ID   WNT2_RHIFE              Reviewed;         360 AA.
AC   Q2IBB5;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=Protein Wnt-2;
DE   Flags: Precursor;
GN   Name=WNT2;
OS   Rhinolophus ferrumequinum (Greater horseshoe bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Rhinolophidae;
OC   Rhinolophinae; Rhinolophus.
OX   NCBI_TaxID=59479;
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 (JAN-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; DP000028; ABC87478.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2IBB5; -.
DR   SMR; Q2IBB5; -.
DR   Ensembl; ENSRFET00010030511; ENSRFEP00010028108; ENSRFEG00010018681.
DR   GeneTree; ENSGT00940000159231; -.
DR   OMA; PKSADWT; -.
DR   Proteomes; UP000472240; Chromosome 26.
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: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_0000248067"
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;  40387 MW;  4EAC6B58DFC6D20C CRC64;
     MNAPVGGIWL WLPLLLTWLS PEVSSSWWYM KATGGSSRVM CDNVPGLVSR QRQLCHRHPD
     VMRAIGLGVA EWTAECQHQF RQHRWNCNTL DRDHSLFGRV LLRSSRESAF VYAISSAGVV
     FAVTRACSQG ELKSCSCDPK KKGTAKDSKG TFDWGGCSDN IDYGIKFARA FVDAKERKGK
     DARALMNVHN NRAGRKAVKR FLKQECKCHG VSGSCTLRTC WLAMADFRKT GDYLWRRYNG
     AIQVVMNQDG TGFTVANKRF KKPTKNDLVY FENSPDYCIR DRDAGSLGTA GRVCNLTSRG
     MDSCEVMCCG RGYDTSRVTR MTKCECKFHW CCAVRCQDCL EALDVHTCKA PKSADWAAPT