WNT2_DROME
ID WNT2_DROME Reviewed; 352 AA.
AC P28465; Q86PC8; Q9V584;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Protein Wnt-2;
DE AltName: Full=dWnt-2;
DE Flags: Precursor;
GN Name=Wnt2; Synonyms=Wnt-2; ORFNames=CG1916;
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], AND TISSUE SPECIFICITY.
RC STRAIN=Canton-S; TISSUE=Embryo;
RX PubMed=1425336; DOI=10.1242/dev.115.2.475;
RA Russell J., Gennissen A., Nusse R.;
RT "Isolation and expression of two novel Wnt/wingless gene homologues in
RT Drosophila.";
RL Development 115:475-485(1992).
RN [2]
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 [3]
RP GENOME REANNOTATION.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
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).
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 function in gonadogenesis and limb development.
CC Wg and Wnt2 have a role in the developing trachea and together are
CC responsible for all dorsal trunk formation.
CC {ECO:0000269|PubMed:11717401}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- TISSUE SPECIFICITY: Dynamic expression pattern during embryogenesis.
CC Expression is predominantly segmented, with expression also seen in the
CC limb primordia and presumptive gonads. In embryonic tracheal cells,
CC expression is close to and dorsal to the tracheal placode.
CC {ECO:0000269|PubMed:11717401, ECO:0000269|PubMed:1425336}.
CC -!- PTM: Palmitoleoylated by porcupine. The lipid group functions as a
CC sorting signal, targeting the ligand to polarized vesicles that
CC transport Wnt2 to unique sites at the cell surface. Depalmitoleoylated
CC by notum, leading to inhibit Wnt signaling pathway.
CC {ECO:0000250|UniProtKB:P09615}.
CC -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000305}.
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DR EMBL; X64735; CAA46001.1; -; mRNA.
DR EMBL; AE013599; AAF58933.1; -; Genomic_DNA.
DR EMBL; BT003204; AAO24959.1; -; mRNA.
DR PIR; S24559; S24559.
DR RefSeq; NP_476810.1; NM_057462.5.
DR AlphaFoldDB; P28465; -.
DR SMR; P28465; -.
DR BioGRID; 61806; 10.
DR IntAct; P28465; 2.
DR STRING; 7227.FBpp0087596; -.
DR GlyGen; P28465; 2 sites.
DR PaxDb; P28465; -.
DR EnsemblMetazoa; FBtr0088512; FBpp0087596; FBgn0004360.
DR GeneID; 35975; -.
DR KEGG; dme:Dmel_CG1916; -.
DR CTD; 7472; -.
DR FlyBase; FBgn0004360; Wnt2.
DR VEuPathDB; VectorBase:FBgn0004360; -.
DR eggNOG; KOG3913; Eukaryota.
DR GeneTree; ENSGT00940000167538; -.
DR InParanoid; P28465; -.
DR OrthoDB; 745245at2759; -.
DR PhylomeDB; P28465; -.
DR Reactome; R-DME-3238698; WNT ligand biogenesis and trafficking.
DR SignaLink; P28465; -.
DR BioGRID-ORCS; 35975; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 35975; -.
DR PRO; PR:P28465; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0004360; Expressed in seminal fluid secreting gland and 5 other tissues.
DR ExpressionAtlas; P28465; baseline and differential.
DR Genevisible; P28465; DM.
DR GO; GO:0005576; C:extracellular region; ISS:FlyBase.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR GO; GO:0005109; F:frizzled binding; IPI:FlyBase.
DR GO; GO:0005102; F:signaling receptor binding; ISS:FlyBase.
DR GO; GO:0048675; P:axon extension; IMP:FlyBase.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IMP:FlyBase.
DR GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR GO; GO:0060250; P:germ-line stem-cell niche homeostasis; IMP:FlyBase.
DR GO; GO:0007517; P:muscle organ development; IMP:FlyBase.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0007424; P:open tracheal system development; IGI:FlyBase.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IBA:GO_Central.
DR GO; GO:0007367; P:segment polarity determination; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Developmental protein; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Lipoprotein; Reference proteome; Secreted; Segmentation polarity protein;
KW Signal; Wnt signaling pathway.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..352
FT /note="Protein Wnt-2"
FT /id="PRO_0000041477"
FT LIPID 202
FT /note="O-palmitoleoyl serine; by PORCN"
FT /evidence="ECO:0000250|UniProtKB:P56704"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 65..76
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 115..123
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 125..148
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 196..210
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 198..205
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 281..312
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 297..307
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 311..351
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 327..342
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 329..339
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 334..335
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT CONFLICT 27
FT /note="V -> A (in Ref. 1; CAA46001)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="Q -> L (in Ref. 4; AAO24959)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="A -> R (in Ref. 1; CAA46001)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="L -> M (in Ref. 1; CAA46001)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 352 AA; 39763 MW; C021663DB4CAC5DF CRC64;
MWKIHNKLLI YILWIMEIRL VSSFTSVMLC GRIPGLTPGQ RNMCREMPDA LIALGEGHQL
GAQECQHQFR GHRWNCSEVW QRNVFAHVIP TASREAAYTY AIASAGAAYA VTAACARGNI
STCGCDVRHK ATPTGGGTPD EPWKWGGCSA DVDFGMRYAR RFMDARELER DSRTLMNLHN
NRAGRTLVKK MLRTDCKCHG VSGSCVMKTC WKSLPPFRLV GDRLMLKYQK AKTVQAVKGK
RGLRLVLSRK KHAGTARAQK PVLDWPKRME LIYLEASPNY CERSLQTGSQ GTSGRTCQRT
GHGPQSCDLL CCGRGHNTQH IRRTTQCRCQ FRWCCEVKCD ECDESYEEFT CK
