E2F4_XENLA
ID E2F4_XENLA Reviewed; 375 AA.
AC Q6DE14;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Transcription factor E2F4 {ECO:0000250|UniProtKB:Q16254};
DE Short=E2F-4 {ECO:0000250|UniProtKB:Q16254};
GN Name=e2f4 {ECO:0000312|Xenbase:XB-GENE-482725};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000312|EMBL:AAH77333.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary {ECO:0000312|EMBL:AAH77333.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND IDENTIFICATION IN THE EDM COMPLEX.
RX PubMed=24934224; DOI=10.1101/gad.243832.114;
RA Ma L., Quigley I., Omran H., Kintner C.;
RT "Multicilin drives centriole biogenesis via E2f proteins.";
RL Genes Dev. 28:1461-1471(2014).
CC -!- FUNCTION: Transcription activator that binds DNA cooperatively with DP
CC proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in
CC the promoter region of a number of genes. Component of the EDM complex,
CC a complex specifically required for multiciliate cell differentiation:
CC the EDM complex binds and activate genes required for centriole
CC biogenesis. Activates genes required for centriole assembly (plk4,
CC cep152) and genes specifically required for motile cilia formation
CC (foxj1). Also promotes the deuterosome pathway of centriole biogenesis
CC by activating expression of deup1, but not its paralog cep63.
CC {ECO:0000250|UniProtKB:Q16254, ECO:0000269|PubMed:24934224}.
CC -!- SUBUNIT: Component of the drtf1/e2f transcription factor complex.
CC Component of the EDM complex, at least composed of e2f4, e2f5, mcidas
CC and tfdp1. {ECO:0000250|UniProtKB:Q16254, ECO:0000269|PubMed:24934224}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q16254}.
CC -!- SIMILARITY: Belongs to the E2F/DP family.
CC {ECO:0000255|RuleBase:RU003796}.
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DR EMBL; BC077333; AAH77333.1; -; mRNA.
DR RefSeq; NP_001086706.1; NM_001093237.1.
DR AlphaFoldDB; Q6DE14; -.
DR SMR; Q6DE14; -.
DR MaxQB; Q6DE14; -.
DR DNASU; 446541; -.
DR GeneID; 446541; -.
DR KEGG; xla:446541; -.
DR CTD; 446541; -.
DR Xenbase; XB-GENE-482725; e2f4.S.
DR OMA; VQNSPHT; -.
DR OrthoDB; 1087250at2759; -.
DR Proteomes; UP000186698; Chromosome 4S.
DR Bgee; 446541; Expressed in blastula and 19 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005667; C:transcription regulator complex; IEA:InterPro.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0098534; P:centriole assembly; IMP:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; IEA:InterPro.
DR GO; GO:0044458; P:motile cilium assembly; IMP:UniProtKB.
DR GO; GO:1903251; P:multi-ciliated epithelial cell differentiation; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR CDD; cd14660; E2F_DD; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR015633; E2F.
DR InterPro; IPR037241; E2F-DP_heterodim.
DR InterPro; IPR028312; E2F4.
DR InterPro; IPR032198; E2F_CC-MB.
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 PANTHER; PTHR12081:SF42; PTHR12081:SF42; 1.
DR Pfam; PF16421; E2F_CC-MB; 1.
DR Pfam; PF02319; E2F_TDP; 1.
DR SMART; SM01372; E2F_TDP; 1.
DR SUPFAM; SSF144074; SSF144074; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW Activator; Cilium biogenesis/degradation; DNA-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..375
FT /note="Transcription factor E2F4"
FT /id="PRO_0000430813"
FT DNA_BIND 12..81
FT /evidence="ECO:0000255"
FT REGION 39..61
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255"
FT REGION 82..177
FT /note="Dimerization"
FT /evidence="ECO:0000255"
FT REGION 197..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..375
FT /note="Transactivation"
FT /evidence="ECO:0000255"
FT MOTIF 44..81
FT /note="DEF box"
FT /evidence="ECO:0000250"
FT COMPBIAS 201..223
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 375 AA; 40909 MW; E81C809F35212AF4 CRC64;
MADPAQLTVT PSRHEKSLGL LTSKFVSLLQ EAEDGVLDLK AAADTLAVRQ KRRIYDITNV
LEGIGLIEKK SKNSIQWKGV GPGCNTREIA DKLIDLKAEL ADLEQREQEL DQQRVWVQQS
IKNVTDDVQN TGLAYLNHED ICRCFRGDTL LAIRAPSGTC LEVPVPENTN GQKKFQIHLK
STTGPIEVLL VNKDTSSSAP VVVPVPPPED LIQAPPAVPS TPQRPALTPQ NDIATSPAPT
VPHSTISNAE SQDCPTGQTF SMENTTSSRL PSIDTCPLQS SASLDNSNDS PDPSTSFQPI
KSDLSDVLEL PKDMISDFFD QTKECITSDL LEELMSSEVF APLLRLSPPP GDHDYVYNLD
ESEGVCDLFD VPINL