ID   WNT2_PAPAN              Reviewed;         360 AA.
AC   A0M8S1;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   24-JAN-2024, entry version 74.
DE   RecName: Full=Protein Wnt-2;
DE   Flags: Precursor;
GN   Name=WNT2;
OS   Papio anubis (Olive baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9555;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12917688; DOI=10.1038/nature01858;
RA   Thomas J.W., Touchman J.W., Blakesley R.W., Bouffard G.G.,
RA   Beckstrom-Sternberg S.M., Margulies E.H., Blanchette M., Siepel A.C.,
RA   Thomas P.J., McDowell J.C., Maskeri B., Hansen N.F., Schwartz M.S.,
RA   Weber R.J., Kent W.J., Karolchik D., Bruen T.C., Bevan R., Cutler D.J.,
RA   Schwartz S., Elnitski L., Idol J.R., Prasad A.B., Lee-Lin S.-Q.,
RA   Maduro V.V.B., Summers T.J., Portnoy M.E., Dietrich N.L., Akhter N.,
RA   Ayele K., Benjamin B., Cariaga K., Brinkley C.P., Brooks S.Y., Granite S.,
RA   Guan X., Gupta J., Haghighi P., Ho S.-L., Huang M.C., Karlins E.,
RA   Laric P.L., Legaspi R., Lim M.J., Maduro Q.L., Masiello C.A.,
RA   Mastrian S.D., McCloskey J.C., Pearson R., Stantripop S., Tiongson E.E.,
RA   Tran J.T., Tsurgeon C., Vogt J.L., Walker M.A., Wetherby K.D.,
RA   Wiggins L.S., Young A.C., Zhang L.-H., Osoegawa K., Zhu B., Zhao B.,
RA   Shu C.L., De Jong P.J., Lawrence C.E., Smit A.F., Chakravarti A.,
RA   Haussler D., Green P., Miller W., Green E.D.;
RT   "Comparative analyses of multi-species sequences from targeted genomic
RT   regions.";
RL   Nature 424:788-793(2003).
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 (By similarity). Functions as a upstream regulator of
CC       FGF10 expression. Plays an important role in embryonic lung
CC       development. May contribute to embryonic brain development by
CC       regulating the proliferation of dopaminergic precursors and neurons (By
CC       similarity). {ECO:0000250|UniProtKB:P09544,
CC       ECO:0000250|UniProtKB:P21552}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250|UniProtKB:P09544}. Secreted
CC       {ECO:0000250|UniProtKB:P09544}.
CC   -!- PTM: Palmitoleoylation is required for efficient binding to frizzled
CC       receptors. Depalmitoleoylation leads to Wnt signaling pathway
CC       inhibition. {ECO:0000250|UniProtKB:P09544}.
CC   -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000305}.
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DR   EMBL; DP000233; AAR16225.1; -; Genomic_DNA.
DR   RefSeq; NP_001162189.1; NM_001168718.1.
DR   AlphaFoldDB; A0M8S1; -.
DR   SMR; A0M8S1; -.
DR   STRING; 9555.ENSPANP00000006658; -.
DR   GlyCosmos; A0M8S1; 1 site, No reported glycans.
DR   Ensembl; ENSPANT00000067785.1; ENSPANP00000060530.1; ENSPANG00000048086.1.
DR   GeneID; 100126674; -.
DR   KEGG; panu:100126674; -.
DR   CTD; 7472; -.
DR   eggNOG; KOG3913; Eukaryota.
DR   GeneTree; ENSGT00940000159231; -.
DR   HOGENOM; CLU_033039_1_4_1; -.
DR   OMA; ITRMTKC; -.
DR   OrthoDB; 2874082at2759; -.
DR   Proteomes; UP000028761; Chromosome 4.
DR   Bgee; ENSPANG00000021495; Expressed in Ammon's horn and 26 other cell types or tissues.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005125; F:cytokine activity; IEA:Ensembl.
DR   GO; GO:0005109; F:frizzled binding; IEA:Ensembl.
DR   GO; GO:0055009; P:atrial cardiac muscle tissue morphogenesis; IEA:Ensembl.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
DR   GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; IEA:Ensembl.
DR   GO; GO:0060038; P:cardiac muscle cell proliferation; IEA:Ensembl.
DR   GO; GO:0033278; P:cell proliferation in midbrain; IEA:Ensembl.
DR   GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
DR   GO; GO:0060502; P:epithelial cell proliferation involved in lung morphogenesis; IEA:Ensembl.
DR   GO; GO:0060716; P:labyrinthine layer blood vessel development; IEA:Ensembl.
DR   GO; GO:0060492; P:lung induction; IEA:Ensembl.
DR   GO; GO:0061180; P:mammary gland epithelium development; IEA:Ensembl.
DR   GO; GO:0010463; P:mesenchymal cell proliferation; IEA:Ensembl.
DR   GO; GO:1904948; P:midbrain dopaminergic neuron differentiation; IEA:Ensembl.
DR   GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IEA:Ensembl.
DR   GO; GO:0060501; P:positive regulation of epithelial cell proliferation involved in lung morphogenesis; IEA:Ensembl.
DR   GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
DR   GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IEA:Ensembl.
DR   GO; GO:0050769; P:positive regulation of neurogenesis; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   CDD; cd19345; Wnt_Wnt2; 1.
DR   Gene3D; 3.30.2460.20; -; 1.
DR   InterPro; IPR005817; Wnt.
DR   InterPro; IPR009140; Wnt2.
DR   InterPro; IPR043158; Wnt_C.
DR   InterPro; IPR018161; Wnt_CS.
DR   PANTHER; PTHR12027:SF86; PROTEIN WNT-2; 1.
DR   PANTHER; PTHR12027; WNT RELATED; 1.
DR   Pfam; PF00110; wnt; 1.
DR   PRINTS; PR01842; WNT2PROTEIN.
DR   PRINTS; PR01349; WNTPROTEIN.
DR   SMART; SM00097; WNT1; 1.
DR   PROSITE; PS00246; WNT1; 1.
PE   3: Inferred from homology;
KW   Developmental protein; Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Lipoprotein; Reference proteome; Secreted; Signal; Wnt signaling pathway.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..360
FT                   /note="Protein Wnt-2"
FT                   /id="PRO_0000279199"
FT   LIPID           212
FT                   /note="O-palmitoleoyl serine; by PORCN"
FT                   /evidence="ECO:0000250|UniProtKB:P56704"
FT   CARBOHYD        295
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        76..87
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        127..135
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        137..157
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        206..220
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        208..215
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        278..309
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        294..304
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        308..348
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        324..339
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        326..336
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        331..332
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
SQ   SEQUENCE   360 AA;  40444 MW;  AA8C825BF68C4788 CRC64;
     MNAPLGGIWL WLPLLLTWLT PEVNSSWWYM RATGGSSRVM CDNVPGLVSS QRQLCHRHPD
     VMRAISQGVA EWTAECQHQF RQHRWNCNTL DRDHSLFGRV LLRSSRESAF VYAISSAGVV
     FAITRACSQG EVKSCSCDPK KMGSAKDSKG IFDWGGCSDN IDYGIKFARA FVDAKERKGK
     DARALMNLHN NRAGRKAVKR FLKQECKCHG VSGSCTLRTC WLAMADFRKT GDYLWRKYNG
     AIQVVMNQDG TGFTVANERF KKPTKNDLVY FENSPDYCIR DREAGSLGTA GRVCNLTSRG
     MDSCEVMCCG RGYDTSHVTR MTKCGCKFHW CCAVRCQDCL EALDVHTCKA PKNADWTTPT
//