ID   WNT2_ECHTE              Reviewed;         359 AA.
AC   A1X153;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=Protein Wnt-2;
DE   Flags: Precursor;
GN   Name=WNT2;
OS   Echinops telfairi (Lesser hedgehog tenrec).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Tenrecidae; Tenrecinae; Echinops.
OX   NCBI_TaxID=9371;
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 (DEC-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; DP000274; ABL76169.1; -; Genomic_DNA.
DR   RefSeq; XP_004707826.1; XM_004707769.1.
DR   AlphaFoldDB; A1X153; -.
DR   SMR; A1X153; -.
DR   GlyCosmos; A1X153; 1 site, No reported glycans.
DR   GeneID; 101651785; -.
DR   KEGG; etf:101651785; -.
DR   CTD; 7472; -.
DR   HOGENOM; CLU_033039_1_4_1; -.
DR   OrthoDB; 2874082at2759; -.
DR   TreeFam; TF105310; -.
DR   Proteomes; UP000694863; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR   GO; GO:0048731; P:system development; IEA:UniProt.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   CDD; cd19345; Wnt_Wnt2; 1.
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:SF86; PROTEIN WNT-2; 1.
DR   PANTHER; PTHR12027; WNT RELATED; 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..359
FT                   /note="Protein Wnt-2"
FT                   /id="PRO_0000279197"
FT   LIPID           211
FT                   /note="O-palmitoleoyl serine; by PORCN"
FT                   /evidence="ECO:0000250|UniProtKB:P56704"
FT   CARBOHYD        294
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        75..86
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        126..134
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        136..156
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        205..219
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        207..214
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        277..308
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        293..303
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        307..347
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        323..338
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        325..335
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
FT   DISULFID        330..331
FT                   /evidence="ECO:0000250|UniProtKB:P28026"
SQ   SEQUENCE   359 AA;  40452 MW;  D872D4D268106543 CRC64;
     MNAPLAGIWP WLPLLWAWLV PEVSSSWWYM RATGTSRVMC DNVPGLVSRQ RQLCHRHPDV
     MRAIGLGVAE WTAECQHQFR QHRWNCDTLD RDHSLFGRLL LRSSRESAFV YAISSAGVVF
     AITRACSQGE LKSCSCDPKK KGTAKDSRGT FDWGGCSDNI DYGVKFARAF VDAKEKKGKD
     ARALMNLHNN RAGRKAVKRF LKQECKCHGV SGSCTLRTCW LAMADFRKTG DYLWRKYNGA
     IQVVMNQDGT GFTVANKRFK KPTKNDLVYF ENSPDYCIRD RDAGSPGTAG RVCNLTSRGM
     DSCEVMCCGR GYDTSRVTRM TKCECKFHWC CAVRCQDCLE ALDVHTCKAP KSADWAVPT
//