ID   WNT2_ATEGE              Reviewed;         360 AA.
AC   Q09YK7;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=Protein Wnt-2;
DE   Flags: Precursor;
GN   Name=WNT2;
OS   Ateles geoffroyi (Black-handed spider monkey) (Geoffroy's spider monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Atelidae;
OC   Atelinae; Ateles.
OX   NCBI_TaxID=9509;
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; DP000177; ABI75273.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q09YK7; -.
DR   SMR; Q09YK7; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
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; 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_0000260339"
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;  40460 MW;  10BAD277AE023FDB CRC64;
     MNSPLRGIWL WLPLLLTWLT PEVSSSWWYM GATGGSSRVM CDNVPGLVSS QRQLCHRHPD
     VMRAIGLGVT EWTAECQYQF RQHRWNCNTL DRDHSLFGRV LLRSSRESAF VYAISSAGVV
     FAITRACSQG EVKSCSCDPK KMGSGKDSKG VFDWGGCSDN IDYGIKFARA FVDAKERKGK
     DARALMNLHN NRAGRKSVKR FLKQECKCHG VSGSCSLRTC WLAMADFRKT GDYLWRKYNG
     AIQVVMNQDG TGFTVANERF KKPTKNDLVY FENSPDYCIR DRETGSLGTA GRVCNLTSRG
     MDSCEVMCCG RGYDTSHVTR MIKCGCKFHW CCAVRCQDCL EALDVHTCKA PKNADWTTPT