ID   E2F7_BOVIN              Reviewed;         911 AA.
AC   E1BE02;
DT   09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Transcription factor E2F7;
DE            Short=E2F-7;
GN   Name=E2F7;
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, polyploidization of specialized
CC       cells and DNA damage response. Mainly acts as a transcription repressor
CC       that binds DNA independently of DP proteins and specifically recognizes
CC       the E2 recognition site 5'-TTTC[CG]CGC-3'. Directly represses
CC       transcription of classical E2F transcription factors such as E2F1. Acts
CC       as a regulator of S-phase by recognizing and binding the E2-related
CC       site 5'-TTCCCGCC-3' and mediating repression of G1/S-regulated genes.
CC       Plays a key role in polyploidization of cells in placenta and liver by
CC       regulating the endocycle, probably by repressing genes promoting
CC       cytokinesis and antagonizing action of classical E2F proteins (E2F1,
CC       E2F2 and/or E2F3). Required for placental development by promoting
CC       polyploidization of trophoblast giant cells. Also involved in DNA
CC       damage response: up-regulated by p53/TP53 following genotoxic stress
CC       and acts as a downstream effector of p53/TP53-dependent repression by
CC       mediating repression of indirect p53/TP53 target genes involved in DNA
CC       replication. Acts as a promoter of sprouting angiogenesis, possibly by
CC       acting as a transcription activator: associates with HIF1A, recognizes
CC       and binds the VEGFA promoter, which is different from canonical E2
CC       recognition site, and activates expression of the VEGFA gene. Acts as a
CC       negative regulator of keratinocyte differentiation (By similarity).
CC       {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). Interacts with MN1
CC       (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q96AV8}.
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; DAAA02012389; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DAAA02012390; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; E1BE02; -.
DR   SMR; E1BE02; -.
DR   STRING; 9913.ENSBTAP00000022518; -.
DR   PaxDb; E1BE02; -.
DR   PRIDE; E1BE02; -.
DR   eggNOG; KOG2578; Eukaryota.
DR   HOGENOM; CLU_014845_1_0_1; -.
DR   InParanoid; E1BE02; -.
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; ISS:UniProtKB.
DR   GO; GO:0060718; P:chorionic trophoblast cell differentiation; ISS:UniProtKB.
DR   GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; ISS:UniProtKB.
DR   GO; GO:0070365; P:hepatocyte differentiation; ISS:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0032466; P:negative regulation of cytokinesis; ISS:UniProtKB.
DR   GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0071930; P:negative regulation of transcription involved in G1/S transition of mitotic cell cycle; 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 damage; DNA-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..911
FT                   /note="Transcription factor E2F7"
FT                   /id="PRO_0000420704"
FT   DNA_BIND        141..210
FT                   /evidence="ECO:0000255"
FT   DNA_BIND        281..366
FT                   /evidence="ECO:0000255"
FT   REGION          239..281
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          409..433
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          565..706
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          873..911
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        239..260
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        565..579
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        594..624
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        652..689
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        896..911
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         94
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96AV8"
FT   MOD_RES         409
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96AV8"
FT   MOD_RES         840
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96AV8"
SQ   SEQUENCE   911 AA;  99229 MW;  E86944E740E22C4C CRC64;
     MEVNCLTLKD LISRPPRLDF AIEDGENAQK ENIFVDLSRM APKTPIKNEP IDLSKQKIFT
     PERNPITPVK LVDRQQVEPW TPTANLKILI SAASPDIRDR EKKKELFRPI ENKDDVFTDS
     LQLDAVDDSA VDEFEKQRPS RKQKSLGLLC QKFLARYPSY PLSTEKTTIS LDEVAVSLGV
     ERRRIYDIVN VLESLHLVSR VAKNQYSWHG RHSLPKTLRN LQRLGEKQKY EEQMAHLQQK
     ELNPIDHKSG ERRRDGCPDS QDPQLLDFPE PDCPSSSANS RKDKSLKIMS QKFVMLFLVS
     KTKIVTLDVA AKILIEESQD IPDHSKFKTK VRRLYDIANV LTSLMLIKKV HVTEDRGRKP
     AFKWIGPVDF SSTDDDLVDV STPVLPELKK EIYGHVQFCA KQKLARHSSF NSEQASERTQ
     RKVNSEPSSP YRQKQGLGVY SLEIGSLAAV SRQKMEDNSE TVAFASQNMM PLPSSLDPAA
     PLPSPSVDSE YRVSPLCHQA LSAAQTDLKA LPAQNGLNGQ GGVSLASMAL DVEHQPQPLA
     AAQPLLYVPP APLFMLCGGL QEGLSPGSGS GSGSVGGGSE VTAAEQPPMP SGQKRLSKER
     RLQEEEEEPA TKRQCRDHED GPLSLVMPKK PSDSADIASP KTSENRASAP HEDTHMNGQL
     SAAKAVSGKA TTNGFVSSEW GNPCSNTEIE KPSEENESTK GPSPLQYLYV QPPAGLNGLS
     VLLPSSQSPH AVGLPVGPLP SLSIQYMVLP SPALSGFPVL CSPTMPGPVS SAPSPLPNVG
     PVNFGLPGLG STAHLLIGPA AMVNPKSSTL PSTDPQLQGP CSLHLSPVMS RSHGSVQPGS
     PAYGSLPAAT VKLQQSPVPV TPKSIRCTHQ ETFFKTPGSL GDPVLRRKER NQSRSSSSAQ
     RRLEISSGGT D