E2F5_RAT
ID E2F5_RAT Reviewed; 300 AA.
AC Q62814;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=Transcription factor E2F5;
DE Short=E2F-5;
DE Flags: Fragment;
GN Name=E2f5;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Lung;
RX PubMed=8589754;
RA Itoh A., Levinson S.F., Morita T., Kourembanas S., Brody J.S.,
RA Mitsialis S.A.;
RT "Structural characterization and specificity of expression of E2F-5: a new
RT member of the E2F family of transcription factors.";
RL Cell. Mol. Biol. Res. 41:147-154(1995).
CC -!- FUNCTION: Transcriptional activator that binds to E2F sites, these
CC sites are present in the promoter of many genes whose products are
CC involved in cell proliferation. May mediate growth factor-initiated
CC signal transduction. It is likely involved in the early responses of
CC resting cells to growth factor stimulation. Specifically required for
CC multiciliate cell differentiation: together with MCIDAS and E2F5, binds
CC and activate genes required for centriole biogenesis.
CC {ECO:0000250|UniProtKB:Q6DE14}.
CC -!- SUBUNIT: Component of the DRTF1/E2F transcription factor complex. Binds
CC cooperatively with DP-1 to E2F sites. Interaction with retinoblastoma
CC protein RB1 or proteins RBL1 and RBL2 inhibits the E2F transactivation
CC domain. Component of the DREAM complex (also named LINC complex) at
CC least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2,
CC RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The complex exists in quiescent
CC cells where it represses cell cycle-dependent genes. It dissociates in
CC S phase when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds
CC to MYBL2 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Found in placenta followed by kidney, lung and
CC brain.
CC -!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}.
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DR EMBL; U31668; AAB00180.1; -; mRNA.
DR AlphaFoldDB; Q62814; -.
DR SMR; Q62814; -.
DR STRING; 10116.ENSRNOP00000044464; -.
DR PaxDb; Q62814; -.
DR UCSC; RGD:621357; rat.
DR RGD; 621357; E2f5.
DR eggNOG; KOG2577; Eukaryota.
DR InParanoid; Q62814; -.
DR PhylomeDB; Q62814; -.
DR Reactome; R-RNO-1538133; G0 and Early G1.
DR Reactome; R-RNO-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR Reactome; R-RNO-69231; Cyclin D associated events in G1.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IBA:GO_Central.
DR GO; GO:0016528; C:sarcoplasm; IDA:RGD.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; ISO:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:RGD.
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:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR GO; GO:0009887; P:animal organ morphogenesis; ISO:RGD.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:0051726; P:regulation of cell cycle; TAS:RGD.
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; ISO:RGD.
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; IPR028316; E2F5.
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; 2.
DR PANTHER; PTHR12081:SF35; PTHR12081:SF35; 2.
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 2: Evidence at transcript level;
KW Activator; Cilium biogenesis/degradation; DNA-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN <1..300
FT /note="Transcription factor E2F5"
FT /id="PRO_0000219471"
FT DNA_BIND 2..73
FT /evidence="ECO:0000255"
FT REGION 31..53
FT /note="Leucine-zipper"
FT REGION 74..170
FT /note="Dimerization"
FT /evidence="ECO:0000255"
FT REGION 191..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..300
FT /note="Transactivation"
FT /evidence="ECO:0000255"
FT REGION 277..294
FT /note="RBL2 association"
FT /evidence="ECO:0000255"
FT MOTIF 36..73
FT /note="DEF box"
FT COMPBIAS 205..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
SQ SEQUENCE 300 AA; 33224 MW; 3FAF0AEA8875541E CRC64;
GGSSRHEKSL GLLTTKFVSL LQEAQDGVLD LKAAADTLAV RQKRRIYDIT NVLEGIDLIE
KKSKNSIQWK GVGAGCNTKE VIDRLRCLKA EIEDLELKER ELDQQKLWLQ QSIKNVMEDS
INNRFSYVTH EDICSCFNGD TLLAIQAPSG TQLEVPIPEM GQNGQKKYQI NLKSHSGPIH
VLLINKESNS SKPVVFPVPP PDDLTQPSSQ SSTSVTPPKS TMAAQNLPEQ HVSERSQNFQ
QTPATEISSG SISGDIIDEL MSSDVFPLLR LSPTPADDYN FNLDDNEGVC DLFDVQILNY
