E2FC_ARATH
ID E2FC_ARATH Reviewed; 396 AA.
AC Q9FV70; Q94LY0; Q9FZG7;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Transcription factor E2FC;
DE AltName: Full=E2F transcription factor-2;
DE Short=AtE2F2;
GN Name=E2FC; Synonyms=E2F2; OrderedLocusNames=At1g47870; ORFNames=T2E6.2;
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], AND DEVELOPMENTAL STAGE.
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH DPA AND DPB,
RP DEVELOPMENTAL STAGE, GENE 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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION
RP 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [7]
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 [8]
RP FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, INTERACTION WITH SKP2A;
RP CDKA-1 AND MAIZE RBR1, INDUCTION BY LIGHT, AND PHOSPHORYLATION.
RX PubMed=12468727; DOI=10.1105/tpc.006791;
RA del Pozo J.C., Boniotti M.B., Gutierrez C.;
RT "Arabidopsis E2Fc functions in cell division and is degraded by the
RT ubiquitin-SCF(AtSKP2) pathway in response to light.";
RL Plant Cell 14:3057-3071(2002).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH DPB.
RX PubMed=16920782; DOI=10.1105/tpc.105.039651;
RA del Pozo J.C., Diaz-Trivino S., Cisneros N., Gutierrez C.;
RT "The balance between cell division and endoreplication depends on E2FC-DPB,
RT transcription factors regulated by the ubiquitin-SCFSKP2A pathway in
RT Arabidopsis.";
RL Plant Cell 18:2224-2235(2006).
RN [10]
RP INDUCTION BY LIGHT.
RX PubMed=18424613; DOI=10.1105/tpc.107.057075;
RA Lopez-Juez E., Dillon E., Magyar Z., Khan S., Hazeldine S., de Jager S.M.,
RA Murray J.A., Beemster G.T., Boegre L., Shanahan H.;
RT "Distinct light-initiated gene expression and cell cycle programs in the
RT shoot apex and cotyledons of Arabidopsis.";
RL Plant Cell 20:947-968(2008).
RN [11]
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).
RN [12]
RP INTERACTION WITH MYB3R3.
RC STRAIN=cv. Columbia;
RX PubMed=26069325; DOI=10.15252/embj.201490899;
RA Kobayashi K., Suzuki T., Iwata E., Nakamichi N., Suzuki T., Chen P.,
RA Ohtani M., Ishida T., Hosoya H., Mueller S., Leviczky T.,
RA Pettko-Szandtner A., Darula Z., Iwamoto A., Nomoto M., Tada Y.,
RA Higashiyama T., Demura T., Doonan J.H., Hauser M.T., Sugimoto K., Umeda M.,
RA Magyar Z., Boegre L., Ito M.;
RT "Transcriptional repression by MYB3R proteins regulates plant organ
RT growth.";
RL EMBO J. 34:1992-2007(2015).
CC -!- FUNCTION: Involved in transcriptional repression. May act by repressing
CC E2F-regulated genes in mature differentiated cells, but is not an
CC antagonist of E2FA. Restricts cell division and is involved in the
CC coordination between cell proliferation and endoreduplication during
CC development. May play a role during the transition from
CC skotomorphogenesis to photomorphogenesis. Regulated by phosphorylation-
CC dependent proteolysis via the protein-ubiquitin ligase SCF(SKP2A)
CC complex. {ECO:0000269|PubMed:11786543, ECO:0000269|PubMed:11891240,
CC ECO:0000269|PubMed:12468727, ECO:0000269|PubMed:16920782,
CC ECO:0000269|PubMed:19662336}.
CC -!- SUBUNIT: Heterodimer with DP proteins. Interacts preferentially with
CC DPB, but also with DPA. No interaction with DPB when phosphorylated.
CC Interacts with SKP2A, CDKA-1 and maize retinoblastoma-related protein
CC RBR1. Component of a DREAM-like complex which modulates a variety of
CC developmentally regulated genes and of the mitotic genes in
CC proliferating and differentiated cells. Interacts with MYB3R3 at later
CC stages of leaves development (PubMed:26069325).
CC {ECO:0000269|PubMed:11786543, ECO:0000269|PubMed:11891240,
CC ECO:0000269|PubMed:12468727, ECO:0000269|PubMed:16920782,
CC ECO:0000269|PubMed:26069325}.
CC -!- INTERACTION:
CC Q9FV70; Q9LKZ3: RBR1; NbExp=2; IntAct=EBI-2131346, EBI-398590;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11891240}.
CC Note=Interaction with either DPA or DPB are unable to induce a nuclear
CC localization.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9FV70-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in meristematic areas, vascular tissues,
CC apical part of the roots, cotyledons, upper region of the hypocotyls,
CC trichomes, young flower buds and pollen grains.
CC {ECO:0000269|PubMed:12468727, ECO:0000269|PubMed:16920782}.
CC -!- DEVELOPMENTAL STAGE: Expressed in a cell cycle-dependent manner. Not
CC detected at the G1/S transition, but increases during the progression
CC into S phase and peaks after the passage into G2.
CC {ECO:0000269|PubMed:11669580, ECO:0000269|PubMed:11786543,
CC ECO:0000269|PubMed:12468727}.
CC -!- INDUCTION: Down-regulated by light. {ECO:0000269|PubMed:12468727,
CC ECO:0000269|PubMed:18424613}.
CC -!- DOMAIN: The N-terminal region (1-100) is important for both SKP2A
CC binding and ubiquitin-mediated degradation.
CC -!- PTM: Phosphorylated by cyclin-dependent kinase. Phosphorylation is
CC necessary to target E2FC for proteolysis.
CC {ECO:0000269|PubMed:12468727}.
CC -!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF99806.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF242581; AAG17609.1; -; mRNA.
DR EMBL; AJ417834; CAD10631.1; -; mRNA.
DR EMBL; AB050114; BAB55644.1; -; mRNA.
DR EMBL; AC012463; AAF99806.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32222.1; -; Genomic_DNA.
DR EMBL; AY045636; AAK73994.1; -; mRNA.
DR EMBL; AY058231; AAL15405.1; -; mRNA.
DR PIR; B96519; B96519.
DR RefSeq; NP_175222.1; NM_103684.3. [Q9FV70-1]
DR AlphaFoldDB; Q9FV70; -.
DR SMR; Q9FV70; -.
DR BioGRID; 26427; 14.
DR IntAct; Q9FV70; 5.
DR STRING; 3702.AT1G47870.1; -.
DR PaxDb; Q9FV70; -.
DR PRIDE; Q9FV70; -.
DR ProteomicsDB; 222034; -. [Q9FV70-1]
DR EnsemblPlants; AT1G47870.1; AT1G47870.1; AT1G47870. [Q9FV70-1]
DR GeneID; 841202; -.
DR Gramene; AT1G47870.1; AT1G47870.1; AT1G47870. [Q9FV70-1]
DR KEGG; ath:AT1G47870; -.
DR Araport; AT1G47870; -.
DR TAIR; locus:2202390; AT1G47870.
DR eggNOG; KOG2577; Eukaryota.
DR InParanoid; Q9FV70; -.
DR PhylomeDB; Q9FV70; -.
DR PRO; PR:Q9FV70; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FV70; baseline and differential.
DR Genevisible; Q9FV70; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070176; C:DRM complex; IDA:TAIR.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
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; IDA:TAIR.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:TAIR.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0051301; P:cell division; IMP:TAIR.
DR GO; GO:0000902; P:cell morphogenesis; IMP:TAIR.
DR GO; GO:0042023; P:DNA endoreduplication; IMP:TAIR.
DR GO; GO:0019760; P:glucosinolate metabolic process; IMP:TAIR.
DR GO; GO:0051782; P:negative regulation of cell division; IMP:TAIR.
DR GO; GO:0043068; P:positive regulation of programmed cell death; IMP:TAIR.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0010767; P:regulation of transcription from RNA polymerase II promoter in response to UV-induced DNA damage; IMP:TAIR.
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 Alternative splicing; Cell cycle; Coiled coil; Cytoplasm; DNA-binding;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..396
FT /note="Transcription factor E2FC"
FT /id="PRO_0000406291"
FT DNA_BIND 155..220
FT /evidence="ECO:0000255"
FT REGION 34..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..264
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255"
FT REGION 376..391
FT /note="Retinoblastoma protein binding"
FT /evidence="ECO:0000255"
FT COILED 226..268
FT /evidence="ECO:0000255"
FT CONFLICT 297
FT /note="A -> T (in Ref. 3; BAB55644)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 396 AA; 44488 MW; 8D071E79F81BF567 CRC64;
MAATSNSGED PTLSYHHRSP FRFELLQSIS SSDPRYSSLT PSSTNRPFSV SQSLPNSQLS
PLISPHWDDS YSQITQKVQK SRKNHRIQLG SIANMSGGES IDIAKVIVKQ ESSPQNVKRV
YNKSKGGTKL LKAGKRMANG EVQNGGLNGA SINCRYDSSL GLLTKKFVKL IQEAEDGTLD
LNYCAVVLEV QKRRIYDITN VLEGIGLIEK TTKNHIRWKG ADNLGQKDLG DQISRLKSEV
ESMQSEESRL DDLIRERQEA LRSLEEDDYC RRYMFMTEED ITSLPRFQNQ TLLAIKAPTA
SYIEVPDPDE MSFPQQYRMV IRSRMGPIDV YLLSKYKGDS AETSDKLGNE SDQKAPVGVD
TPSLKIVTSD TDLKADYWFE SDAEVSLTDL WSNFNS
