ID   WNT1_AMBME              Reviewed;         369 AA.
AC   P21551;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Protein Wnt-1;
DE   Flags: Precursor;
GN   Name=WNT-1;
OS   Ambystoma mexicanum (Axolotl).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Caudata; Salamandroidea; Ambystomatidae; Ambystoma.
OX   NCBI_TaxID=8296;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2259633; DOI=10.1093/nar/18.24.7439;
RA   Busse U., Guay J., Seguin C.;
RT   "Nucleotide sequence of a cDNA encoding Wnt-1 of the Mexican axolotl
RT   Ambystoma mexicanum.";
RL   Nucleic Acids Res. 18:7439-7439(1990).
RN   [2]
RP   ERRATUM OF PUBMED:2259633.
RX   PubMed=2017393; DOI=10.1093/nar/19.4.981;
RA   Busse U., Guay J., Seguin C.;
RL   Nucleic Acids Res. 19:981-981(1991).
RN   [3]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=8508949; DOI=10.1111/j.1432-0436.1993.tb00640.x;
RA   Busse U., Seguin C.;
RT   "Molecular analysis of the Wnt-1 proto-oncogene in Ambystoma mexicanum
RT   (axolotl) embryos.";
RL   Differentiation 53:7-15(1993).
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   -!- DEVELOPMENTAL STAGE: Early blastula until gastrulation, barely
CC       expressed during gastrulation and present again from neurulation until
CC       late embryogenesis. {ECO:0000269|PubMed:8508949}.
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; X55270; CAA38991.1; -; mRNA.
DR   PIR; S13721; S13721.
DR   AlphaFoldDB; P21551; -.
DR   SMR; P21551; -.
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; IPR009139; Wnt1.
DR   InterPro; IPR043158; Wnt_C.
DR   InterPro; IPR018161; Wnt_CS.
DR   PANTHER; PTHR12027; PTHR12027; 1.
DR   Pfam; PF00110; wnt; 1.
DR   PRINTS; PR01841; WNT1PROTEIN.
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; Secreted; Signal; Wnt signaling pathway.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..369
FT                   /note="Protein Wnt-1"
FT                   /id="PRO_0000041407"
FT   REGION          263..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           223
FT                   /note="O-palmitoleoyl serine; by PORCN"
FT                   /evidence="ECO:0000250|UniProtKB:Q91029"
FT   CARBOHYD        28
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        315
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        358
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        92..103
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        142..150
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        152..169
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        217..231
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        219..226
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        298..329
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        314..324
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        328..368
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        344..359
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        346..356
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        351..352
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
SQ   SEQUENCE   369 AA;  41383 MW;  DC215A620F619321 CRC64;
     MRPMTFIVGL KTLWILAFSS LSNTLAVNNS GRWWGVVNVV TSTNLLTDTK NVQLVLDPSL
     QLLSRKQRKL IRQNPGILHS INSGLQSAMK ECKWQFRSRR WNCPTTGGDN IFGKIVNKGC
     RETAFIFAIT SAGVTHSVAR SCSEGSIESC TCDYRRRGPG GTDWHWGGCS DNIDFGRVFG
     REFVDSSERG RDLRYLMNRH NNEAGRMTVF SEMKQECKCH GMSGSCAVRT CWMRLPTFRA
     VGDFLKDRFD GASRVIYGNK GSNRASRVQT HHLEPENPTH KPPSPQDLVY FEKSPNFCTY
     NGKTGTSGTS GRVCNSSSLG LDGCELLCCG RGYRTKTQRV TERCHCTFHW CCHVSCLNCT
     NTQVLHECL