ID   WNT1_EVATR              Reviewed;         143 AA.
AC   P28089;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Protein Wnt-1;
DE   Flags: Fragment;
GN   Name=WNT-1;
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. Probable developmental protein.
CC       {ECO:0000250|UniProtKB:Q91029}.
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; M91272; AAA29130.1; -; Genomic_DNA.
DR   AlphaFoldDB; P28089; -.
DR   SMR; P28089; -.
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..>143
FT                   /note="Protein Wnt-1"
FT                   /id="PRO_0000200604"
FT   REGION          38..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..61
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           1
FT                   /note="O-palmitoleoyl serine; by PORCN"
FT                   /evidence="ECO:0000250|UniProtKB:Q91029"
FT   CARBOHYD        110
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        111
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        109..124
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   NON_TER         1
FT   NON_TER         143
SQ   SEQUENCE   143 AA;  15918 MW;  F42A719CA4424DCB CRC64;
     SGTCTIETCW MRLPTFRSVG EFLKDRFDGA SRVALRNEGV RGNSNRGDRG DRRDRGDRSD
     NGGTEANFQP YNSNHKPPGP RDLVYFDDSP DFCVRNERAG TLGTVGRECN NTSLGVDGCD
     LMCCGRDYDG SEVRIKERCS CTF