ID   WNT1_PITME              Reviewed;         126 AA.
AC   P28139;
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-1;
DE   Flags: Fragment;
GN   Name=WNT-1;
OS   Pituophis melanoleucus (Pine snake) (Coluber melanoleucus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Colubridae; Colubrinae; Pituophis.
OX   NCBI_TaxID=8595;
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. Acts in the canonical Wnt signaling pathway by
CC       promoting beta-catenin-dependent transcriptional activation (By
CC       similarity). Plays an essential role in the development of the
CC       embryonic brain and central nervous system (CNS) (By similarity). Has a
CC       role in osteoblast function, bone development and bone homeostasis (By
CC       similarity). {ECO:0000250|UniProtKB:P04426,
CC       ECO:0000250|UniProtKB:P04628}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250|UniProtKB:P04628}. Secreted
CC       {ECO:0000250|UniProtKB:P04628}.
CC   -!- PTM: Palmitoleoylation is required for efficient binding to frizzled
CC       receptors. Palmitoleoylation is necessary for proper trafficking to
CC       cell surface (By similarity). Depalmitoleoylated by NOTUM, leading to
CC       inhibit Wnt signaling pathway (By similarity).
CC       {ECO:0000250|UniProtKB:P56704, ECO:0000250|UniProtKB:Q91029}.
CC   -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000305}.
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DR   EMBL; M91296; AAA49454.1; -; Genomic_DNA.
DR   AlphaFoldDB; P28139; -.
DR   SMR; P28139; -.
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; IPR009139; Wnt1.
DR   InterPro; IPR043158; Wnt_C.
DR   PANTHER; PTHR12027; PTHR12027; 1.
DR   Pfam; PF00110; wnt; 1.
DR   PRINTS; PR01841; WNT1PROTEIN.
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..>126
FT                   /note="Protein Wnt-1"
FT                   /id="PRO_0000200605"
FT   LIPID           1
FT                   /note="O-palmitoleoyl serine; by PORCN"
FT                   /evidence="ECO:0000250|UniProtKB:Q91029"
FT   CARBOHYD        93
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        123
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        92..107
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   NON_TER         1
FT   NON_TER         126
SQ   SEQUENCE   126 AA;  14020 MW;  4C1AEDC4FECFB8B5 CRC64;
     SGSCTVKTCW MRLPTFRTVG DFLKDRFDGA SRVIYGNKGS NRASRMELHH LEPENPAHKP
     PSPHDLVYFE KSPNFCTYSG KTGTAGTAGR FCNSTSPALD GCELLCCGRG YRTRTQRVTE
     RCNCTF