ELOA1_DROME
ID ELOA1_DROME Reviewed; 643 AA.
AC Q9VCP0; Q86NR0; Q95RH9;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Transcription elongation factor B polypeptide 3;
DE AltName: Full=Elongin-A;
DE AltName: Full=RNA polymerase II transcription factor SIII subunit A;
DE AltName: Full=dEloA;
GN Name=EloA; ORFNames=CG6755;
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] {ECO:0000312|EMBL:AAF56117.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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 [2] {ECO:0000305, ECO:0000312|EMBL:AAF56117.1}
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 [3] {ECO:0000305, ECO:0000312|EMBL:AAL28911.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL28911.1};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
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 [4] {ECO:0000305, ECO:0000312|EMBL:AAO41456.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAO41456.1}; 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 (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=15509793; DOI=10.1128/mcb.24.22.9911-9919.2004;
RA Gerber M., Eissenberg J.C., Kong S., Tenney K., Conaway J.W., Conaway R.C.,
RA Shilatifard A.;
RT "In vivo requirement of the RNA polymerase II elongation factor elongin A
RT for proper gene expression and development.";
RL Mol. Cell. Biol. 24:9911-9919(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, AND IDENTIFICATION BY
RP 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: SIII, also known as elongin, is a general transcription
CC elongation factor that increases the RNA polymerase II transcription
CC elongation past template-encoded arresting sites. Subunit A is
CC transcriptionally active and its transcription activity is strongly
CC enhanced by binding to the dimeric complex of the SIII regulatory
CC subunits B and C (elongin BC complex). May play an important role in
CC metamorphosis. {ECO:0000269|PubMed:15509793}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00649}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A {ECO:0000303|PubMed:10731132};
CC IsoId=Q9VCP0-1; Sequence=Displayed;
CC Name=B {ECO:0000303|PubMed:10731132};
CC IsoId=Q9VCP0-2; Sequence=VSP_050782;
CC -!- DEVELOPMENTAL STAGE: Expression at low levels during embryonic
CC expression and peaks during mid larval stages.
CC {ECO:0000269|PubMed:15509793}.
CC -!- DOMAIN: The elongin BC complex binding domain is also known as BC-box
CC with the consensus [APST]-L-x(3)-C-x(3)-[AILV].
CC {ECO:0000250|UniProtKB:Q63187}.
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DR EMBL; AE014297; AAF56117.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13934.1; -; Genomic_DNA.
DR EMBL; AY061363; AAL28911.1; -; mRNA.
DR EMBL; BT003775; AAO41456.1; -; mRNA.
DR RefSeq; NP_651135.1; NM_142878.4. [Q9VCP0-2]
DR RefSeq; NP_732846.1; NM_170061.3. [Q9VCP0-1]
DR AlphaFoldDB; Q9VCP0; -.
DR SMR; Q9VCP0; -.
DR BioGRID; 67692; 15.
DR IntAct; Q9VCP0; 5.
DR STRING; 7227.FBpp0083766; -.
DR iPTMnet; Q9VCP0; -.
DR PaxDb; Q9VCP0; -.
DR PRIDE; Q9VCP0; -.
DR DNASU; 42749; -.
DR EnsemblMetazoa; FBtr0084374; FBpp0083766; FBgn0039066. [Q9VCP0-1]
DR EnsemblMetazoa; FBtr0084375; FBpp0083767; FBgn0039066. [Q9VCP0-2]
DR GeneID; 42749; -.
DR KEGG; dme:Dmel_CG6755; -.
DR CTD; 6924; -.
DR FlyBase; FBgn0039066; EloA.
DR VEuPathDB; VectorBase:FBgn0039066; -.
DR eggNOG; KOG2821; Eukaryota.
DR GeneTree; ENSGT00390000002428; -.
DR HOGENOM; CLU_021679_1_0_1; -.
DR InParanoid; Q9VCP0; -.
DR OMA; MYIDHYR; -.
DR PhylomeDB; Q9VCP0; -.
DR Reactome; R-DME-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-DME-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-DME-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-DME-75955; RNA Polymerase II Transcription Elongation.
DR BioGRID-ORCS; 42749; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 42749; -.
DR PRO; PR:Q9VCP0; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0039066; Expressed in cleaving embryo and 43 other tissues.
DR ExpressionAtlas; Q9VCP0; baseline and differential.
DR Genevisible; Q9VCP0; DM.
DR GO; GO:0070449; C:elongin complex; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0008023; C:transcription elongation factor complex; ISS:UniProtKB.
DR GO; GO:0007474; P:imaginal disc-derived wing vein specification; IMP:FlyBase.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:FlyBase.
DR Gene3D; 1.20.930.10; -; 1.
DR InterPro; IPR010684; RNA_pol_II_trans_fac_SIII_A.
DR InterPro; IPR003617; TFIIS/CRSP70_N_sub.
DR InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR InterPro; IPR017923; TFIIS_N.
DR Pfam; PF06881; Elongin_A; 1.
DR Pfam; PF08711; Med26; 1.
DR SMART; SM00509; TFS2N; 1.
DR SUPFAM; SSF47676; SSF47676; 1.
DR PROSITE; PS51319; TFIIS_N; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..643
FT /note="Transcription elongation factor B polypeptide 3"
FT /id="PRO_0000086959"
FT DOMAIN 9..82
FT /note="TFIIS N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00649"
FT REGION 86..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..571
FT /note="Activation domain"
FT /evidence="ECO:0000250"
FT REGION 439..448
FT /note="Interacting with Elongin BC complex"
FT /evidence="ECO:0000250"
FT COMPBIAS 96..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1..77
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:10731132,
FT ECO:0000303|PubMed:12537569"
FT /id="VSP_050782"
FT CONFLICT 485
FT /note="N -> D (in Ref. 4; AAO41456)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 643 AA; 71162 MW; 45A28A4BBC5F9B57 CRC64;
MASTSNLLDV VRHYQRSIEK HGEDEQRLLH CITKLFNLPI KFEHLQETGI GKTVNALRKI
SGEVGVAAKT LVTKWKAMVA KEDPSIASTP TAIHNEEDSG KTKSSDEDPD QENKGGNSSS
GEDLNTSKHK SKHAKSTKHE RSSSSRSHSK SRSDSDKKHK SSRHDKSKDR DKDREGQKEA
KEHKEKKSNG EHKSKDSSKS SSSHKSSKSE SHKSEHTKSK HEKDKTSHSE LKEVKDKSSK
HKSSSSKSSK RSHSPPRHEE ESQKAKIPKV KSKSEEDSAD GFDSSMGANF DDVLGLLNIP
ISSKKSSSNS KSKFVAKPTA APSSSALSAP TTAGSSKEAL STSSRPTSKK PELLASTAKL
EPLDPNIALE LPTISNNYKP MPLNQTVMDV VFNQGGSHKA QASRYFNESE ALAQGISSKT
MRTKIYSGVR TGQILQVPSL FDLCTRVLQK NIDALEYTGG VPFEVLRPVL ERATPQQLLN
FEEYNPYLMD DSDVLWQQHV QRHCRSQRRE EMETWREMFL RCQEEKDRKL SILAESIKAS
QKISEAPVRK TQLAFVDSMV KPPRSVQRKQ EQYGTKGKLI ATPAARVAAL SSVTPNAAKV
GDARLRVLAA ARDTAQVGAG PARSKKAPLM AKTLQFMRGR LKR
