ID   WNT2_CHLAE              Reviewed;         360 AA.
AC   Q2IBB0;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Protein Wnt-2;
DE   Flags: Precursor;
GN   Name=WNT2;
OS   Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=9534;
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; DP000029; ABC87489.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2IBB0; -.
DR   SMR; Q2IBB0; -.
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_0000248065"
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;  40444 MW;  AA8C825BF68C4788 CRC64;
     MNAPLGGIWL WLPLLLTWLT PEVNSSWWYM RATGGSSRVM CDNVPGLVSS QRQLCHRHPD
     VMRAISQGVA EWTAECQHQF RQHRWNCNTL DRDHSLFGRV LLRSSRESAF VYAISSAGVV
     FAITRACSQG EVKSCSCDPK KMGSAKDSKG IFDWGGCSDN IDYGIKFARA FVDAKERKGK
     DARALMNLHN NRAGRKAVKR FLKQECKCHG VSGSCTLRTC WLAMADFRKT GDYLWRKYNG
     AIQVVMNQDG TGFTVANERF KKPTKNDLVY FENSPDYCIR DREAGSLGTA GRVCNLTSRG
     MDSCEVMCCG RGYDTSHVTR MTKCGCKFHW CCAVRCQDCL EALDVHTCKA PKNADWTTPT