        89..104
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   NON_TER         1
FT   NON_TER         123
SQ   SEQUENCE   123 AA;  14296 MW;  66A1E9CF05BBBC6F CRC64;
     SGSCEVKTCW WSQPDFRVIG DYLKDKYDSA SEMVVEKHRE SRGWVETLRP KYNFFKAPTE
     RDLVYYENSP NFCEPNPETG SFGTRDRICN VTSHGIDGCD LLCCGRGHNT RTEKRKEKCH
     CIF