E2F7_DANRE
ID E2F7_DANRE Reviewed; 723 AA.
AC Q5RIX9;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Transcription factor E2F7;
DE Short=E2F-7;
GN Name=e2f7; ORFNames=si:dkey-217k21.2;
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 e2f8. {ECO:0000250}.
CC -!- INTERACTION:
CC Q5RIX9; Q16665: HIF1A; Xeno; NbExp=2; IntAct=EBI-8030618, EBI-447269;
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; BX072538; CAI20917.2; -; Genomic_DNA.
DR RefSeq; NP_001038612.2; NM_001045147.2.
DR AlphaFoldDB; Q5RIX9; -.
DR SMR; Q5RIX9; -.
DR IntAct; Q5RIX9; 1.
DR MINT; Q5RIX9; -.
DR STRING; 7955.ENSDARP00000117568; -.
DR PaxDb; Q5RIX9; -.
DR Ensembl; ENSDART00000140760; ENSDARP00000117568; ENSDARG00000008986.
DR GeneID; 567941; -.
DR KEGG; dre:567941; -.
DR CTD; 144455; -.
DR ZFIN; ZDB-GENE-030131-3527; e2f7.
DR eggNOG; KOG2578; Eukaryota.
DR GeneTree; ENSGT00940000157713; -.
DR HOGENOM; CLU_014845_1_0_1; -.
DR InParanoid; Q5RIX9; -.
DR OMA; VEDSCQF; -.
DR OrthoDB; 145070at2759; -.
DR PhylomeDB; Q5RIX9; -.
DR TreeFam; TF105567; -.
DR Reactome; R-DRE-6804116; TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest.
DR SignaLink; Q5RIX9; -.
DR PRO; PR:Q5RIX9; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 4.
DR Bgee; ENSDARG00000008986; Expressed in testis and 22 other tissues.
DR ExpressionAtlas; Q5RIX9; baseline.
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; 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:0001946; P:lymphangiogenesis; IGI:ZFIN.
DR GO; GO:0008045; P:motor neuron axon guidance; IGI:ZFIN.
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: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 1: Evidence at protein level;
KW Activator; Cell cycle; DNA-binding; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..723
FT /note="Transcription factor E2F7"
FT /id="PRO_0000420706"
FT DNA_BIND 147..216
FT /evidence="ECO:0000255"
FT DNA_BIND 264..349
FT /evidence="ECO:0000255"
FT REGION 121..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..135
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..515
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 723 AA; 79326 MW; 679462218849C317 CRC64;
MQEVKCLTLK DLLGVRTLVN KTGSDDAASM NDHKENICMD RRKMTPLKSE SLTAALNGHG
KISSPEITHI TPIKLTEKAH PDPWTPTANL KMLINAASPD IRDREMKKTL FKPIENKGKI
AEEEEEEELD DSCQYEALDE SERRPSRKQK SLGLLCQKFL ALYPDYPESS ESINISLDEV
ATCLGVERRR IYDIVNVLES LMLVSRKAKN MYVWHGRSRL PQTLQGLLQA GRDQHYDLLM
DQREGNGLHA VQHVQNAHAA SSRRKDKSLR IMSQKFVMLF LVSKTQTVTL DMAAKILIEE
GQEESYDSKY KTKVRRLYDI ANVLTSLNLI KKIHMREEKT RKPVFKWIGP GNFQSSSNSD
DLRGQISNSG TERREKMARH SSFQVITAPP VNQRLISSAP STPHRYSTDE PVDYSRKSGN
NSAVCRLQFG DGVHPSVSPA VPSALASLAM PLQADLMPVP ASFSHPLAIL PQTPLLMLYS
GNISDGASSL RKRERSEEDD HQTTKCRRRS ASIESDTVES ESLSSSTRRS PVCSPEGSPW
DEASFGGLHE DDVAASSSKD ALLSPHYLYV PNTAGLNSFN FLLPAGHAQG GVPAVAMPYF
VVQSPLIAGA MPTSSTEGAA GFSVPTVLSP AQFVMAGGAY GVTEILQSPE HHGNVPATTS
SPRAEESPKP AQTQTPVTPK EASLGSKSFF ETPGAFGSLV NQSAARKRGS AQRRLDIGHT
AAN
