E2F8_DANRE
ID E2F8_DANRE Reviewed; 917 AA.
AC F1QZ88;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Transcription factor E2F8;
DE Short=E2F-8;
GN Name=e2f8; ORFNames=si:ch211-215h6.2;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22903062; DOI=10.1038/emboj.2012.231;
RA Weijts B.G., Bakker W.J., Cornelissen P.W., Liang K.H., Schaftenaar F.H.,
RA Westendorp B., de Wolf C.A., Paciejewska M., Scheele C.L., Kent L.,
RA Leone G., Schulte-Merker S., de Bruin A.;
RT "E2F7 and E2F8 promote angiogenesis through transcriptional activation of
RT VEGFA in cooperation with HIF1.";
RL EMBO J. 31:3871-3884(2012).
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 (By similarity).
CC Acts as a promoter of sprouting angiogenesis, possibly by acting as a
CC transcription activator and promoting expression of vegfa.
CC {ECO:0000250, ECO:0000269|PubMed:22903062}.
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 -!- DISRUPTION PHENOTYPE: Embryos lacking both e2f7 and e2f8 contain
CC multiple intersegmental arteries that completely fail to migrate from
CC the dorsal aorta. Gross morphology of these embryos and initial
CC formation of main axial vessels are unaltered.
CC {ECO:0000269|PubMed:22903062}.
CC -!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}.
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DR EMBL; BX890598; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU041375; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001334620.1; NM_001347691.1.
DR RefSeq; XP_694311.6; XM_689219.8.
DR AlphaFoldDB; F1QZ88; -.
DR SMR; F1QZ88; -.
DR STRING; 7955.ENSDARP00000074403; -.
DR PaxDb; F1QZ88; -.
DR Ensembl; ENSDART00000128488; ENSDARP00000105923; ENSDARG00000057323.
DR GeneID; 565952; -.
DR KEGG; dre:565952; -.
DR CTD; 79733; -.
DR ZFIN; ZDB-GENE-041111-260; e2f8.
DR eggNOG; KOG2578; Eukaryota.
DR GeneTree; ENSGT00940000158651; -.
DR HOGENOM; CLU_014845_2_0_1; -.
DR InParanoid; F1QZ88; -.
DR OMA; NGHTEMC; -.
DR OrthoDB; 145070at2759; -.
DR Reactome; R-DRE-6804116; TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest.
DR PRO; PR:F1QZ88; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 7.
DR Bgee; ENSDARG00000057323; Expressed in testis and 32 other tissues.
DR ExpressionAtlas; F1QZ88; baseline and differential.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IDA:ZFIN.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IMP: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:0001946; P:lymphangiogenesis; IGI:ZFIN.
DR GO; GO:0008045; P:motor neuron axon guidance; IGI:ZFIN.
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:0045892; P:negative regulation of transcription, DNA-templated; IGI:ZFIN.
DR GO; GO:0032877; P:positive regulation of DNA endoreduplication; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0002040; P:sprouting angiogenesis; IMP: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..917
FT /note="Transcription factor E2F8"
FT /id="PRO_0000420710"
FT DNA_BIND 126..195
FT /evidence="ECO:0000255"
FT DNA_BIND 273..359
FT /evidence="ECO:0000255"
FT REGION 1..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..610
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..833
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 917 AA; 100456 MW; 58C7ED1C1C41B812 CRC64;
MSSTLSEGQT LIKKSLSPSK ATSTNNKGHV FVEPQTPLKN SNKASTSEAA LPETLKIMGP
LTTPTKVLDA PSSDPWTPTS NLKMLISAAS PEIRNREKER AVDSSESENS QETEQGEEVE
KLHISRKDKS LGLLCYKFLA RYPNYPNPAL NNGISLDDVA AELHVERRRI YDIMNVLESL
NMVSRLAKNR YTWHGRVKLA QTLAVLKRAG KENRYEQLMQ QIRQRSQERE EREFDLDGEE
KENEEMSSFE VDGDSGLADL PGADSKAASA NSRKDKSLRV MSQKFVMLFL VSSPPVVSLD
VAAKILIGED HVVDQDKNKF KTKIRRLYDI ANVLSSLELI KKVHVTEDKG RKPAFKWTGP
EDIPSPKDLE ISTTSSAPKP LESRSSVENC AKNLFSSPGT KRGFTRHHSL VKLVKSIQDD
RRKINSAPSS PIKMTGDSAD SDFYTTKMAH LAAICKKHLD EQSADGRPNN AVTDSSQSSK
QPESTSASNH GPPGMQIPVL PAGAISYLPT KCSPIIPLLI PQHQTGGPYA VYMHPTSLRP
QPTSLAVRSM TFESPVGANA KTSPATLTSN NQTNQSSSYG KEQTSPVNLK RASGEKSSVG
SPSKMQRTEP KSVSPKLCEI LQARLKARRG ALTSNRPSAR ALHLEFSKPS ESQPTVQTGT
ASLEHSLETF LEKEEKSQTS DNEAGLTPVR QPHSQPQKLS APFQDMVLPS GPIHTETLIP
AGYLIPISQQ SIVNFREPQC SNESSKASTP TYNIYHTPTA GSRPAFPQEV TPTRLPLHRI
PPISPFPSHG HRLHSPSPAI LNFTLQNLGL IPGSVTPNPH TPEQSSSLQS PHPGLPHQGM
IFVKPMSPAR ALQQTSIHGQ PVTLISIPQA LVTTPKGGQA FQQSFFHTPV SFPTVNTTAP
KKIYIPQRKL DVSPEEI
