ID   WNT2_ORNAN              Reviewed;         361 AA.
AC   Q07DZ8;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Protein Wnt-2;
DE   Flags: Precursor;
GN   Name=WNT2;
OS   Ornithorhynchus anatinus (Duckbill platypus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX   NCBI_TaxID=9258;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Antonellis A., Ayele K., Benjamin B., Blakesley R.W., Boakye A.,
RA   Bouffard G.G., Brinkley C., Brooks S., Chu G., Coleman H., Engle J.,
RA   Gestole M., Greene A., Guan X., Gupta J., Haghighi P., Han J., Hansen N.,
RA   Ho S.-L., Hu P., Hunter G., Hurle B., Idol J.R., Kwong P., Laric P.,
RA   Larson S., Lee-Lin S.-Q., Legaspi R., Madden M., Maduro Q.L., Maduro V.B.,
RA   Margulies E.H., Masiello C., Maskeri B., McDowell J., Mojidi H.A.,
RA   Mullikin J.C., Oestreicher J.S., Park M., Portnoy M.E., Prasad A., Puri O.,
RA   Reddix-Dugue N., Schandler K., Schueler M.G., Sison C., Stantripop S.,
RA   Stephen E., Taye A., Thomas J.W., Thomas P.J., Tsipouri V., Ung L.,
RA   Vogt J.L., Wetherby K.D., Young A., Green E.D.;
RT   "NISC comparative sequencing initiative.";
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Ligand for members of the frizzled family of seven
CC       transmembrane receptors. Probable developmental protein. May be a
CC       signaling molecule which affects the development of discrete regions of
CC       tissues. Is likely to signal over only few cell diameters (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}.
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; DP000185; ABI93678.1; -; Genomic_DNA.
DR   RefSeq; NP_001229667.1; NM_001242738.1.
DR   AlphaFoldDB; Q07DZ8; -.
DR   SMR; Q07DZ8; -.
DR   STRING; 9258.ENSOANP00000013967; -.
DR   Ensembl; ENSOANT00000064799; ENSOANP00000049932; ENSOANG00000008766.
DR   GeneID; 100077640; -.
DR   KEGG; oaa:100077640; -.
DR   CTD; 7472; -.
DR   eggNOG; KOG3913; Eukaryota.
DR   GeneTree; ENSGT00940000159231; -.
DR   InParanoid; Q07DZ8; -.
DR   OrthoDB; 745245at2759; -.
DR   Proteomes; UP000002279; Chromosome 10.
DR   Bgee; ENSOANG00000008766; Expressed in ovary and 6 other 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-KW.
DR   GO; GO:0031232; C:extrinsic component of external side of plasma membrane; IEA:Ensembl.
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:1904954; P:canonical Wnt signaling pathway involved in midbrain dopaminergic neuron differentiation; 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: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:0060045; P:positive regulation of cardiac muscle cell proliferation; IEA:Ensembl.
DR   GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; 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   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; PTHR12027; 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..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..361
FT                   /note="Protein Wnt-2"
FT                   /id="PRO_0000260347"
FT   LIPID           213
FT                   /note="O-palmitoleoyl serine; by PORCN"
FT                   /evidence="ECO:0000250|UniProtKB:P56704"
FT   CARBOHYD        296
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        77..88
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        128..136
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        138..158
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        207..221
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        209..216
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        279..310
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        295..305
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        309..349
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        325..340
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        327..337
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        332..333
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
SQ   SEQUENCE   361 AA;  40114 MW;  674EF359A8EBE99E CRC64;
     MNASVLGLCL SGPLVLLLAW LAPPVTSSWW YMRAAGSSRV MCDNVPGLVS RQRQLCHRHP
     EVMRSIGLGI AEWTAECQHQ FRQHRWNCNT LDRDHSLFGR VLLRSSREAA FVYAISSAGV
     VFAITRACSQ GELKSCSCDP KKKGSAKDSK GTFDWGGCSD NIDYGIKFAR AFVDAKERKG
     KDARALMNLH NNRAGRKAVK RFLKQECKCH GVSGSCTLRT CWLAMADFRK TGDYLWRKYN
     GAIQVVMNQD GTGFTVANKR FKKPTKNDLV YFENSPDYCI KDRDAGSLGT AGRVCNLTSR
     GMDSCEVMCC GRGYDTARVT RMTKCECKFH WCCAVRCQDC LEALDVHTCK APSSASEGAP
     T