ELL_DROME
ID ELL_DROME Reviewed; 1059 AA.
AC Q9VW51; Q95VE6;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 3.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=RNA polymerase II elongation factor Ell;
DE Short=dELL;
GN Name=Ell; Synonyms=Su(Tpl); ORFNames=CG32217;
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], FUNCTION, ASSOCIATION WITH RNA POLYMERASE II,
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=11689450; DOI=10.1093/emboj/20.21.6104;
RA Gerber M., Ma J., Dean K., Eissenberg J.C., Shilatifard A.;
RT "Drosophila ELL is associated with actively elongating RNA polymerase II on
RT transcriptionally active sites in vivo.";
RL EMBO J. 20:6104-6114(2001).
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 FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE LEC COMPLEX, AND
RP IDENTIFICATION IN THE SEC COMPLEX.
RX PubMed=22195968; DOI=10.1016/j.molcel.2011.12.008;
RA Smith E.R., Lin C., Garrett A.S., Thornton J., Mohaghegh N., Hu D.,
RA Jackson J., Saraf A., Swanson S.K., Seidel C., Florens L., Washburn M.P.,
RA Eissenberg J.C., Shilatifard A.;
RT "The little elongation complex regulates small nuclear RNA transcription.";
RL Mol. Cell 44:954-965(2011).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=23932780; DOI=10.1016/j.molcel.2013.07.003;
RA Hu D., Smith E.R., Garruss A.S., Mohaghegh N., Varberg J.M., Lin C.,
RA Jackson J., Gao X., Saraf A., Florens L., Washburn M.P., Eissenberg J.C.,
RA Shilatifard A.;
RT "The little elongation complex functions at initiation and elongation
RT phases of snRNA gene transcription.";
RL Mol. Cell 51:493-505(2013).
CC -!- FUNCTION: Elongation factor component of the super elongation complex
CC (SEC), a complex required to increase the catalytic rate of RNA
CC polymerase II transcription by suppressing transient pausing by the
CC polymerase at multiple sites along the DNA (PubMed:11689450).
CC Elongation factor component of the little elongation complex (LEC), a
CC complex required to regulate small nuclear RNA (snRNA) gene
CC transcription by RNA polymerase II and III (PubMed:22195968,
CC PubMed:23932780). {ECO:0000269|PubMed:11689450,
CC ECO:0000269|PubMed:22195968, ECO:0000269|PubMed:23932780}.
CC -!- SUBUNIT: Component of the super elongation complex (SEC), at least
CC composed of Ell, Cdk9, cyclin-T (CycT), lilli and ear. Component of the
CC little elongation complex, at least composed of Ell, Eaf, Ice1 and
CC Ice2. Associates with RNA polymerase II. {ECO:0000269|PubMed:22195968}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11689450,
CC ECO:0000269|PubMed:22195968}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:11689450}. Chromosome {ECO:0000269|PubMed:11689450,
CC ECO:0000269|PubMed:23932780}. Note=Localizes with RNA polymerase II at
CC many transcriptionally active sites along polytene euchromatic
CC chromosome arms and at developmental puff sites. Upon heat shock,
CC relocalizes together with RNA polymerase II to selected heat shock
CC puffs (PubMed:11689450). Associates to transcriptionally active
CC chromatin at snRNA genes (PubMed:22195968).
CC {ECO:0000269|PubMed:11689450, ECO:0000269|PubMed:22195968}.
CC -!- DEVELOPMENTAL STAGE: Expressed in salivary glands (at protein level).
CC {ECO:0000269|PubMed:11689450}.
CC -!- SIMILARITY: Belongs to the ELL/occludin family. {ECO:0000305}.
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DR EMBL; AF416770; AAL13036.1; -; mRNA.
DR EMBL; AE014296; AAF49098.3; -; Genomic_DNA.
DR EMBL; AE014296; ACZ94748.1; -; Genomic_DNA.
DR EMBL; AE014296; AHN58147.1; -; Genomic_DNA.
DR EMBL; BT050407; ACI88733.1; -; mRNA.
DR EMBL; BT058015; ACM16731.1; -; mRNA.
DR RefSeq; NP_001163477.1; NM_001170006.2.
DR RefSeq; NP_001287122.1; NM_001300193.1.
DR RefSeq; NP_649155.3; NM_140898.5.
DR AlphaFoldDB; Q9VW51; -.
DR SMR; Q9VW51; -.
DR BioGRID; 65439; 17.
DR IntAct; Q9VW51; 2.
DR STRING; 7227.FBpp0291257; -.
DR PaxDb; Q9VW51; -.
DR DNASU; 40171; -.
DR EnsemblMetazoa; FBtr0074920; FBpp0074689; FBgn0014037.
DR EnsemblMetazoa; FBtr0302047; FBpp0291257; FBgn0014037.
DR EnsemblMetazoa; FBtr0344257; FBpp0310656; FBgn0014037.
DR GeneID; 40171; -.
DR KEGG; dme:Dmel_CG32217; -.
DR UCSC; CG32217-RA; d. melanogaster.
DR CTD; 40171; -.
DR FlyBase; FBgn0014037; Su(Tpl).
DR VEuPathDB; VectorBase:FBgn0014037; -.
DR eggNOG; KOG4796; Eukaryota.
DR GeneTree; ENSGT00940000170989; -.
DR HOGENOM; CLU_009447_0_0_1; -.
DR InParanoid; Q9VW51; -.
DR OMA; SHRYTDD; -.
DR OrthoDB; 335949at2759; -.
DR PhylomeDB; Q9VW51; -.
DR Reactome; R-DME-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-DME-351906; Apoptotic cleavage of cell adhesion proteins.
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-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-DME-75955; RNA Polymerase II Transcription Elongation.
DR SignaLink; Q9VW51; -.
DR BioGRID-ORCS; 40171; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 40171; -.
DR PRO; PR:Q9VW51; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0014037; Expressed in egg cell and 21 other tissues.
DR ExpressionAtlas; Q9VW51; baseline and differential.
DR Genevisible; Q9VW51; DM.
DR GO; GO:0000791; C:euchromatin; IMP:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0005703; C:polytene chromosome puff; IDA:UniProtKB.
DR GO; GO:0008023; C:transcription elongation factor complex; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0070063; F:RNA polymerase binding; IDA:UniProtKB.
DR GO; GO:0097150; P:neuronal stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IDA:UniProtKB.
DR GO; GO:0043620; P:regulation of DNA-templated transcription in response to stress; IMP:FlyBase.
DR GO; GO:0042795; P:snRNA transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IEA:InterPro.
DR GO; GO:0048190; P:wing disc dorsal/ventral pattern formation; IGI:FlyBase.
DR Gene3D; 1.10.10.2670; -; 1.
DR InterPro; IPR042065; E3_ELL-like.
DR InterPro; IPR031176; ELL/occludin.
DR InterPro; IPR019464; ELL_N.
DR InterPro; IPR010844; Occludin_ELL.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR23288; PTHR23288; 2.
DR Pfam; PF10390; ELL; 1.
DR Pfam; PF07303; Occludin_ELL; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS51980; OCEL; 1.
PE 1: Evidence at protein level;
KW Chromosome; Coiled coil; Nucleus; Photosynthesis; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..1059
FT /note="RNA polymerase II elongation factor Ell"
FT /id="PRO_0000430426"
FT DOMAIN 827..939
FT /note="OCEL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01324"
FT REGION 171..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 968..1059
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 853..883
FT /evidence="ECO:0000255"
FT COMPBIAS 188..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..680
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..803
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1001..1029
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1051
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 229
FT /note="R -> S (in Ref. 1; AAL13036)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="V -> G (in Ref. 1; AAL13036)"
FT /evidence="ECO:0000305"
FT CONFLICT 501
FT /note="S -> G (in Ref. 1; AAL13036)"
FT /evidence="ECO:0000305"
FT CONFLICT 783
FT /note="S -> SQ (in Ref. 1; AAL13036)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1059 AA; 114915 MW; 07863C7ABEA17911 CRC64;
MTNSIASTKC LPNALSTGNY GMSQSHRYTD DSKEYIIVKL TDSAFRAIEE YQRDDNAKRL
QPGQRAKIQF VGNTGVIQFP RPATDANGIP NANGNGSDAT GAGGGGGRKF GFTINNMEGT
LECVQQQQRS LGVLGAVTLR MRIHANEDVY DSTRTKMAIA EETEKSKCIR EIKPNQSDIG
RKVKKPPSAI QSSASTASAF SSNSSNSGLT TTAFHHHSNS NNSGNNNNRS SSSSNSFNSN
NHSRKLGSSP FNGLGVGSSS SSSAFASRSP NPSTLGAIGT VNGSGVVGGR YGGGAASSLA
STFANGISQG YHNLSGSSPR DSMTAGTSSA TASSVISSRN KMPSGGLTSS NSNSSSSSRS
ANSKSSGGNK MSDVSRRNIR ERLIHLLALK AFKKPELFAR LKNEGIRDRE RNQITNILMD
ISTMSHNTYN LRRQMWNDVD ENWPFFSEQE VQQLKRRKPQ NLTPPMSSDA GSSTSGQSPT
STHTGSPPPP SSNGGPGGVG SGAGGTSMKR TSLEYDETMF STVQPKKQRI SHYKKDTPPS
GTSYSSAGVS MSLGSSGSSS RSRYTPPQRQ PGPLDDHSTT DLSYNVLDNI VEFMSSTAAA
TQQSMEQQQH PRSNSSNNRR GSSSLAGTSN GGNNKDKRNS TGSNSSSSSG YETQQDRQRS
TTPMSSNRSS ASSSTTPPKL AASFVPAATS GSASGTSKQR MPPQQSDYNS YNSNNAQHVA
SNSKKRMGSV GPSGGSNGQR QRSASGSNSG YQQVPPPSSN SRSSIQQQNQ HQKQQVQQKQ
APSQQQQQQQ QQYHQQAKHP SPSQQLAAAA HAYAHATADT DSSATPRYDF SQYVPIQTLE
VRRRYKTEFE SDYDEYRKLL TRVEDVRNRF QDLSERLESA RRCDNGYGDY DHIKRQIVCE
YERINNDRTI GEDKERFDYL HAKLAHIKQL VMDYDKTLMS ATMAMAPTDV VAAQGPDPAV
AKAAARLAEH HRRQHHAAET IKQQQQQKQT HQHHLQRHLQ HHLQQQQNLL QQQQNLLQQQ
SVSNSDDSSD SSDSNDDDDD DDEDCDDSNS NTDDDEARY
