E2F8_XENTR
ID E2F8_XENTR Reviewed; 736 AA.
AC F7EA39;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Transcription factor E2F8;
DE Short=E2F-8;
GN Name=e2f8;
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 e2f7. {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; AAMC01129757; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; F7EA39; -.
DR SMR; F7EA39; -.
DR PaxDb; F7EA39; -.
DR eggNOG; KOG2578; Eukaryota.
DR HOGENOM; CLU_014845_2_0_1; -.
DR InParanoid; F7EA39; -.
DR OMA; NGHTEMC; -.
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; 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: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..736
FT /note="Transcription factor E2F8"
FT /id="PRO_0000420711"
FT DNA_BIND 98..167
FT /evidence="ECO:0000255"
FT DNA_BIND 240..326
FT /evidence="ECO:0000255"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..549
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 736 AA; 80331 MW; F2388BE4FDD2E7E5 CRC64;
MEEGSKENCG FNGSPMGSRS PPKQLTSAAS VLGEIQIAAA NLKTPTKPQE RNNADPWTPT
ANLKMLISAA SPEIRNRERE ILEEQFSGDE LEKTLPSRKE KSLGLLCHKF LARYPSYPNP
AVNNSICLDE VAGELSVERR RIYDIVNVLE SLHMVSRLAK NKYIWHGRLN LSKTFDALKK
VGEENRYGEQ IQLLRKREQE ECDSQNSPNA ETQKPLAKQP EVGFVELPGL EFRAASVNSR
KEKSLRVMSQ RFVMLFLVSD PQIVSLEVAA KILIGEDQLE DLDKSKFKTK IRRLYDIANV
LTSLNLIKKV HVTEEKGRKP AFQWTCPELC TDDQENRSSP AALTPVAIDL SSPKENCAKN
LFASGGKTFT RHPSLIKLAK SIENDRRKIN SAPSSPIKSG DGSSSAASKM AQLAAICKQQ
LQQSRDQTKV KLKVSACKAK STVKQPGGSD KNQTPTYCRA IPLLHPHPSA APPYTVIVQP
PQEQTLSRQS PPALGYTNRT PPEAPLQGGR HEGDGTSHSE DHSAQERHPK RLPESDRGCT
SKRMKSSAVD DVTETLYPSG YLIPIHLAPV APEPSKENTG PSSENKLFTS PIPGVFPLKL
MFSPGPVTAV PVMSRGGQHV GGGSGSASRS PSPGMFTFAL QNRELISAGL PQGATVSPRN
GRGQEELSAA SVLNCKHVSP VPYHGQPFTV FALQQSAVPV TPKGYHSLQE TFFRTPGGMG
CSPPESARKL DVGTDD