ID   E2F7_XENTR              Reviewed;         862 AA.
AC   F6YVB9;
DT   09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Transcription factor E2F7;
DE            Short=E2F-7;
GN   Name=e2f7;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20431018; DOI=10.1126/science.1183670;
RA   Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA   Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA   Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA   Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA   Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA   Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA   Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA   Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA   Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT   "The genome of the Western clawed frog Xenopus tropicalis.";
RL   Science 328:633-636(2010).
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. Acts as a regulator
CC       of S-phase by recognizing and binding the E2-related site 5'-TTCCCGCC-
CC       3' and mediating repression of G1/S-regulated genes. Acts as a promoter
CC       of sprouting angiogenesis, possibly by acting as a transcription
CC       activator (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer and heterodimer: mainly forms homodimers and, to a
CC       lesser extent, heterodimers with e2f8. {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; AAMC01048174; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAMC01048175; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAMC01048176; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; F6YVB9; -.
DR   SMR; F6YVB9; -.
DR   STRING; 8364.ENSXETP00000031323; -.
DR   PaxDb; F6YVB9; -.
DR   eggNOG; KOG2578; Eukaryota.
DR   HOGENOM; CLU_014845_1_0_1; -.
DR   InParanoid; F6YVB9; -.
DR   OMA; VEDSCQF; -.
DR   TreeFam; TF105567; -.
DR   Proteomes; UP000008143; Genome assembly.
DR   Proteomes; UP000790000; 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: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   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; Reference proteome; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..862
FT                   /note="Transcription factor E2F7"
FT                   /id="PRO_0000420707"
FT   DNA_BIND        140..209
FT                   /evidence="ECO:0000255"
FT   DNA_BIND        279..364
FT                   /evidence="ECO:0000255"
FT   REGION          561..592
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          617..643
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          788..862
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        574..592
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        788..814
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        829..862
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   862 AA;  95487 MW;  00A75B31066023E2 CRC64;
     MEVTSCLTLK DLISTKKNKS DPVADGRSAQ KENMFDRFKI SPRLPLRSEP IDLSKQKSFT
     PERIPVTPVK VAERPQADPW TPTANLKMLI SAASPEIRDR EKKKELFRPI ENNGIEETDT
     DLQLMDSVDD IDDLEKRPSR KQKSLGLLCQ KFLARYPSYP ISTEKMTISL DEAASSLGVE
     RRRIYDIVNV LESLHLVSRV AKNQYCWHGQ HNLNETLRNL QHIGEKQNYR AQIACFNLRD
     MGMEYKCDEQ EKGCHIDHLN TPLIELSEAD CPSVSSSSRK DKSLRIMSQK FVMLFLVSTT
     KIITLEIAAK ILIEESQDAA DHSKFKTKVR RLYDIANVLT SLGLIKKVHV TDERGRKPAF
     KWIGPVDFTA EDQKMEVTTT IPSPDSKKDA CNLSPASDRV KQRLFRHSSF NIVQSFSAVK
     RKVCSHPCSP QKPQGVESSD SYASKMAHLA TICKPKAEED SKNGNIENSS LPFSVVVPMP
     VDSDYRVKPV VHQVPLVSHK TVCEPLGIMP PSQSNEDCTN HGFVPNQPYM YLPSNSVFML
     CGNLSEGKAT DHLAMSLYPV PGSDSPTLEE TTMSKQERPT KRQLNDKDDA PLSLVLPKKS
     RVDNTQSLQK PICKTTTPEQ LQHVSREEEY NTEPVTKHSN VGETTEEVGS RILPHENVHL
     HPAVPPQFLY VPTTQGLNSF NFLLPANHSA GLSQSQLASL NVPYVMVPSS ALTAFPFICS
     PAVSSGASGS TLNGRMNFSQ AGTSSPTRLI IGAPQMAVPQ PPEPAVDQTK NLSPLSVSPV
     SAKCASSKAD SHDSLSQSIH TAKLHKSPTP STPKSIRPLH KDAFFKTPGS LDVSSSRKPQ
     RTQTRTSSSA QRKLDIDSSA GN