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Transcription factor E2FA (E2F transcription factor-3) (AtE2F3)

 E2FA_ARATH              Reviewed;         485 AA.
Q9FNY0; Q9C5B5; Q9FV69; Q9M454; Q9SJ49;
05-APR-2011, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
22-NOV-2017, entry version 122.
RecName: Full=Transcription factor E2FA;
AltName: Full=E2F transcription factor-3;
Short=AtE2F3;
Name=E2FA; Synonyms=E2F3, E2F4; OrderedLocusNames=At2g36010;
ORFNames=F11F19.8;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH DPA AND DPB,
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=11108847; DOI=10.1016/S0014-5793(00)02238-9;
Magyar Z., Atanassova A., De Veylder L., Rombauts S., Inze D.;
"Characterization of two distinct DP-related genes from Arabidopsis
thaliana.";
FEBS Lett. 486:79-87(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH
MAIZE RBR1, AND DEVELOPMENTAL STAGE.
STRAIN=cv. Columbia;
PubMed=11669580; DOI=10.1023/A:1011848528377;
de Jager S.M., Menges M., Bauer U.M., Murra J.A.;
"Arabidopsis E2F1 binds a sequence present in the promoter of S-phase-
regulated gene AtCDC6 and is a member of a multigene family with
differential activities.";
Plant Mol. Biol. 47:555-568(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH DPA
AND DPB, DEVELOPMENTAL STAGE, GENE FAMILY, AND NOMENCLATURE.
STRAIN=cv. Columbia;
PubMed=11786543; DOI=10.1074/jbc.M110616200;
Mariconti L., Pellegrini B., Cantoni R., Stevens R., Bergounioux C.,
Cella R., Albani D.;
"The E2F family of transcription factors from Arabidopsis thaliana.
Novel and conserved components of the retinoblastoma/E2F pathway in
plants.";
J. Biol. Chem. 277:9911-9919(2002).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Labra M., Ghiani A., Citterio S., Sgorbati S.;
"Isolation and characterization of E2F-like protein in Arabidopsis
thaliana.";
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[6]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
"Arabidopsis ORF Clones.";
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
[8]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=11889041; DOI=10.1093/emboj/21.6.1360;
De Veylder L., Beeckman T., Beemster G.T., de Almeida Engler J.,
Ormenese S., Maes S., Naudts M., Van Der Schueren E., Jacqmard A.,
Engler G., Inze D.;
"Control of proliferation, endoreduplication and differentiation by
the Arabidopsis E2Fa-DPa transcription factor.";
EMBO J. 21:1360-1368(2002).
[9]
INTERACTION WITH DPA; DPB AND E2FD.
PubMed=11867638; DOI=10.1074/jbc.M200913200;
Kosugi S., Ohashi Y.;
"E2Ls, E2F-like repressors of Arabidopsis that bind to E2F sites in a
monomeric form.";
J. Biol. Chem. 277:16553-16558(2002).
[10]
FUNCTION.
PubMed=11862494; DOI=10.1007/s00438-001-0624-7;
Rossignol P., Stevens R., Perennes C., Jasinski S., Cella R.,
Tremousaygue D., Bergounioux C.;
"AtE2F-a and AtDP-a, members of the E2F family of transcription
factors, induce Arabidopsis leaf cells to re-enter S phase.";
Mol. Genet. Genomics 266:995-1003(2002).
[11]
GENE FAMILY, AND NOMENCLATURE.
PubMed=11971144; DOI=10.1105/tpc.010445;
Vandepoele K., Raes J., de Veylder L., Rouze P., Rombauts S., Inze D.;
"Genome-wide analysis of core cell cycle genes in Arabidopsis.";
Plant Cell 14:903-916(2002).
[12]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DPA AND DPB.
STRAIN=cv. Columbia;
PubMed=11891240; DOI=10.1104/pp.010642;
Kosugi S., Ohashi Y.;
"Interaction of the Arabidopsis E2F and DP proteins confers their
concomitant nuclear translocation and transactivation.";
Plant Physiol. 128:833-843(2002).
[13]
FUNCTION.
PubMed=12913157; DOI=10.1104/pp.103.025080;
Kosugi S., Ohashi Y.;
"Constitutive E2F expression in tobacco plants exhibits altered cell
cycle control and morphological change in a cell type-specific
manner.";
Plant Physiol. 132:2012-2022(2003).
[14]
FUNCTION.
PubMed=15377755; DOI=10.1105/tpc.104.024398;
Boudolf V., Vlieghe K., Beemster G.T.S., Magyar Z.,
Torres Acosta J.A., Maes S., Van Der Schueren E., Inze D.,
De Veylder L.;
"The plant-specific cyclin-dependent kinase CDKB1;1 and transcription
factor E2Fa-DPa control the balance of mitotically dividing and
endoreduplicating cells in Arabidopsis.";
Plant Cell 16:2683-2692(2004).
[15]
FUNCTION.
PubMed=16514015; DOI=10.1104/pp.106.077990;
Sozzani R., Maggio C., Varotto S., Canova S., Bergounioux C.,
Albani D., Cella R.;
"Interplay between Arabidopsis activating factors E2Fb and E2Fa in
cell cycle progression and development.";
Plant Physiol. 140:1355-1366(2006).
[16]
FUNCTION.
PubMed=19662336; DOI=10.1007/s11103-009-9527-5;
de Jager S.M., Scofield S., Huntley R.P., Robinson A.S.,
den Boer B.G., Murray J.A.;
"Dissecting regulatory pathways of G1/S control in Arabidopsis: common
and distinct targets of CYCD3;1, E2Fa and E2Fc.";
Plant Mol. Biol. 71:345-365(2009).
-!- FUNCTION: Transcription activator that binds DNA cooperatively
with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-
3' found in the promoter region of a number of genes whose
products are involved in cell cycle regulation or in DNA
replication. The binding of retinoblastoma-related proteins
represses transactivation. Regulates gene expression both
positively and negatively. Activates the expression of E2FB.
Involved in the control of cell-cycle progression from G1 to S
phase. Stimulates cell proliferation and delays differentiation.
{ECO:0000269|PubMed:11669580, ECO:0000269|PubMed:11786543,
ECO:0000269|PubMed:11862494, ECO:0000269|PubMed:11889041,
ECO:0000269|PubMed:11891240, ECO:0000269|PubMed:12913157,
ECO:0000269|PubMed:15377755, ECO:0000269|PubMed:16514015,
ECO:0000269|PubMed:19662336}.
-!- SUBUNIT: Heterodimer with DP proteins. Interacts (via dimerization
domain) preferentially with DPA, but also with DPB. Interacts with
maize retinoblastoma-related protein RBR1. No interaction with
E2FD. {ECO:0000269|PubMed:11108847, ECO:0000269|PubMed:11669580,
ECO:0000269|PubMed:11786543, ECO:0000269|PubMed:11867638,
ECO:0000269|PubMed:11891240}.
-!- INTERACTION:
Q9FNY3:DPA; NbExp=6; IntAct=EBI-1774747, EBI-1774763;
Q9FNY2:DPB; NbExp=5; IntAct=EBI-1774747, EBI-1774876;
Q9LKZ3:RBR1; NbExp=4; IntAct=EBI-1774747, EBI-398590;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11891240}.
Nucleus {ECO:0000269|PubMed:11891240}. Note=Interaction with DPA
induces an exclusive nuclear localization, but an interaction with
DPB has no effect.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9FNY0-1; Sequence=Displayed;
Name=2;
IsoId=Q9FNY0-2; Sequence=VSP_040803;
Name=3;
IsoId=Q9FNY0-3; Sequence=VSP_040801, VSP_040802;
-!- TISSUE SPECIFICITY: Highly expressed in the shoot apical meristem,
emerging leaf primordia, and vascular tissues of young leaf
primordia. Expressed in flowers, in epidermis and cortex of
hypocotyls, and at lower levels in leaves.
{ECO:0000269|PubMed:11108847, ECO:0000269|PubMed:11889041}.
-!- DEVELOPMENTAL STAGE: Expressed in a cell cycle-dependent manner.
Most abundant in early S phase. Decreased expression during the
passage into G2. {ECO:0000269|PubMed:11108847,
ECO:0000269|PubMed:11669580, ECO:0000269|PubMed:11786543}.
-!- DOMAIN: The C-terminal region (366-485) is required for
transactivational activity. The N-terminal region (92-128) is
important for nuclear localization.
-!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AJ294534; CAC15486.1; -; mRNA.
EMBL; AF242582; AAG17610.1; -; mRNA.
EMBL; AJ276619; CAC34724.1; -; mRNA.
EMBL; AJ271597; CAB70599.1; -; mRNA.
EMBL; AC007017; AAD21456.2; -; Genomic_DNA.
EMBL; CP002685; AEC09191.1; -; Genomic_DNA.
EMBL; CP002685; AEC09192.1; -; Genomic_DNA.
EMBL; BT026376; ABH04483.1; -; mRNA.
PIR; G84775; G84775.
RefSeq; NP_565831.3; NM_129160.4. [Q9FNY0-2]
RefSeq; NP_973610.1; NM_201881.2.
RefSeq; NP_973611.1; NM_201882.3. [Q9FNY0-1]
UniGene; At.10190; -.
UniGene; At.64435; -.
ProteinModelPortal; Q9FNY0; -.
SMR; Q9FNY0; -.
BioGrid; 3518; 17.
DIP; DIP-40175N; -.
IntAct; Q9FNY0; 11.
PRIDE; Q9FNY0; -.
EnsemblPlants; AT2G36010.1; AT2G36010.1; AT2G36010. [Q9FNY0-2]
EnsemblPlants; AT2G36010.3; AT2G36010.3; AT2G36010. [Q9FNY0-1]
GeneID; 818174; -.
Gramene; AT2G36010.1; AT2G36010.1; AT2G36010.
Gramene; AT2G36010.3; AT2G36010.3; AT2G36010.
KEGG; ath:AT2G36010; -.
Araport; AT2G36010; -.
HOGENOM; HOG000232044; -.
InParanoid; Q9FNY0; -.
KO; K06620; -.
PhylomeDB; Q9FNY0; -.
Reactome; R-ATH-1538133; G0 and Early G1.
Reactome; R-ATH-68689; CDC6 association with the ORC:origin complex.
Reactome; R-ATH-68911; G2 Phase.
Reactome; R-ATH-69298; Association of licensing factors with the pre-replicative complex.
Reactome; R-ATH-8953750; Transcriptional Regulation by E2F6.
PRO; PR:Q9FNY0; -.
Proteomes; UP000006548; Chromosome 2.
ExpressionAtlas; Q9FNY0; baseline and differential.
Genevisible; Q9FNY0; AT.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005667; C:transcription factor complex; IEA:InterPro.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051446; P:positive regulation of meiotic cell cycle; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd14660; E2F_DD; 1.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR015633; E2F.
InterPro; IPR037241; E2F-DP_heterodim.
InterPro; IPR032198; E2F_CC-MB.
InterPro; IPR003316; E2F_WHTH_DNA-bd_dom.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
PANTHER; PTHR12081; PTHR12081; 1.
Pfam; PF16421; E2F_CC-MB; 1.
Pfam; PF02319; E2F_TDP; 1.
SMART; SM01372; E2F_TDP; 1.
SUPFAM; SSF144074; SSF144074; 1.
SUPFAM; SSF46785; SSF46785; 1.
1: Evidence at protein level;
Activator; Alternative splicing; Cell cycle; Coiled coil;
Complete proteome; Cytoplasm; DNA-binding; Nucleus;
Reference proteome; Repressor; Transcription;
Transcription regulation.
CHAIN 1 485 Transcription factor E2FA.
/FTId=PRO_0000406289.
DNA_BIND 167 232
REGION 249 277 Leucine-zipper.
REGION 435 450 Retinoblastoma protein binding.
{ECO:0000255}.
COILED 245 286 {ECO:0000255}.
COMPBIAS 9 53 Pro-rich.
VAR_SEQ 92 92 P -> PIFPSEIGLEIRGCFGDFDCYLLLLSLIQKLRSVRL
SSIRVNFCRLFSFAM (in isoform 3).
{ECO:0000303|Ref.4}.
/FTId=VSP_040801.
VAR_SEQ 155 173 GSPITLTPSGSCRYDSSLG -> VRSFYEISFMSRVTS
(in isoform 3). {ECO:0000303|Ref.4}.
/FTId=VSP_040802.
VAR_SEQ 247 248 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_040803.
CONFLICT 264 264 D -> G (in Ref. 1; CAC15486).
{ECO:0000305}.
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


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