E2FE_ARATH
ID E2FE_ARATH Reviewed; 403 AA.
AC Q8LSZ4; Q8RYD8; Q9STS2;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 139.
DE RecName: Full=E2F transcription factor-like E2FE;
DE AltName: Full=DP-E2F-like protein 1;
DE AltName: Full=E2F-like repressor E2L3;
GN Name=E2FE; Synonyms=DEL1, E2L3, ELP2; OrderedLocusNames=At3g48160;
GN ORFNames=T24C20.40;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, DEVELOPMENTAL STAGE, GENE
RP FAMILY, AND NOMENCLATURE.
RX PubMed=11786543; DOI=10.1074/jbc.m110616200;
RA Mariconti L., Pellegrini B., Cantoni R., Stevens R., Bergounioux C.,
RA Cella R., Albani D.;
RT "The E2F family of transcription factors from Arabidopsis thaliana. Novel
RT and conserved components of the retinoblastoma/E2F pathway in plants.";
RL J. Biol. Chem. 277:9911-9919(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=11867638; DOI=10.1074/jbc.m200913200;
RA Kosugi S., Ohashi Y.;
RT "E2Ls, E2F-like repressors of Arabidopsis that bind to E2F sites in a
RT monomeric form.";
RL J. Biol. Chem. 277:16553-16558(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11971144; DOI=10.1105/tpc.010445;
RA Vandepoele K., Raes J., de Veylder L., Rouze P., Rombauts S., Inze D.;
RT "Genome-wide analysis of core cell cycle genes in Arabidopsis.";
RL Plant Cell 14:903-916(2002).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15649366; DOI=10.1016/j.cub.2004.12.038;
RA Vlieghe K., Boudolf V., Beemster G.T., Maes S., Magyar Z., Atanassova A.,
RA de Almeida Engler J., De Groodt R., Inze D., De Veylder L.;
RT "The DP-E2F-like gene DEL1 controls the endocycle in Arabidopsis
RT thaliana.";
RL Curr. Biol. 15:59-63(2005).
RN [8]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=18787127; DOI=10.1073/pnas.0806510105;
RA Lammens T., Boudolf V., Kheibarshekan L., Zalmas L.P., Gaamouche T.,
RA Maes S., Vanstraelen M., Kondorosi E., La Thangue N.B., Govaerts W.,
RA Inze D., De Veylder L.;
RT "Atypical E2F activity restrains APC/CCCS52A2 function obligatory for
RT endocycle onset.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:14721-14726(2008).
CC -!- FUNCTION: Inhibitor of E2F-dependent activation of gene expression.
CC Binds specifically the E2 recognition site without interacting with DP
CC proteins and prevents transcription activation by E2F/DP heterodimers.
CC Controls the timing of endocycle onset and inhibits endoreduplication.
CC {ECO:0000269|PubMed:11786543, ECO:0000269|PubMed:11867638,
CC ECO:0000269|PubMed:15649366, ECO:0000269|PubMed:18787127}.
CC -!- INTERACTION:
CC Q8LSZ4; Q8VZI9: At3g11100; NbExp=3; IntAct=EBI-2651542, EBI-1998580;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11867638}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Named isoforms=2.;
CC Name=1;
CC IsoId=Q8LSZ4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8LSZ4-2; Sequence=VSP_040805, VSP_040806;
CC -!- TISSUE SPECIFICITY: Expressed exclusively in mitotically dividing
CC cells. Highly expressed in young leaves and mature flowers. Lower
CC expression in young stalk and in young and mature flowers.
CC {ECO:0000269|PubMed:11867638, ECO:0000269|PubMed:15649366}.
CC -!- DEVELOPMENTAL STAGE: Expressed in a cell cycle-dependent manner. Not
CC detected during early S phase. Expressed at both the G1/S and S/G2
CC transitions, with a peak during G2. {ECO:0000269|PubMed:11786543,
CC ECO:0000269|PubMed:18787127}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, but increased ploidy
CC levels. {ECO:0000269|PubMed:15649366}.
CC -!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB51063.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB074533; BAB91414.1; -; mRNA.
DR EMBL; AJ417836; CAD10633.1; -; mRNA.
DR EMBL; AL096856; CAB51063.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002686; AEE78374.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78375.1; -; Genomic_DNA.
DR EMBL; BT004258; AAO42262.1; -; mRNA.
DR EMBL; BT005524; AAO63944.1; -; mRNA.
DR PIR; T13005; T13005.
DR RefSeq; NP_190399.2; NM_114685.4. [Q8LSZ4-1]
DR RefSeq; NP_851012.1; NM_180681.1. [Q8LSZ4-2]
DR AlphaFoldDB; Q8LSZ4; -.
DR SMR; Q8LSZ4; -.
DR BioGRID; 9290; 15.
DR IntAct; Q8LSZ4; 13.
DR STRING; 3702.AT3G48160.2; -.
DR PaxDb; Q8LSZ4; -.
DR PRIDE; Q8LSZ4; -.
DR ProteomicsDB; 222010; -. [Q8LSZ4-1]
DR EnsemblPlants; AT3G48160.1; AT3G48160.1; AT3G48160. [Q8LSZ4-2]
DR EnsemblPlants; AT3G48160.2; AT3G48160.2; AT3G48160. [Q8LSZ4-1]
DR GeneID; 823971; -.
DR Gramene; AT3G48160.1; AT3G48160.1; AT3G48160. [Q8LSZ4-2]
DR Gramene; AT3G48160.2; AT3G48160.2; AT3G48160. [Q8LSZ4-1]
DR KEGG; ath:AT3G48160; -.
DR Araport; AT3G48160; -.
DR TAIR; locus:2100444; AT3G48160.
DR eggNOG; KOG2578; Eukaryota.
DR HOGENOM; CLU_041969_1_0_1; -.
DR InParanoid; Q8LSZ4; -.
DR OMA; RSKTHES; -.
DR OrthoDB; 706632at2759; -.
DR PhylomeDB; Q8LSZ4; -.
DR PRO; PR:Q8LSZ4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8LSZ4; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0042023; P:DNA endoreduplication; IMP:TAIR.
DR GO; GO:0032876; P:negative regulation of DNA endoreduplication; IGI:TAIR.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 2.
DR InterPro; IPR015633; E2F.
DR InterPro; IPR003316; E2F_WHTH_DNA-bd_dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR12081; PTHR12081; 1.
DR Pfam; PF02319; E2F_TDP; 2.
DR SMART; SM01372; E2F_TDP; 2.
DR SUPFAM; SSF46785; SSF46785; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; DNA-binding; Nucleus; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..403
FT /note="E2F transcription factor-like E2FE"
FT /id="PRO_0000406293"
FT DNA_BIND 34..99
FT DNA_BIND 169..250
FT REGION 128..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 371..379
FT /note="VLKDLFSHY -> GAYILFTSI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11786543"
FT /id="VSP_040805"
FT VAR_SEQ 380..403
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11786543"
FT /id="VSP_040806"
SQ SEQUENCE 403 AA; 45461 MW; 0C9E724B5AF7BC94 CRC64;
MSDLSPERFK LAVTSPSSIP ESSSALQLHH SYSRKQKSLG LLCTNFLALY NREGIEMVGL
DDAASKLGVE RRRIYDIVNV LESVGVLTRR AKNQYTWKGF SAIPGALKEL QEEGVKDTFH
RFYVNENVKG SDDEDDDEES SQPHSSSQTD SSKPGSLPQS SDPSKIDNRR EKSLGLLTQN
FIKLFICSEA IRIISLDDAA KLLLGDAHNT SIMRTKVRRL YDIANVLSSM NLIEKTHTLD
SRKPAFKWLG YNGEPTFTLS SDLLQLESRK RAFGTDITNV NVKRSKSSSS SQENATERRL
KMKKHSTPES SYNKSFDVHE SRHGSRGGYH FGPFAPGTGT YPTAGLEDNS RRAFDVENLD
SDYRPSYQNQ VLKDLFSHYM DAWKTWFSEV TQENPLPNTS QHR
