E2F3_MOUSE
ID E2F3_MOUSE Reviewed; 457 AA.
AC O35261; Q5T0I6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Transcription factor E2F3;
DE Short=E2F-3;
GN Name=E2f3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 102-457.
RC STRAIN=Swiss albino; TISSUE=Fibroblast;
RX PubMed=9376316; DOI=10.1016/s0925-4773(97)00083-x;
RA Dagnino L., Fry C.J., Bartley S.M., Farnham P., Gallie B.L., Phillips R.A.;
RT "Expression patterns of the E2F family of transcription factors during
RT mouse nervous system development.";
RL Mech. Dev. 66:13-25(1997).
RN [3]
RP DEVELOPMENTAL STAGE.
RX PubMed=9149906;
RA Dagnino L., Fry C.J., Bartley S.M., Farnham P., Gallie B.L., Phillips R.A.;
RT "Expression patterns of the E2F family of transcription factors during
RT murine epithelial development.";
RL Cell Growth Differ. 8:553-563(1997).
RN [4]
RP INTERACTION WITH EAPP.
RX PubMed=15716352; DOI=10.1091/mbc.e04-11-0975;
RA Novy M., Pohn R., Andorfer P., Novy-Weiland T., Galos B., Schwarzmayr L.,
RA Rotheneder H.;
RT "EAPP, a novel E2F binding protein that modulates E2F-dependent
RT transcription.";
RL Mol. Biol. Cell 16:2181-2190(2005).
RN [5]
RP FUNCTION.
RX PubMed=20176812; DOI=10.1128/mcb.01619-09;
RA Zaragoza K., Begay V., Schuetz A., Heinemann U., Leutz A.;
RT "Repression of transcriptional activity of C/EBPalpha by E2F-dimerization
RT partner complexes.";
RL Mol. Cell. Biol. 30:2293-2304(2010).
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 DRTF1/E2F complex
CC functions in the control of cell-cycle progression from G1 to S phase.
CC E2F3 binds specifically to RB1 in a cell-cycle dependent manner.
CC Inhibits adipogenesis, probably through the repression of CEBPA binding
CC to its target gene promoters (PubMed:20176812).
CC {ECO:0000269|PubMed:20176812}.
CC -!- SUBUNIT: Component of the DRTF1/E2F transcription factor complex. Binds
CC cooperatively with TFDP1/Dp-1 to E2F sites. Interacts with
CC retinoblastoma protein RB1 and related proteins (such as RBL1) that
CC inhibit the E2F transactivation domain. Binds EAPP.
CC {ECO:0000269|PubMed:15716352}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DEVELOPMENTAL STAGE: In the developing nervous system, high levels
CC expressed in both ventral and dorsal regions of the spinal cord from
CC 13.5 dpc. Also expressed in dorsal root and cranial ganglia in 11.5-
CC 18.5 dpc embryos. Only low levels of expression in developing brain. In
CC the developing retina (15.5 dpc), expression of E2F3 is localized to
CC the ganglion cell layer. In other developing tissues, expressed in
CC liver, lung and heart. Weak expression in developing kidney and
CC skeletal muscle. Absent from the developing choroid plexus, thymus and
CC developing skin. Low levels of expression in the developing intestinal
CC epithelium and mesenchyme in 12.5-18.5 dpc embryos.
CC {ECO:0000269|PubMed:9149906}.
CC -!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}.
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DR EMBL; AL513025; CAI24679.1; -; Genomic_DNA.
DR EMBL; AF015948; AAB71671.1; -; mRNA.
DR CCDS; CCDS26413.1; -.
DR RefSeq; NP_034223.1; NM_010093.3.
DR AlphaFoldDB; O35261; -.
DR SMR; O35261; -.
DR BioGRID; 199351; 2.
DR CORUM; O35261; -.
DR DIP; DIP-59314N; -.
DR IntAct; O35261; 1.
DR STRING; 10090.ENSMUSP00000100012; -.
DR iPTMnet; O35261; -.
DR PhosphoSitePlus; O35261; -.
DR EPD; O35261; -.
DR PaxDb; O35261; -.
DR PeptideAtlas; O35261; -.
DR PRIDE; O35261; -.
DR Antibodypedia; 10438; 349 antibodies from 36 providers.
DR DNASU; 13557; -.
DR Ensembl; ENSMUST00000102948; ENSMUSP00000100012; ENSMUSG00000016477.
DR GeneID; 13557; -.
DR KEGG; mmu:13557; -.
DR UCSC; uc007pyq.2; mouse.
DR CTD; 1871; -.
DR MGI; MGI:1096340; E2f3.
DR VEuPathDB; HostDB:ENSMUSG00000016477; -.
DR eggNOG; KOG2577; Eukaryota.
DR GeneTree; ENSGT00940000155115; -.
DR HOGENOM; CLU_032091_0_0_1; -.
DR InParanoid; O35261; -.
DR OrthoDB; 1087250at2759; -.
DR PhylomeDB; O35261; -.
DR TreeFam; TF105566; -.
DR Reactome; R-MMU-68911; G2 Phase.
DR Reactome; R-MMU-69231; Cyclin D associated events in G1.
DR BioGRID-ORCS; 13557; 3 hits in 73 CRISPR screens.
DR ChiTaRS; E2f3; mouse.
DR PRO; PR:O35261; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; O35261; protein.
DR Bgee; ENSMUSG00000016477; Expressed in floor plate of midbrain and 221 other tissues.
DR ExpressionAtlas; O35261; baseline and differential.
DR Genevisible; O35261; MM.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; ISO:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
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:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:0070345; P:negative regulation of fat cell proliferation; IMP:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:1905461; P:positive regulation of vascular associated smooth muscle cell apoptotic process; ISO:MGI.
DR GO; GO:0006606; P:protein import into nucleus; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
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; Cell cycle; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..457
FT /note="Transcription factor E2F3"
FT /id="PRO_0000219467"
FT DNA_BIND 147..237
FT /evidence="ECO:0000255"
FT REGION 80..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..145
FT /note="Cyclin A/CDK2 binding"
FT /evidence="ECO:0000255"
FT REGION 196..217
FT /note="Leucine-zipper"
FT REGION 238..329
FT /note="Dimerization"
FT /evidence="ECO:0000255"
FT REGION 350..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..457
FT /note="Transactivation"
FT /evidence="ECO:0000255"
FT REGION 424..441
FT /note="Retinoblastoma protein binding"
FT /evidence="ECO:0000255"
FT MOTIF 201..237
FT /note="DEF box"
FT COMPBIAS 89..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 102..109
FT /note="SSRVGLLQ -> CSSPTLLE (in Ref. 2; AAB71671)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="V -> L (in Ref. 2; AAB71671)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 457 AA; 48757 MW; 076AC9F360101075 CRC64;
MRKGIQPALE QYLVTAGGGE GAAVVAAAAA ASMDKRALLA SPGFAAAAAP GTYIQILTTN
PSTTSCATSL QSGALTAGPL LPSVPGTEPA ASSLYTTPQG PSSRVGLLQQ PPAPGRGGGG
GPPAKRRLEL GESGHQYLSD GLKTPKGKGR AALRSPDSPK TPKSPSEKTR YDTSLGLLTK
KFIQLLSQSP DGVLDLNKAA EVLKVQKRRI YDITNVLEGI HLIKKKSKNN VQWMGCSLSE
DGGMLAQCQG LSKEVTELSQ EEKKLDELIQ SCTLDLKLLT EDSENQRLAY VTYQDIRKIS
GLKDQTVIVV KAPPETRLEV PDSIESLQIH LASTQGPIEV YLCPEETETH RPMKTNNQDH
NGNIPKPTSK DLASNNSGHS DCSVSTANLS PLASPANLLQ QTEDQIPSNL EGPFVNLLPP
LLQEDYLLSL GEEEGISDLF DAYDLEKLPL VEDFMCS
