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WNT2_CALJA
ID   WNT2_CALJA              Reviewed;         360 AA.
AC   Q2QLG1;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Protein Wnt-2;
DE   Flags: Precursor;
GN   Name=WNT2;
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483;
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 (OCT-2005) to the EMBL/GenBank/DDBJ databases.
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 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; DP000014; ABA90395.1; -; Genomic_DNA.
DR   RefSeq; XP_002751822.1; XM_002751776.4.
DR   AlphaFoldDB; Q2QLG1; -.
DR   SMR; Q2QLG1; -.
DR   STRING; 9483.ENSCJAP00000009098; -.
DR   Ensembl; ENSCJAT00000009611; ENSCJAP00000009098; ENSCJAG00000004983.
DR   GeneID; 100411308; -.
DR   KEGG; cjc:100411308; -.
DR   CTD; 7472; -.
DR   eggNOG; KOG3913; Eukaryota.
DR   GeneTree; ENSGT00940000159231; -.
DR   HOGENOM; CLU_033039_1_4_1; -.
DR   InParanoid; Q2QLG1; -.
DR   OMA; PKSADWT; -.
DR   OrthoDB; 745245at2759; -.
DR   TreeFam; TF105310; -.
DR   Proteomes; UP000008225; Chromosome 8.
DR   Bgee; ENSCJAG00000004983; Expressed in cerebellum and 2 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-SubCell.
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: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: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..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..360
FT                   /note="Protein Wnt-2"
FT                   /id="PRO_0000226061"
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;  40475 MW;  D9D15592A073BC04 CRC64;
     MNSPLRGIWL WLPLLLTWLT PEVSSSWWYM GATGGSSRVM CDNVPGLVSS QRQLCHRHPD
     VMRAIGLGVT EWTSECQYQF RQHRWNCNTL DRDHSLFGRV LLRSSRESAF VYAISSAGVV
     FAVTRACSQG EVKSCSCDPK KMGSGKDSKG VFDWGGCSDN IDYGIKFARA FVDAKERKGK
     DARALMNLHN NRAGRKSVKR FLKQECKCHG VSGSCSLRTC WLAMADFRKT GDYLWRKYNG
     AIQVVMNQDG TGFTVANERF KKPTKNDLVY FENSPDYCIR DRETGSLGTA GRVCNLTSRG
     MDSCEVMCCG RGYDTSHVTR MIKCGCKFHW CCAVRCQDCL EALDVHTCKA PKNADWKSPT
 
 
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