WNT2_HORSE
ID WNT2_HORSE Reviewed; 360 AA.
AC Q2QLA5;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Protein Wnt-2;
DE Flags: Precursor;
GN Name=WNT2;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
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 (NOV-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; DP000020; ABB89804.1; -; Genomic_DNA.
DR RefSeq; NP_001107622.1; NM_001114150.1.
DR AlphaFoldDB; Q2QLA5; -.
DR SMR; Q2QLA5; -.
DR STRING; 9796.ENSECAP00000022226; -.
DR PaxDb; Q2QLA5; -.
DR Ensembl; ENSECAT00000026622; ENSECAP00000022226; ENSECAG00000024641.
DR GeneID; 100056092; -.
DR KEGG; ecb:100056092; -.
DR CTD; 7472; -.
DR VGNC; VGNC:25044; WNT2.
DR GeneTree; ENSGT00940000159231; -.
DR HOGENOM; CLU_033039_1_4_1; -.
DR InParanoid; Q2QLA5; -.
DR OMA; PKSADWT; -.
DR OrthoDB; 745245at2759; -.
DR TreeFam; TF105310; -.
DR Proteomes; UP000002281; Chromosome 4.
DR Bgee; ENSECAG00000024641; Expressed in endometrium and 13 other tissues.
DR ExpressionAtlas; Q2QLA5; baseline.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0031232; C:extrinsic component of external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR GO; GO:0005109; F:frizzled binding; IBA:GO_Central.
DR GO; GO:0055009; P:atrial cardiac muscle tissue morphogenesis; IEA:Ensembl.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
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:0045165; P:cell fate commitment; IBA:GO_Central.
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:0030182; P:neuron differentiation; IBA:GO_Central.
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_0000226064"
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; 40443 MW; 5B122A940F0D1CA7 CRC64;
MNAPLGGIWL WLPLLLTWLT PEVSSSWWYM RATGGASRVM CDNVPGLVSR QRQLCHRHPD
VMRAIGLGVA EWTAECQHQF RQHRWNCNTL DRDHSLFGRV LLRSSRESAF VYAISSAGVV
FAITRACSQG ELRSCSCDPK KKGTAKDSKG TFDWGGCSDN IDYGIKFARA FVDAKERKGK
DARALMNLHN NRAGRKAVKR FLKQECKCHG VSGSCTLRTC WLAMADFRKT GDYLWRKYNG
AIQVVMNQDG TGFTVANKKF KKPTKNDLVY FENSPDYCIR DRDAGSLGTA GRVCNLTSRG
MDSCEVMCCG RGYDTSRVTR MTKCECKFHW CCAVRCQDCL EALDVHTCKA PKSADWASPT
