WNTG_DROME
ID WNTG_DROME Reviewed; 468 AA.
AC P09615; Q27768; Q27769; Q8IPI1; Q8MQP9; Q9VM27;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 223.
DE RecName: Full=Protein wingless;
DE AltName: Full=Protein Wnt-1;
DE AltName: Full=Protein int-1;
DE AltName: Full=dInt-1;
DE AltName: Full=dWnt-1;
DE Flags: Precursor;
GN Name=wg; ORFNames=CG4889;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=3111720; DOI=10.1016/0092-8674(87)90038-9;
RA Rijsewijk F., Schuermann M., Wagenaar E., Parren P., Weigel D., Nusse R.;
RT "The Drosophila homolog of the mouse mammary oncogene int-1 is identical to
RT the segment polarity gene wingless.";
RL Cell 50:649-657(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND DEVELOPMENTAL STAGE.
RX PubMed=3129722; DOI=10.1073/pnas.85.9.3034;
RA Uzvoelgyi E., Kiss I., Pitt A., Arsenian S., Ingvarsson S., Udvardy A.,
RA Hamada M., Klein G., Suemegi J.;
RT "Drosophila homolog of the murine Int-1 protooncogene.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:3034-3038(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF CYS-104 AND GLY-221.
RX PubMed=8262072;
RA van den Heuvel M., Harryman-Samos C., Klingensmith J., Perrimon N.,
RA Nusse R.;
RT "Mutations in the segment polarity genes wingless and porcupine impair
RT secretion of the wingless protein.";
RL EMBO J. 12:5293-5302(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [5]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [7]
RP SECRETION.
RX PubMed=2582493; DOI=10.1016/0092-8674(89)90020-2;
RA van den Heuvel M., Nusse R., Johnston P., Lawrence P.A.;
RT "Distribution of the wingless gene product in Drosophila embryos: a protein
RT involved in cell-cell communication.";
RL Cell 59:739-749(1989).
RN [8]
RP INTERACTION WITH EN.
RC TISSUE=Embryo;
RX PubMed=1335365; DOI=10.1016/s0092-8674(05)80065-0;
RA Siegfried E., Chou T.B., Perrimon N.;
RT "wingless signaling acts through zeste-white 3, the Drosophila homolog of
RT glycogen synthase kinase-3, to regulate engrailed and establish cell
RT fate.";
RL Cell 71:1167-1179(1992).
RN [9]
RP MUTAGENESIS OF CYS-93 AND CYS-104.
RX PubMed=7954794; DOI=10.1016/0092-8674(94)90195-3;
RA Couso J.P., Martinez Arias A.;
RT "Notch is required for wingless signaling in the epidermis of Drosophila.";
RL Cell 79:259-272(1994).
RN [10]
RP PHOSPHORYLATION OF ARM.
RX PubMed=7529201; DOI=10.1006/dbio.1994.1336;
RA Peifer M., Pai L.-M., Casey M.;
RT "Phosphorylation of the Drosophila adherens junction protein Armadillo:
RT roles for wingless signal and zeste-white 3 kinase.";
RL Dev. Biol. 166:543-556(1994).
RN [11]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11717401; DOI=10.1073/pnas.251304398;
RA Llimargas M., Lawrence P.A.;
RT "Seven Wnt homologues in Drosophila: a case study of the developing
RT tracheae.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:14487-14492(2001).
RN [12]
RP SUBUNIT, INTERACTION WITH PORCUPINE, GLYCOSYLATION AT ASN-103 AND ASN-414,
RP AND MUTAGENESIS OF THR-51; SER-105; SER-110 AND THR-416.
RX PubMed=11821428; DOI=10.1074/jbc.m200187200;
RA Tanaka K., Kitagawa Y., Kadowaki T.;
RT "Drosophila segment polarity gene product porcupine stimulates the
RT posttranslational N-glycosylation of wingless in the endoplasmic
RT reticulum.";
RL J. Biol. Chem. 277:12816-12823(2002).
RN [13]
RP PALMITOLEOYLATION BY PORCUPINE, AND SUBCELLULAR LOCATION.
RX PubMed=15166250; DOI=10.1074/jbc.m403407200;
RA Zhai L., Chaturvedi D., Cumberledge S.;
RT "Drosophila wnt-1 undergoes a hydrophobic modification and is targeted to
RT lipid rafts, a process that requires porcupine.";
RL J. Biol. Chem. 279:33220-33227(2004).
RN [14]
RP ROLE OF LIPOPHORIN IN MOVEMENT.
RX PubMed=15875013; DOI=10.1038/nature03504;
RA Panakova D., Sprong H., Marois E., Thiele C., Eaton S.;
RT "Lipoprotein particles are required for Hedgehog and Wingless signalling.";
RL Nature 435:58-65(2005).
RN [15]
RP FUNCTION, INTERACTION WITH WLS, AND SUBCELLULAR LOCATION.
RX PubMed=18193037; DOI=10.1038/ncb1678;
RA Franch-Marro X., Wendler F., Guidato S., Griffith J., Baena-Lopez A.,
RA Itasaki N., Maurice M.M., Vincent J.P.;
RT "Wingless secretion requires endosome-to-Golgi retrieval of
RT Wntless/Evi/Sprinter by the retromer complex.";
RL Nat. Cell Biol. 10:170-177(2008).
RN [16]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18193032; DOI=10.1038/ncb1687;
RA Port F., Kuster M., Herr P., Furger E., Banziger C., Hausmann G.,
RA Basler K.;
RT "Wingless secretion promotes and requires retromer-dependent cycling of
RT Wntless.";
RL Nat. Cell Biol. 10:178-185(2008).
RN [17]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19837038; DOI=10.1016/j.cell.2009.07.051;
RA Korkut C., Ataman B., Ramachandran P., Ashley J., Barria R., Gherbesi N.,
RA Budnik V.;
RT "Trans-synaptic transmission of vesicular Wnt signals through
RT Evi/Wntless.";
RL Cell 139:393-404(2009).
RN [18]
RP INTERACTION WITH COW.
RX PubMed=25360738; DOI=10.1371/journal.pone.0111573;
RA Chang Y.H., Sun Y.H.;
RT "Carrier of Wingless (Cow), a secreted heparan sulfate proteoglycan,
RT promotes extracellular transport of Wingless.";
RL PLoS ONE 9:E111573-E111573(2014).
RN [19]
RP DEPALMITOLEOYLATION.
RX PubMed=25731175; DOI=10.1038/nature14259;
RA Kakugawa S., Langton P.F., Zebisch M., Howell S.A., Chang T.H., Liu Y.,
RA Feizi T., Bineva G., O'Reilly N., Snijders A.P., Jones E.Y., Vincent J.P.;
RT "Notum deacylates Wnt proteins to suppress signalling activity.";
RL Nature 519:187-192(2015).
RN [20]
RP SUBCELLULAR LOCATION.
RX PubMed=26974662; DOI=10.1038/ncb3325;
RA Yamazaki Y., Palmer L., Alexandre C., Kakugawa S., Beckett K., Gaugue I.,
RA Palmer R.H., Vincent J.P.;
RT "Godzilla-dependent transcytosis promotes Wingless signalling in Drosophila
RT wing imaginal discs.";
RL Nat. Cell Biol. 18:451-457(2016).
CC -!- FUNCTION: Binds as a ligand to a family of frizzled seven-transmembrane
CC receptors and acts through a cascade of genes on the nucleus. Segment
CC polarity protein. May be a growth factor. Acts on neighboring cells to
CC regulate at least one gene, the homeobox segmentation gene engrailed.
CC Wg signal represses arm phosphorylation. Wg signaling operates by
CC inactivating the sgg repression of engrailed autoactivation. Wg and
CC Wnt2 have a role in the developing trachea and together are responsible
CC for all dorsal trunk formation. Wg also acts in the developing
CC epidermis. Acts as a morphogen, and diffuses long distances despite its
CC lipidation. Lipophorin is required for diffusion, probably by acting as
CC vehicle for its movement, explaining how it can spread over long
CC distances despite its lipidation. In non-neuronal cells, wls directs wg
CC secretion via clathrin-mediated endocytosis and the retromer complex (a
CC conserved protein complex consisting of Vps26 and Vps35) to sustain a
CC wls traffic loop encompassing the Golgi, the cell surface, an endocytic
CC compartment and a retrograde route leading back to the Golgi. In
CC neuronal cells (the larval motorneuron NMJ), wg signal moves across the
CC synapse through the release of wls-containing exosome-like vesicles.
CC {ECO:0000269|PubMed:11717401, ECO:0000269|PubMed:18193032,
CC ECO:0000269|PubMed:18193037, ECO:0000269|PubMed:19837038}.
CC -!- SUBUNIT: Monomer; folds by intramolecular disulfide bonds
CC (PubMed:11821428). Interacts with porcupine (por) (PubMed:11821428).
CC Interacts with wls; in the Golgi (PubMed:18193037). Interacts with en
CC (PubMed:1335365). Interacts with the proteoglycan Cow (heparan sulfate-
CC bound form); this stabilizes wg and promotes its extracellular
CC distribution (PubMed:25360738). {ECO:0000269|PubMed:11821428,
CC ECO:0000269|PubMed:1335365, ECO:0000269|PubMed:18193037,
CC ECO:0000269|PubMed:25360738}.
CC -!- INTERACTION:
CC P09615; Q9VXY9: opm; NbExp=2; IntAct=EBI-98242, EBI-7560899;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15166250,
CC ECO:0000269|PubMed:18193037, ECO:0000269|PubMed:26974662,
CC ECO:0000269|PubMed:8262072}. Synapse {ECO:0000269|PubMed:19837038}.
CC Membrane; Lipid-anchor. Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:15166250}. Note=Palmitoleoylation converts
CC wg into a membrane-anchored protein that is partitioned into
CC specialized lipid raft microdomains before secretion (PubMed:15166250).
CC In the wing imaginal disK epithelium, the protein is produced in the
CC apical region of the cell and undergoes transcytosis to the basolateral
CC surface to be released in the extracellular space (PubMed:26974662).
CC Possibly associated with the extracellular matrix (PubMed:15166250).
CC {ECO:0000269|PubMed:15166250, ECO:0000269|PubMed:26974662}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=P09615-1; Sequence=Displayed;
CC Name=B;
CC IsoId=P09615-2; Sequence=VSP_016535;
CC -!- TISSUE SPECIFICITY: Segmented expression in embryos. In embryonic
CC tracheal cells, expression is in stripes flanking the tracheal placode.
CC {ECO:0000269|PubMed:11717401, ECO:0000269|PubMed:3111720}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development, but barely
CC detectable in adults. {ECO:0000269|PubMed:3111720,
CC ECO:0000269|PubMed:3129722}.
CC -!- PTM: Palmitoleoylated by porcupine. The lipid group functions as a
CC sorting signal, targeting the ligand to polarized vesicles that
CC transport wg to unique sites at the cell surface. Depalmitoleoylated by
CC notum, leading to inhibit Wnt signaling pathway.
CC {ECO:0000305|PubMed:11821428, ECO:0000305|PubMed:15166250,
CC ECO:0000305|PubMed:25731175}.
CC -!- PTM: Major form is glycosylated at 2 sites, glycosylation is stimulated
CC by porcupine at the ER. {ECO:0000269|PubMed:11821428}.
CC -!- DISRUPTION PHENOTYPE: Accumulation in the Golgi, thereby preventing
CC secretion. {ECO:0000269|PubMed:18193032}.
CC -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000305}.
CC -!- CAUTION: Was initially thought to be palmitoylated at Ser-239. It was
CC later shown that it is palmitoleoylated. {ECO:0000305}.
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DR EMBL; M17230; AAA28647.1; -; mRNA.
DR EMBL; J03650; AAA28646.1; -; mRNA.
DR EMBL; S67382; AAB29368.1; -; mRNA.
DR EMBL; S67383; AAB29369.1; -; mRNA.
DR EMBL; AE014134; AAF52501.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10628.1; -; Genomic_DNA.
DR EMBL; AY128458; AAM75051.1; -; mRNA.
DR PIR; A29650; A29650.
DR PIR; A31337; TVFFT1.
DR RefSeq; NP_523502.1; NM_078778.5. [P09615-1]
DR AlphaFoldDB; P09615; -.
DR SMR; P09615; -.
DR BioGRID; 60155; 130.
DR DIP; DIP-21777N; -.
DR IntAct; P09615; 1.
DR MINT; P09615; -.
DR STRING; 7227.FBpp0079060; -.
DR GlyGen; P09615; 3 sites.
DR iPTMnet; P09615; -.
DR SwissPalm; P09615; -.
DR PaxDb; P09615; -.
DR PRIDE; P09615; -.
DR EnsemblMetazoa; FBtr0079432; FBpp0079060; FBgn0284084. [P09615-1]
DR GeneID; 34009; -.
DR KEGG; dme:Dmel_CG4889; -.
DR CTD; 474168; -.
DR FlyBase; FBgn0284084; wg.
DR VEuPathDB; VectorBase:FBgn0284084; -.
DR eggNOG; KOG3913; Eukaryota.
DR GeneTree; ENSGT00940000160329; -.
DR HOGENOM; CLU_033039_1_1_1; -.
DR InParanoid; P09615; -.
DR OMA; NDHMPDI; -.
DR PhylomeDB; P09615; -.
DR Reactome; R-DME-201681; TCF dependent signaling in response to WNT.
DR Reactome; R-DME-209387; Phosphorylation of ARR.
DR Reactome; R-DME-209440; Recruitment of the 'destruction complex' to the receptor complex, the degradation of AXN and release of ARM.
DR Reactome; R-DME-209472; Assembly of receptor complex.
DR Reactome; R-DME-3238698; WNT ligand biogenesis and trafficking.
DR Reactome; R-DME-4086400; PCP/CE pathway.
DR Reactome; R-DME-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR SignaLink; P09615; -.
DR GenomeRNAi; 34009; -.
DR PRO; PR:P09615; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0284084; Expressed in anlage and 84 other tissues.
DR ExpressionAtlas; P09615; baseline and differential.
DR Genevisible; P09615; DM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IDA:FlyBase.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:FlyBase.
DR GO; GO:0005576; C:extracellular region; IDA:FlyBase.
DR GO; GO:0005615; C:extracellular space; IDA:FlyBase.
DR GO; GO:0045121; C:membrane raft; IDA:FlyBase.
DR GO; GO:0005771; C:multivesicular body; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0043195; C:terminal bouton; IDA:FlyBase.
DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR GO; GO:0050840; F:extracellular matrix binding; IDA:FlyBase.
DR GO; GO:0005109; F:frizzled binding; IDA:FlyBase.
DR GO; GO:0005539; F:glycosaminoglycan binding; IDA:FlyBase.
DR GO; GO:0043395; F:heparan sulfate proteoglycan binding; IPI:FlyBase.
DR GO; GO:0016015; F:morphogen activity; IDA:FlyBase.
DR GO; GO:0048018; F:receptor ligand activity; IDA:FlyBase.
DR GO; GO:0007448; P:anterior/posterior pattern specification, imaginal disc; IMP:FlyBase.
DR GO; GO:0035147; P:branch fusion, open tracheal system; IMP:FlyBase.
DR GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IMP:FlyBase.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:FlyBase.
DR GO; GO:0061316; P:canonical Wnt signaling pathway involved in heart development; IMP:FlyBase.
DR GO; GO:0010002; P:cardioblast differentiation; IMP:FlyBase.
DR GO; GO:0090254; P:cell elongation involved in imaginal disc-derived wing morphogenesis; IDA:FlyBase.
DR GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR GO; GO:0035293; P:chitin-based larval cuticle pattern formation; IMP:FlyBase.
DR GO; GO:0001745; P:compound eye morphogenesis; IMP:FlyBase.
DR GO; GO:0035225; P:determination of genital disc primordium; IMP:FlyBase.
DR GO; GO:0048546; P:digestive tract morphogenesis; IMP:FlyBase.
DR GO; GO:0007391; P:dorsal closure; IMP:FlyBase.
DR GO; GO:0007450; P:dorsal/ventral pattern formation, imaginal disc; IMP:FlyBase.
DR GO; GO:0007398; P:ectoderm development; IMP:FlyBase.
DR GO; GO:0008544; P:epidermis development; IMP:FlyBase.
DR GO; GO:0061331; P:epithelial cell proliferation involved in Malpighian tubule morphogenesis; IMP:FlyBase.
DR GO; GO:0035153; P:epithelial cell type specification, open tracheal system; IMP:FlyBase.
DR GO; GO:0035224; P:genital disc anterior/posterior pattern formation; IEP:FlyBase.
DR GO; GO:0035263; P:genital disc sexually dimorphic development; IMP:FlyBase.
DR GO; GO:0060914; P:heart formation; IMP:FlyBase.
DR GO; GO:0007442; P:hindgut morphogenesis; IMP:FlyBase.
DR GO; GO:0007488; P:histoblast morphogenesis; IMP:FlyBase.
DR GO; GO:0007444; P:imaginal disc development; IMP:FlyBase.
DR GO; GO:0008587; P:imaginal disc-derived wing margin morphogenesis; IMP:FlyBase.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0035217; P:labial disc development; IMP:FlyBase.
DR GO; GO:0035167; P:larval lymph gland hemopoiesis; IMP:FlyBase.
DR GO; GO:0007523; P:larval visceral muscle development; IMP:FlyBase.
DR GO; GO:0007616; P:long-term memory; IMP:FlyBase.
DR GO; GO:0035170; P:lymph gland crystal cell differentiation; IMP:FlyBase.
DR GO; GO:0048542; P:lymph gland development; IMP:FlyBase.
DR GO; GO:0061332; P:Malpighian tubule bud morphogenesis; IMP:FlyBase.
DR GO; GO:0061382; P:Malpighian tubule tip cell differentiation; IMP:FlyBase.
DR GO; GO:0007498; P:mesoderm development; IMP:FlyBase.
DR GO; GO:0048332; P:mesoderm morphogenesis; IMP:FlyBase.
DR GO; GO:0009996; P:negative regulation of cell fate specification; IMP:FlyBase.
DR GO; GO:0032876; P:negative regulation of DNA endoreduplication; IMP:FlyBase.
DR GO; GO:0045611; P:negative regulation of hemocyte differentiation; IMP:FlyBase.
DR GO; GO:0014019; P:neuroblast development; IMP:FlyBase.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
DR GO; GO:0061320; P:pericardial nephrocyte differentiation; IMP:FlyBase.
DR GO; GO:0010942; P:positive regulation of cell death; IMP:FlyBase.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:FlyBase.
DR GO; GO:0046672; P:positive regulation of compound eye retinal cell programmed cell death; IMP:FlyBase.
DR GO; GO:0042691; P:positive regulation of crystal cell differentiation; IMP:FlyBase.
DR GO; GO:0045572; P:positive regulation of imaginal disc growth; IMP:FlyBase.
DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IMP:FlyBase.
DR GO; GO:0061328; P:posterior Malpighian tubule development; IMP:FlyBase.
DR GO; GO:0048728; P:proboscis development; IMP:FlyBase.
DR GO; GO:0048076; P:regulation of compound eye pigmentation; IMP:FlyBase.
DR GO; GO:0072091; P:regulation of stem cell proliferation; IMP:FlyBase.
DR GO; GO:0007367; P:segment polarity determination; IMP:FlyBase.
DR GO; GO:0060061; P:Spemann organizer formation; IMP:BHF-UCL.
DR GO; GO:0035277; P:spiracle morphogenesis, open tracheal system; IMP:FlyBase.
DR GO; GO:0050808; P:synapse organization; IMP:FlyBase.
DR GO; GO:0051124; P:synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR GO; GO:0042246; P:tissue regeneration; IMP:FlyBase.
DR GO; GO:0007418; P:ventral midline development; IMP:FlyBase.
DR GO; GO:0035311; P:wing cell fate specification; IMP:FlyBase.
DR GO; GO:0035220; P:wing disc development; IGI:FlyBase.
DR Gene3D; 3.30.2460.20; -; 1.
DR InterPro; IPR005817; Wnt.
DR InterPro; IPR043158; Wnt_C.
DR InterPro; IPR018161; Wnt_CS.
DR PANTHER; PTHR12027; PTHR12027; 1.
DR Pfam; PF00110; wnt; 1.
DR PRINTS; PR01349; WNTPROTEIN.
DR SMART; SM00097; WNT1; 1.
DR PROSITE; PS00246; WNT1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Lipoprotein; Membrane; Morphogen;
KW Reference proteome; Secreted; Segmentation polarity protein; Signal;
KW Synapse; Wnt signaling pathway.
FT SIGNAL 1..17
FT CHAIN 18..468
FT /note="Protein wingless"
FT /id="PRO_0000041476"
FT REGION 83..106
FT /note="Binds porcupine"
FT REGION 333..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 239
FT /note="O-palmitoleoyl serine; by PORCN"
FT /evidence="ECO:0000250|UniProtKB:P56704"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11821428"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11821428"
FT DISULFID 93..104
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 146..154
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 156..185
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 233..247
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 235..242
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 397..428
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 413..423
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 427..467
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 443..458
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 445..455
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 450..451
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT VAR_SEQ 1..53
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_016535"
FT MUTAGEN 51
FT /note="T->A: No effect on glycosylation."
FT /evidence="ECO:0000269|PubMed:11821428"
FT MUTAGEN 93
FT /note="C->Y: In allele wg-S21; results in lethality."
FT /evidence="ECO:0000269|PubMed:7954794"
FT MUTAGEN 104
FT /note="C->S: In allele wg-IL114; temperature sensitive
FT lethal."
FT /evidence="ECO:0000269|PubMed:7954794,
FT ECO:0000269|PubMed:8262072"
FT MUTAGEN 105
FT /note="S->A: Glycosylation disrupted."
FT /evidence="ECO:0000269|PubMed:11821428"
FT MUTAGEN 110
FT /note="S->A: No effect on glycosylation."
FT /evidence="ECO:0000269|PubMed:11821428"
FT MUTAGEN 221
FT /note="G->D: In allele wg-IN67; embryonic lethal."
FT /evidence="ECO:0000269|PubMed:8262072"
FT MUTAGEN 416
FT /note="T->A: Glycosylation disrupted."
FT /evidence="ECO:0000269|PubMed:11821428"
FT CONFLICT 92
FT /note="E -> K (in Ref. 6; AAM75051)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="W -> C (in Ref. 2; AAA28646)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="E -> D (in Ref. 2; AAA28646)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="N -> T (in Ref. 2; AAA28646)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="G -> A (in Ref. 2; AAA28646)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="E -> EE (in Ref. 2; AAA28646)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="K -> N (in Ref. 2; AAA28646)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="E -> D (in Ref. 2; AAA28646)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="E -> D (in Ref. 2; AAA28646)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 468 AA; 51986 MW; F766972A731E6171 CRC64;
MDISYIFVIC LMALCSGGSS LSQVEGKQKS GRGRGSMWWG IAKVGEPNNI TPIMYMDPAI
HSTLRRKQRR LVRDNPGVLG ALVKGANLAI SECQHQFRNR RWNCSTRNFS RGKNLFGKIV
DRGCRETSFI YAITSAAVTH SIARACSEGT IESCTCDYSH QSRSPQANHQ AGSVAGVRDW
EWGGCSDNIG FGFKFSREFV DTGERGRNLR EKMNLHNNEA GRAHVQAEMR QECKCHGMSG
SCTVKTCWMR LANFRVIGDN LKARFDGATR VQVTNSLRAT NALAPVSPNA AGSNSVGSNG
LIIPQSGLVY GEEEERMLND HMPDILLENS HPISKIHHPN MPSPNSLPQA GQRGGRNGRR
QGRKHNRYHF QLNPHNPEHK PPGSKDLVYL EPSPSFCEKN LRQGILGTHG RQCNETSLGV
DGCGLMCCGR GYRRDEVVVV ERCACTFHWC CEVKCKLCRT KKVIYTCL
