EAF_DROME
ID EAF_DROME Reviewed; 504 AA.
AC Q7JRJ1; E1JGZ1; Q86PA3;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Ell-associated factor Eaf;
DE Short=dEaf;
GN Name=Eaf; ORFNames=CG11166;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, 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).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18562276; DOI=10.1073/pnas.0804379105;
RA Smith E.R., Winter B., Eissenberg J.C., Shilatifard A.;
RT "Regulation of the transcriptional activity of poised RNA polymerase II by
RT the elongation factor ELL.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:8575-8579(2008).
RN [7]
RP IDENTIFICATION IN THE LEC 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).
CC -!- FUNCTION: Promotes transcriptional elongation by Su(Tpl)/ELL. Essential
CC for development. {ECO:0000269|PubMed:18562276}.
CC -!- SUBUNIT: Component of the little elongation complex, at least composed
CC of Ell, Eaf, Ice1 and Ice2. {ECO:0000269|PubMed:22195968}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A {ECO:0000312|FlyBase:FBgn0033166}; Synonyms=C, D;
CC IsoId=Q7JRJ1-1; Sequence=Displayed;
CC Name=B {ECO:0000312|FlyBase:FBgn0033166};
CC IsoId=Q7JRJ1-2; Sequence=VSP_035952;
CC -!- DISRUPTION PHENOTYPE: Loss of adult progeny and reduced male-female sex
CC ratio. {ECO:0000269|PubMed:18562276}.
CC -!- SIMILARITY: Belongs to the EAF family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE013599; AAF59263.2; -; Genomic_DNA.
DR EMBL; AE013599; AAF59266.2; -; Genomic_DNA.
DR EMBL; AE013599; AAM68888.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68889.1; -; Genomic_DNA.
DR EMBL; BT001503; AAN71258.1; -; mRNA.
DR EMBL; BT001556; AAN71311.1; -; mRNA.
DR EMBL; BT003263; AAO25020.1; -; mRNA.
DR RefSeq; NP_610273.1; NM_136429.4. [Q7JRJ1-1]
DR RefSeq; NP_724547.1; NM_165518.3. [Q7JRJ1-1]
DR RefSeq; NP_724548.1; NM_165519.3. [Q7JRJ1-1]
DR RefSeq; NP_724550.1; NM_165521.3. [Q7JRJ1-2]
DR AlphaFoldDB; Q7JRJ1; -.
DR SMR; Q7JRJ1; -.
DR BioGRID; 61540; 26.
DR IntAct; Q7JRJ1; 14.
DR STRING; 7227.FBpp0088079; -.
DR iPTMnet; Q7JRJ1; -.
DR PaxDb; Q7JRJ1; -.
DR DNASU; 35660; -.
DR EnsemblMetazoa; FBtr0089006; FBpp0088078; FBgn0033166. [Q7JRJ1-1]
DR EnsemblMetazoa; FBtr0089007; FBpp0088079; FBgn0033166. [Q7JRJ1-1]
DR EnsemblMetazoa; FBtr0089008; FBpp0088080; FBgn0033166. [Q7JRJ1-1]
DR EnsemblMetazoa; FBtr0089009; FBpp0088081; FBgn0033166. [Q7JRJ1-2]
DR GeneID; 35660; -.
DR KEGG; dme:Dmel_CG11166; -.
DR UCSC; CG11166-RA; d. melanogaster. [Q7JRJ1-1]
DR UCSC; CG11166-RB; d. melanogaster.
DR CTD; 35660; -.
DR FlyBase; FBgn0033166; Eaf.
DR VEuPathDB; VectorBase:FBgn0033166; -.
DR eggNOG; KOG4795; Eukaryota.
DR GeneTree; ENSGT00390000017724; -.
DR HOGENOM; CLU_025755_2_1_1; -.
DR InParanoid; Q7JRJ1; -.
DR OMA; SIPMIMD; -.
DR PhylomeDB; Q7JRJ1; -.
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-75955; RNA Polymerase II Transcription Elongation.
DR BioGRID-ORCS; 35660; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 35660; -.
DR PRO; PR:Q7JRJ1; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0033166; Expressed in egg cell and 19 other tissues.
DR Genevisible; Q7JRJ1; DM.
DR GO; GO:0005654; C:nucleoplasm; HDA:FlyBase.
DR GO; GO:0032783; C:super elongation complex; IPI:FlyBase.
DR GO; GO:0008023; C:transcription elongation factor complex; IDA:UniProtKB.
DR GO; GO:0003711; F:transcription elongation regulator activity; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0043620; P:regulation of DNA-templated transcription in response to stress; IMP:FlyBase.
DR GO; GO:0034243; P:regulation of transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR GO; GO:0042060; P:wound healing; HMP:FlyBase.
DR InterPro; IPR027093; EAF_fam.
DR InterPro; IPR019194; Tscrpt_elong_fac_Eaf_N.
DR PANTHER; PTHR15970; PTHR15970; 1.
DR Pfam; PF09816; EAF; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Developmental protein; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..504
FT /note="Ell-associated factor Eaf"
FT /id="PRO_0000355634"
FT REGION 174..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1..54
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_035952"
SQ SEQUENCE 504 AA; 54928 MW; 4B40707FED53F15C CRC64;
MMMTKQKNSL AERLNIGEEV RELKLGATFN PKNTSTAFHT IKYDFKPASV DTSRMASVDV
GSNNQVTVTV PNSESSGVPH TVYKGNQREY AKECLMIYDK ETGAITIEKL NHNIQVKKTR
NEVTNKSVQL PGQNMGQPHN QGANGAAPVA VPVPGQGSGT APKMENSTMR ISTKTKVSTG
SRRNNIIDFK PRNSPMQQNS PSRPVPVHRS PQSAPAWDAN NAQQTLPSIP LITDDDDFGL
RAALHNSGHG NTSGTAAGQP DFGSTSSSTH IGKQRQAPPH GHGKRQQMHQ RLSPPMAQQQ
QPSNYGRGYN GGHNHAQQQQ HHQRNSPQQQ RPSAYGHGNS MPIDVDSSRE HELTSQSVAQ
AAAALEQQIG GALSASSSSS ESDSSDSDSG SDSDDSTEDD RSTQGQQQDH QQQQQQQHQV
YQNHKHTQQQ VAQQHHNQLP NLGLGSISPA YGSSHQQQHQ QQMLPHQQKQ KQQSGIYASN
GGFPNDFLQN DLQLSSNSSD DDDD