ELG_DROME
ID ELG_DROME Reviewed; 464 AA.
AC Q04688; Q1LZ02; Q8SZC7; Q9VBA4;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=DNA-binding protein Ets97D;
DE Short=D-elg;
GN Name=Ets97D; Synonyms=elg; ORFNames=CG6338;
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 [GENOMIC DNA].
RX PubMed=1461651;
RA The S.M., Xie X., Smyth F., Papas T.S., Watson D.K., Schultz R.A.;
RT "Molecular characterization and structural organization of D-elg, an ets
RT proto-oncogene-related gene of Drosophila.";
RL Oncogene 7:2471-2478(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;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C.,
RA Celniker S.E.;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 298-449, FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S; TISSUE=Larva;
RX PubMed=1577186; DOI=10.1016/0012-1606(92)90225-6;
RA Chen T., Bunting M., Karim F.D., Thummel C.S.;
RT "Isolation and characterization of five Drosophila genes that encode an
RT ets-related DNA binding domain.";
RL Dev. Biol. 151:176-191(1992).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 323-463.
RC STRAIN=Oregon-R; TISSUE=Pupae;
RX PubMed=1713660;
RA Pribyl L.J., Watson D.K., Schulz R.A., Papas T.S.;
RT "D-elg, a member of the Drosophila ets gene family: sequence, expression
RT and evolutionary comparison.";
RL Oncogene 6:1175-1183(1991).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153; THR-157; SER-167 AND
RP SER-171, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: May have a role in germline development.
CC {ECO:0000269|PubMed:1577186}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Uniform distribution throughout embryonic
CC development, with slightly higher expression in pole cells.
CC {ECO:0000269|PubMed:1577186}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development with lower levels
CC during larval development. {ECO:0000269|PubMed:1577186}.
CC -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL48582.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA41390.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; X68259; CAA48327.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF56638.1; -; Genomic_DNA.
DR EMBL; AY070960; AAL48582.1; ALT_FRAME; mRNA.
DR EMBL; BT025224; ABF17915.1; -; mRNA.
DR EMBL; M88471; AAC34199.1; -; mRNA.
DR EMBL; X58481; CAA41390.1; ALT_SEQ; mRNA.
DR PIR; S24300; S24300.
DR PIR; S37616; S37616.
DR RefSeq; NP_524523.2; NM_079799.3.
DR AlphaFoldDB; Q04688; -.
DR SMR; Q04688; -.
DR BioGRID; 68127; 15.
DR IntAct; Q04688; 2.
DR STRING; 7227.FBpp0084458; -.
DR iPTMnet; Q04688; -.
DR PaxDb; Q04688; -.
DR PRIDE; Q04688; -.
DR EnsemblMetazoa; FBtr0085088; FBpp0084458; FBgn0004510.
DR GeneID; 43236; -.
DR KEGG; dme:Dmel_CG6338; -.
DR CTD; 43236; -.
DR FlyBase; FBgn0004510; Ets97D.
DR VEuPathDB; VectorBase:FBgn0004510; -.
DR eggNOG; KOG3806; Eukaryota.
DR GeneTree; ENSGT00940000155799; -.
DR HOGENOM; CLU_037064_1_0_1; -.
DR InParanoid; Q04688; -.
DR OMA; YSFWLQD; -.
DR OrthoDB; 526256at2759; -.
DR PhylomeDB; Q04688; -.
DR Reactome; R-DME-2151201; Transcriptional activation of mitochondrial biogenesis.
DR SignaLink; Q04688; -.
DR BioGRID-ORCS; 43236; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Ets97D; fly.
DR GenomeRNAi; 43236; -.
DR PRO; PR:Q04688; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0004510; Expressed in adult abdomen and 22 other tissues.
DR ExpressionAtlas; Q04688; baseline and differential.
DR Genevisible; Q04688; DM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0009267; P:cellular response to starvation; IMP:FlyBase.
DR GO; GO:1903862; P:positive regulation of oxidative phosphorylation; IMP:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0000820; P:regulation of glutamine family amino acid metabolic process; IMP:FlyBase.
DR GO; GO:0010821; P:regulation of mitochondrion organization; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR InterPro; IPR000418; Ets_dom.
DR InterPro; IPR046328; ETS_fam.
DR InterPro; IPR024668; GABP_asu_N.
DR InterPro; IPR003118; Pointed_dom.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR016312; TF_GA-bd_asu.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11849; PTHR11849; 1.
DR Pfam; PF00178; Ets; 1.
DR Pfam; PF11620; GABP-alpha; 1.
DR Pfam; PF02198; SAM_PNT; 1.
DR PIRSF; PIRSF001703; GABP_alpha; 1.
DR PRINTS; PR00454; ETSDOMAIN.
DR SMART; SM00413; ETS; 1.
DR SMART; SM00251; SAM_PNT; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR PROSITE; PS00345; ETS_DOMAIN_1; 1.
DR PROSITE; PS00346; ETS_DOMAIN_2; 1.
DR PROSITE; PS50061; ETS_DOMAIN_3; 1.
DR PROSITE; PS51433; PNT; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..464
FT /note="DNA-binding protein Ets97D"
FT /id="PRO_0000204094"
FT DOMAIN 184..269
FT /note="PNT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00762"
FT DNA_BIND 346..426
FT /note="ETS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT REGION 138..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 157
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 454
FT /note="V -> L (in Ref. 1; CAA48327 and 5; CAA41390)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 464 AA; 52644 MW; 258A038E8DF427A2 CRC64;
MNSSNDLSDE LIRRLSVGGA LEEVIASEMF EDSIDVETEA EPDDIIIVHM DIREPLSMLK
SLVEQKIGVC LNYYTFWLQD AQELESHKNL VDQCVKGEGL VQINVQIQTI RKRINIADVL
KPTEAALAAL AEEVVGQLSP PETASQKSSS SESPIKTPLK RMHKEDSEEE SVEGKDVKPV
LNWVLDSKFK REQIRLKIPE AANEWTHAHV TYWLEWAVKQ FELVGINMSD WQMNGQELCA
MTHEEFNQKL PRDPGNIFWT HLQLLKECNF VSVVHKRAEE QRKPKQPRIM SANSISTNSG
GSLSLEQRIM RKSYQSVKSS DSVESTTSSM NPSNYTTIGS GNNGQVQLWQ FLLEILTDCE
HTDVIEWVGT EGEFKLTDPD RVARLWGEKK NKPAMNYEKL SRALRYYYDG DMISKVSGKR
FAYKFDCDLK LLIGYDANEL STLVSEGKTA PERVAATETI TEDT
