E2F8_BOVIN
ID E2F8_BOVIN Reviewed; 866 AA.
AC E1BKK0;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Transcription factor E2F8;
DE Short=E2F-8;
GN Name=E2F8;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
CC -!- FUNCTION: Atypical E2F transcription factor that participates in
CC various processes such as angiogenesis and polyploidization of
CC specialized cells. Mainly acts as a transcription repressor that binds
CC DNA independently of DP proteins and specifically recognizes the E2
CC recognition site 5'-TTTC[CG]CGC-3'. Directly represses transcription of
CC classical E2F transcription factors such as E2F1: component of a
CC feedback loop in S phase by repressing the expression of E2F1, thereby
CC preventing p53/TP53-dependent apoptosis. Plays a key role in
CC polyploidization of cells in placenta and liver by regulating the
CC endocycle, probably by repressing genes promoting cytokinesis and
CC antagonizing action of classical E2F proteins (E2F1, E2F2 and/or E2F3).
CC Required for placental development by promoting polyploidization of
CC trophoblast giant cells. Acts as a promoter of sprouting angiogenesis,
CC possibly by acting as a transcription activator: associates with HIF1A,
CC recognizes and binds the VEGFA promoter, which is different from
CC canonical E2 recognition site, and activates expression of the VEGFA
CC gene (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer and heterodimer: mainly forms homodimers and, to a
CC lesser extent, heterodimers with E2F8. Dimerization is important for
CC DNA-binding. Interacts with HIF1A (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: In contrast to classical members of the E2F transcription
CC factor, atypical members contain 2 DNA-binding domains and regulate
CC transcription in a DP-independent manner. Both DNA-binding domains are
CC required for DNA-binding and are proposed to form an intramolecular
CC structure that is similar to the winged helix structure of the E2F-DP
CC heterodimer (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}.
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DR EMBL; DAAA02062974; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001178163.1; NM_001191234.1.
DR AlphaFoldDB; E1BKK0; -.
DR SMR; E1BKK0; -.
DR STRING; 9913.ENSBTAP00000023190; -.
DR PaxDb; E1BKK0; -.
DR PRIDE; E1BKK0; -.
DR GeneID; 786629; -.
DR KEGG; bta:786629; -.
DR CTD; 79733; -.
DR eggNOG; KOG2578; Eukaryota.
DR HOGENOM; CLU_014845_2_0_1; -.
DR InParanoid; E1BKK0; -.
DR OrthoDB; 145070at2759; -.
DR TreeFam; TF105567; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0033301; P:cell cycle comprising mitosis without cytokinesis; ISS:UniProtKB.
DR GO; GO:0060718; P:chorionic trophoblast cell differentiation; ISS:UniProtKB.
DR GO; GO:0070365; P:hepatocyte differentiation; ISS:UniProtKB.
DR GO; GO:0032466; P:negative regulation of cytokinesis; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0001890; P:placenta development; ISS:UniProtKB.
DR GO; GO:0032877; P:positive regulation of DNA endoreduplication; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0002040; P:sprouting angiogenesis; ISS:UniProtKB.
DR GO; GO:0060707; P:trophoblast giant cell differentiation; ISS:UniProtKB.
DR Gene3D; 1.10.10.10; -; 2.
DR InterPro; IPR015633; E2F.
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; PF02319; E2F_TDP; 2.
DR SMART; SM01372; E2F_TDP; 2.
DR SUPFAM; SSF46785; SSF46785; 2.
PE 3: Inferred from homology;
KW Activator; Cell cycle; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..866
FT /note="Transcription factor E2F8"
FT /id="PRO_0000420708"
FT DNA_BIND 113..182
FT /evidence="ECO:0000255"
FT DNA_BIND 261..347
FT /evidence="ECO:0000255"
FT REGION 409..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..624
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..812
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A0AVK6"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A0AVK6"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A0AVK6"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A0AVK6"
SQ SEQUENCE 866 AA; 94043 MW; 11EF64179816FCE5 CRC64;
MENEKENLFF EPHKRGLMKT PLKESTAANI VLADIQPDFG PLTTPTKPKE ISQGEPWTPT
ANLKMLISAV SPEIRNRDQK RGLFDNRNGL SDVKDCLHEH FSGDEYEKSQ PSRKEKSLGL
LCHKFLARYP NYPNPAVNND ICLDEVAEEL NVERRRIYDI VNVLESLHMV SRLAKNRYTW
HGRHNLNQIL ETLKSVGEEN KYAEQIMMIK KKEYEQEFEV SKSYNTEDPI IKSNTGQNGH
PDMCCAERPG VELRAASVNS RKDKSLKVMS QKFVTLFLVS TPQIVSLEIA AKILTWEDHV
EDLDRSKFKT KIRRLYDIAN VLSSLDLIKK VHVTEERGRK PAFKWTGPEI SPNPSGLSPV
LPCAASDLEA RQSSKENCAK NLFSTRGKPN FTRHPSLIKL VKSIESDRRK INSAPSSPIK
THKAESTQNS VPFRSKMAQL AAICKMQLEE QSSEPRKNVT VQLAGSGHCK SVAPLDTPAN
AEPEMMAPSL IQPLGVVPLL PSPLSPAVPV ILPQTPSGTS YAIYLQPAQA QTITPPPGLS
PTVCPTTSSN AMISEDSTDA TGENADSDAP KSSVSTRPGS LLPGPERQGA KNREREPARE
KGSKRASMLE DSGSKKKFKE DQKAPENVST TLFPSGYLIP LTQCSTLGAE SILSSNENSG
TLSPNHSIYS SPIAGVIPVT SSELTAVNFP SFQVTPLKLM VSPTSMAAVP VGNSPALSSS
HPLPIQNPSS AIVNFTLQHL GLISPGVQVS TSPGPGTIAV SPRIEAVSVT PENAGAEQGR
ATKCDASILS QNQTNGQSFA GTGAQQPVPV TPKGSQPVAE SFFRTPGGPT KPTGSPCTDF
DGANYTSVGT LLVPQRKLEV SVEDVH
