VG_DROME
ID VG_DROME Reviewed; 453 AA.
AC Q26366; Q9V6H9;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Protein vestigial;
GN Name=vg; ORFNames=CG3830;
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, AND FUNCTION.
RX PubMed=1752439; DOI=10.1101/gad.5.12b.2481;
RA Williams J.A., Bell J.B., Carroll S.B.;
RT "Control of Drosophila wing and haltere development by the nuclear
RT vestigial gene product.";
RL Genes Dev. 5:2481-2495(1991).
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 FUNCTION, INTERACTION WITH SD, AND TISSUE SPECIFICITY.
RX PubMed=9869635; DOI=10.1101/gad.12.24.3815;
RA Simmonds A.J., Liu X., Soanes K.H., Krause H.M., Irvine K.D., Bell J.B.;
RT "Molecular interactions between Vestigial and Scalloped promote wing
RT formation in Drosophila.";
RL Genes Dev. 12:3815-3820(1998).
RN [5]
RP FUNCTION, INTERACTION WITH SD, AND TISSUE SPECIFICITY.
RX PubMed=9869643; DOI=10.1101/gad.12.24.3900;
RA Halder G., Polaczyk P., Kraus M.E., Hudson A., Kim J., Laughon A.,
RA Carroll S.B.;
RT "The Vestigial and Scalloped proteins act together to directly regulate
RT wing-specific gene expression in Drosophila.";
RL Genes Dev. 12:3900-3909(1998).
RN [6]
RP DNA-BINDING OF VG-SD COMPLEX.
RX PubMed=11546746; DOI=10.1242/dev.128.17.3295;
RA Halder G., Carroll S.B.;
RT "Binding of the vestigial co-factor switches the DNA-target selectivity of
RT the scalloped selector protein.";
RL Development 128:3295-3305(2001).
RN [7]
RP FUNCTION, AND INTERACTION WITH SD AND DHFR.
RX PubMed=14526388; DOI=10.1038/sj.cdd.4401321;
RA Delanoue R., Legent K., Godefroy N., Flagiello D., Dutriaux A., Vaudin P.,
RA Becker J.L., Silber J.;
RT "The Drosophila wing differentiation factor vestigial-scalloped is required
RT for cell proliferation and cell survival at the dorso-ventral boundary of
RT the wing imaginal disc.";
RL Cell Death Differ. 11:110-122(2004).
CC -!- FUNCTION: Involved in determining which thoracic imaginal disk cells
CC will form wings and halteres, perhaps by interacting with other nuclear
CC regulatory proteins. When in combination with scalloped (sd), it acts
CC as a transcriptional activation complex that regulates gene expression
CC in the wing. Binding to sd switches the DNA target selectivity of sd.
CC Required and sufficient for cell proliferation at the dorsal/ventral
CC (D/V) boundary of the wing imaginal disk. Also required for cell
CC proliferation in the wing imaginal disk, mediated via activation of
CC E2f. By interacting with Dhfr, may control genes involved in DNA
CC replication. {ECO:0000269|PubMed:14526388, ECO:0000269|PubMed:1752439,
CC ECO:0000269|PubMed:9869635, ECO:0000269|PubMed:9869643}.
CC -!- SUBUNIT: The Ser-rich protein domain within the C-terminal region
CC interacts with the C-terminus of sd to form a complex which acts as a
CC selector for wing development. Interacts with Dhfr.
CC {ECO:0000269|PubMed:14526388, ECO:0000269|PubMed:9869635,
CC ECO:0000269|PubMed:9869643}.
CC -!- INTERACTION:
CC Q26366; P30052: sd; NbExp=7; IntAct=EBI-162687, EBI-151228;
CC Q26366; P28347: TEAD1; Xeno; NbExp=3; IntAct=EBI-162687, EBI-529156;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Expressed in the developing wing primordia
CC initially along the D/V wing boundary, and by the late third larval
CC instar, maximal expression is seen in cells at the D/V wing disk
CC boundary. Less expression is seen in cells located farther from this
CC boundary. {ECO:0000269|PubMed:9869635, ECO:0000269|PubMed:9869643}.
CC -!- MISCELLANEOUS: Loss of vestigial function selectively eliminates wing
CC and haltere formation.
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DR EMBL; S72379; AAB20671.1; -; Unassigned_DNA.
DR EMBL; AE013599; AAF58444.1; -; Genomic_DNA.
DR PIR; A41640; A41640.
DR RefSeq; NP_523723.1; NM_078999.4.
DR PDB; 6Y20; X-ray; 1.85 A; C/D=298-337.
DR PDBsum; 6Y20; -.
DR AlphaFoldDB; Q26366; -.
DR SMR; Q26366; -.
DR BioGRID; 62192; 33.
DR IntAct; Q26366; 2.
DR STRING; 7227.FBpp0086898; -.
DR PaxDb; Q26366; -.
DR EnsemblMetazoa; FBtr0087785; FBpp0086898; FBgn0003975.
DR GeneID; 36421; -.
DR KEGG; dme:Dmel_CG3830; -.
DR UCSC; CG3830-RA; d. melanogaster.
DR CTD; 36421; -.
DR FlyBase; FBgn0003975; vg.
DR VEuPathDB; VectorBase:FBgn0003975; -.
DR eggNOG; ENOG502QS1A; Eukaryota.
DR GeneTree; ENSGT00530000063353; -.
DR HOGENOM; CLU_661018_0_0_1; -.
DR InParanoid; Q26366; -.
DR OMA; PFYQYER; -.
DR OrthoDB; 1146285at2759; -.
DR PhylomeDB; Q26366; -.
DR SignaLink; Q26366; -.
DR BioGRID-ORCS; 36421; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 36421; -.
DR PRO; PR:Q26366; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0003975; Expressed in spermathecum and 11 other tissues.
DR Genevisible; Q26366; DM.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:FlyBase.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0090254; P:cell elongation involved in imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0001745; P:compound eye morphogenesis; IMP:FlyBase.
DR GO; GO:0016204; P:determination of muscle attachment site; IMP:FlyBase.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0007451; P:dorsal/ventral lineage restriction, imaginal disc; IMP:FlyBase.
DR GO; GO:0007482; P:haltere development; IMP:FlyBase.
DR GO; GO:0007480; P:imaginal disc-derived leg morphogenesis; IMP:FlyBase.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:FlyBase.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007525; P:somatic muscle development; IMP:FlyBase.
DR GO; GO:0035220; P:wing disc development; IMP:FlyBase.
DR GO; GO:0048190; P:wing disc dorsal/ventral pattern formation; IMP:FlyBase.
DR GO; GO:0007472; P:wing disc morphogenesis; IMP:FlyBase.
DR GO; GO:0007473; P:wing disc proximal/distal pattern formation; IMP:FlyBase.
DR InterPro; IPR006627; TDU_repeat.
DR InterPro; IPR011520; Vg_fam.
DR PANTHER; PTHR15950; PTHR15950; 2.
DR Pfam; PF07545; Vg_Tdu; 1.
DR SMART; SM00711; TDU; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Cell cycle; Developmental protein;
KW DNA replication; DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..453
FT /note="Protein vestigial"
FT /id="PRO_0000065807"
FT REGION 145..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..335
FT /note="Ser-rich sd binding domain"
FT COMPBIAS 152..174
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 299..310
FT /evidence="ECO:0007829|PDB:6Y20"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:6Y20"
FT HELIX 331..334
FT /evidence="ECO:0007829|PDB:6Y20"
SQ SEQUENCE 453 AA; 46327 MW; E65D18E6FE4D9B28 CRC64;
MAVSCPEVMY GAYYPYLYGR AGTSRSFYQY ERFNQDLYSS SGVNLAASSS ASGSSHSPCS
PILPPSVSAN AAAAVAAAAH NSAAAAVAVA ANQASSSGGI GGGGLGGLGG LGGGPASGLL
GSNVVPGSSS VGSVGLGMSP VLSGAAGHSL HSSHRTHAHS LAHAHTHPHS HTHTHTHQTK
EEDLIVPRSE AEARLVGSQQ HQHHNESSCS SGPDSPRHAH SHSHPLHGGG GATGGPSSAG
GTGSGGGDGG GTGAIPKNLP ALETPMGSGG GGLAGSGQGQ AQYLSASCVV FTNYSGDTAS
QVDEHFSRAL NYNNKDSKES SSPMSNRNFP PSFWNSNYVH PIPAPTHHQV SDLYGTATDT
GYATDPWVPH AAHYGSYAHA AHAHAAHAHA YHHNMAQYGS LLRLPQQYAS HGSRLHHDQQ
TAHALEYSSY PTMAGLEAQV AQVQESSKDL YWF
