E2FA_ARATH
ID E2FA_ARATH Reviewed; 485 AA.
AC Q9FNY0; Q9C5B5; Q9FV69; Q9M454; Q9SJ49;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Transcription factor E2FA;
DE AltName: Full=E2F transcription factor-3;
DE Short=AtE2F3;
GN Name=E2FA; Synonyms=E2F3, E2F4; OrderedLocusNames=At2g36010;
GN ORFNames=F11F19.8;
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 1), INTERACTION WITH DPA AND DPB,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11108847; DOI=10.1016/s0014-5793(00)02238-9;
RA Magyar Z., Atanassova A., De Veylder L., Rombauts S., Inze D.;
RT "Characterization of two distinct DP-related genes from Arabidopsis
RT thaliana.";
RL FEBS Lett. 486:79-87(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH MAIZE
RP RBR1, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=11669580; DOI=10.1023/a:1011848528377;
RA de Jager S.M., Menges M., Bauer U.M., Murra J.A.;
RT "Arabidopsis E2F1 binds a sequence present in the promoter of S-phase-
RT regulated gene AtCDC6 and is a member of a multigene family with
RT differential activities.";
RL Plant Mol. Biol. 47:555-568(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH DPA AND
RP DPB, DEVELOPMENTAL STAGE, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Labra M., Ghiani A., Citterio S., Sgorbati S.;
RT "Isolation and characterization of E2F-like protein in Arabidopsis
RT thaliana.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF Clones.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11889041; DOI=10.1093/emboj/21.6.1360;
RA De Veylder L., Beeckman T., Beemster G.T., de Almeida Engler J.,
RA Ormenese S., Maes S., Naudts M., Van Der Schueren E., Jacqmard A.,
RA Engler G., Inze D.;
RT "Control of proliferation, endoreduplication and differentiation by the
RT Arabidopsis E2Fa-DPa transcription factor.";
RL EMBO J. 21:1360-1368(2002).
RN [9]
RP INTERACTION WITH DPA; DPB AND E2FD.
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 [10]
RP FUNCTION.
RX PubMed=11862494; DOI=10.1007/s00438-001-0624-7;
RA Rossignol P., Stevens R., Perennes C., Jasinski S., Cella R.,
RA Tremousaygue D., Bergounioux C.;
RT "AtE2F-a and AtDP-a, members of the E2F family of transcription factors,
RT induce Arabidopsis leaf cells to re-enter S phase.";
RL Mol. Genet. Genomics 266:995-1003(2002).
RN [11]
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 [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DPA AND DPB.
RC STRAIN=cv. Columbia;
RX PubMed=11891240; DOI=10.1104/pp.010642;
RA Kosugi S., Ohashi Y.;
RT "Interaction of the Arabidopsis E2F and DP proteins confers their
RT concomitant nuclear translocation and transactivation.";
RL Plant Physiol. 128:833-843(2002).
RN [13]
RP FUNCTION.
RX PubMed=12913157; DOI=10.1104/pp.103.025080;
RA Kosugi S., Ohashi Y.;
RT "Constitutive E2F expression in tobacco plants exhibits altered cell cycle
RT control and morphological change in a cell type-specific manner.";
RL Plant Physiol. 132:2012-2022(2003).
RN [14]
RP FUNCTION.
RX PubMed=15377755; DOI=10.1105/tpc.104.024398;
RA Boudolf V., Vlieghe K., Beemster G.T.S., Magyar Z., Torres Acosta J.A.,
RA Maes S., Van Der Schueren E., Inze D., De Veylder L.;
RT "The plant-specific cyclin-dependent kinase CDKB1;1 and transcription
RT factor E2Fa-DPa control the balance of mitotically dividing and
RT endoreduplicating cells in Arabidopsis.";
RL Plant Cell 16:2683-2692(2004).
RN [15]
RP FUNCTION.
RX PubMed=16514015; DOI=10.1104/pp.106.077990;
RA Sozzani R., Maggio C., Varotto S., Canova S., Bergounioux C., Albani D.,
RA Cella R.;
RT "Interplay between Arabidopsis activating factors E2Fb and E2Fa in cell
RT cycle progression and development.";
RL Plant Physiol. 140:1355-1366(2006).
RN [16]
RP FUNCTION.
RX PubMed=19662336; DOI=10.1007/s11103-009-9527-5;
RA de Jager S.M., Scofield S., Huntley R.P., Robinson A.S., den Boer B.G.,
RA Murray J.A.;
RT "Dissecting regulatory pathways of G1/S control in Arabidopsis: common and
RT distinct targets of CYCD3;1, E2Fa and E2Fc.";
RL Plant Mol. Biol. 71:345-365(2009).
CC -!- FUNCTION: Transcription activator that binds DNA cooperatively with DP
CC proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in
CC the promoter region of a number of genes whose products are involved in
CC cell cycle regulation or in DNA replication. The binding of
CC retinoblastoma-related proteins represses transactivation. Regulates
CC gene expression both positively and negatively. Activates the
CC expression of E2FB. Involved in the control of cell-cycle progression
CC from G1 to S phase. Stimulates cell proliferation and delays
CC differentiation. {ECO:0000269|PubMed:11669580,
CC ECO:0000269|PubMed:11786543, ECO:0000269|PubMed:11862494,
CC ECO:0000269|PubMed:11889041, ECO:0000269|PubMed:11891240,
CC ECO:0000269|PubMed:12913157, ECO:0000269|PubMed:15377755,
CC ECO:0000269|PubMed:16514015, ECO:0000269|PubMed:19662336}.
CC -!- SUBUNIT: Heterodimer with DP proteins. Interacts (via dimerization
CC domain) preferentially with DPA, but also with DPB. Interacts with
CC maize retinoblastoma-related protein RBR1. No interaction with E2FD.
CC {ECO:0000269|PubMed:11108847, ECO:0000269|PubMed:11669580,
CC ECO:0000269|PubMed:11786543, ECO:0000269|PubMed:11867638,
CC ECO:0000269|PubMed:11891240}.
CC -!- INTERACTION:
CC Q9FNY0; Q9FNY3: DPA; NbExp=6; IntAct=EBI-1774747, EBI-1774763;
CC Q9FNY0; Q9FNY2: DPB; NbExp=5; IntAct=EBI-1774747, EBI-1774876;
CC Q9FNY0; Q9LKZ3: RBR1; NbExp=4; IntAct=EBI-1774747, EBI-398590;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11891240}. Nucleus
CC {ECO:0000269|PubMed:11891240}. Note=Interaction with DPA induces an
CC exclusive nuclear localization, but an interaction with DPB has no
CC effect.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9FNY0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FNY0-2; Sequence=VSP_040803;
CC Name=3;
CC IsoId=Q9FNY0-3; Sequence=VSP_040801, VSP_040802;
CC -!- TISSUE SPECIFICITY: Highly expressed in the shoot apical meristem,
CC emerging leaf primordia, and vascular tissues of young leaf primordia.
CC Expressed in flowers, in epidermis and cortex of hypocotyls, and at
CC lower levels in leaves. {ECO:0000269|PubMed:11108847,
CC ECO:0000269|PubMed:11889041}.
CC -!- DEVELOPMENTAL STAGE: Expressed in a cell cycle-dependent manner. Most
CC abundant in early S phase. Decreased expression during the passage into
CC G2. {ECO:0000269|PubMed:11108847, ECO:0000269|PubMed:11669580,
CC ECO:0000269|PubMed:11786543}.
CC -!- DOMAIN: The C-terminal region (366-485) is required for
CC transactivational activity. The N-terminal region (92-128) is important
CC for nuclear localization.
CC -!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}.
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DR EMBL; AJ294534; CAC15486.1; -; mRNA.
DR EMBL; AF242582; AAG17610.1; -; mRNA.
DR EMBL; AJ276619; CAC34724.1; -; mRNA.
DR EMBL; AJ271597; CAB70599.1; -; mRNA.
DR EMBL; AC007017; AAD21456.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC09191.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09192.1; -; Genomic_DNA.
DR EMBL; BT026376; ABH04483.1; -; mRNA.
DR PIR; G84775; G84775.
DR RefSeq; NP_565831.3; NM_129160.4. [Q9FNY0-2]
DR RefSeq; NP_973610.1; NM_201881.2.
DR RefSeq; NP_973611.1; NM_201882.3. [Q9FNY0-1]
DR AlphaFoldDB; Q9FNY0; -.
DR SMR; Q9FNY0; -.
DR BioGRID; 3518; 17.
DR DIP; DIP-40175N; -.
DR IntAct; Q9FNY0; 11.
DR PRIDE; Q9FNY0; -.
DR ProteomicsDB; 222032; -. [Q9FNY0-1]
DR EnsemblPlants; AT2G36010.1; AT2G36010.1; AT2G36010. [Q9FNY0-2]
DR EnsemblPlants; AT2G36010.3; AT2G36010.3; AT2G36010. [Q9FNY0-1]
DR GeneID; 818174; -.
DR Gramene; AT2G36010.1; AT2G36010.1; AT2G36010. [Q9FNY0-2]
DR Gramene; AT2G36010.3; AT2G36010.3; AT2G36010. [Q9FNY0-1]
DR KEGG; ath:AT2G36010; -.
DR Araport; AT2G36010; -.
DR HOGENOM; CLU_032091_3_2_1; -.
DR InParanoid; Q9FNY0; -.
DR OMA; PDEGVGH; -.
DR OrthoDB; 1087250at2759; -.
DR PhylomeDB; Q9FNY0; -.
DR PRO; PR:Q9FNY0; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9FNY0; baseline and differential.
DR Genevisible; Q9FNY0; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051446; P:positive regulation of meiotic cell cycle; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd14660; E2F_DD; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR015633; E2F.
DR InterPro; IPR037241; E2F-DP_heterodim.
DR InterPro; IPR032198; E2F_CC-MB.
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; PF16421; E2F_CC-MB; 1.
DR Pfam; PF02319; E2F_TDP; 1.
DR SMART; SM01372; E2F_TDP; 1.
DR SUPFAM; SSF144074; SSF144074; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Cell cycle; Coiled coil; Cytoplasm;
KW DNA-binding; Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..485
FT /note="Transcription factor E2FA"
FT /id="PRO_0000406289"
FT DNA_BIND 167..232
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..277
FT /note="Leucine-zipper"
FT REGION 435..450
FT /note="Retinoblastoma protein binding"
FT /evidence="ECO:0000255"
FT COILED 245..286
FT /evidence="ECO:0000255"
FT COMPBIAS 10..33
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 92
FT /note="P -> PIFPSEIGLEIRGCFGDFDCYLLLLSLIQKLRSVRLSSIRVNFCRLF
FT SFAM (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_040801"
FT VAR_SEQ 155..173
FT /note="GSPITLTPSGSCRYDSSLG -> VRSFYEISFMSRVTS (in isoform
FT 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_040802"
FT VAR_SEQ 247..248
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_040803"
FT CONFLICT 264
FT /note="D -> G (in Ref. 1; CAC15486)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 485 AA; 52839 MW; 838A5AD7A31B035C CRC64;
MSGVVRSSPG SSQPPPPPPH HPPSSPVPVT STPVIPPIRR HLAFASTKPP FHPSDDYHRF
NPSSLSNNND RSFVHGCGVV DREEDAVVVR SPSRKRKATM DMVVAPSNNG FTSSGFTNIP
SSPCQTPRKG GRVNIKSKAK GNKSTPQTPI STNAGSPITL TPSGSCRYDS SLGLLTKKFV
NLIKQAKDGM LDLNKAAETL EVQKRRIYDI TNVLEGIDLI EKPFKNRILW KGVDACPGDE
DADVSVLQLQ AEIENLALEE QALDNQIRQT EERLRDLSEN EKNQKWLFVT EEDIKSLPGF
QNQTLIAVKA PHGTTLEVPD PDEAADHPQR RYRIILRSTM GPIDVYLVSE FEGKFEDTNG
SGAAPPACLP IASSSGSTGH HDIEALTVDN PETAIVSHDH PHPQPGDTSD LNYLQEQVGG
MLKITPSDVE NDESDYWLLS NAEISMTDIW KTDSGIDWDY GIADVSTPPP GMGEIAPTAV
DSTPR
