EBNA4_EBVA8
ID EBNA4_EBVA8 Reviewed; 946 AA.
AC Q1HVG4;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 2.
DT 29-SEP-2021, entry version 48.
DE RecName: Full=Epstein-Barr nuclear antigen 4;
DE Short=EBNA-4;
DE Short=EBV nuclear antigen 4;
DE AltName: Full=Epstein-Barr nuclear antigen 3B;
DE Short=EBNA-3B;
DE Short=EBV nuclear antigen 3B;
GN Name=EBNA4; ORFNames=BERF2A-BERF2B;
OS Epstein-Barr virus (strain AG876) (HHV-4) (Human herpesvirus 4).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX NCBI_TaxID=82830;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16490228; DOI=10.1016/j.virol.2006.01.015;
RA Dolan A., Addison C., Gatherer D., Davison A.J., McGeoch D.J.;
RT "The genome of Epstein-Barr virus type 2 strain AG876.";
RL Virology 350:164-170(2006).
CC -!- FUNCTION: May be involved in transcriptional regulation of both viral
CC and cellular genes by interacting with the host DNA-binding protein
CC RBPJ. {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via N-terminus) with host RBPJ. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Host nucleus.
CC -!- SIMILARITY: Belongs to the herpesviridae EBNA-4 family. {ECO:0000305}.
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DR EMBL; DQ279927; ABB89244.1; ALT_SEQ; Genomic_DNA.
DR PRIDE; Q1HVG4; -.
DR Proteomes; UP000007639; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016032; P:viral process; IEA:InterPro.
DR InterPro; IPR007706; EBNA-3/4/6.
DR Pfam; PF05009; EBV-NA3; 1.
PE 3: Inferred from homology;
KW Host nucleus; Host-virus interaction; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..946
FT /note="Epstein-Barr nuclear antigen 4"
FT /id="PRO_0000375938"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 858..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..82
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..379
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..618
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..761
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..919
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..946
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 946 AA; 104104 MW; 7F428D409134E869 CRC64;
MKKAWLSRAQ QADAGGASGS EDPPDYGDQG NVQQVGSDPI SPAIGPFELS AASEDDPQSG
PVEENLDAAA REEEEPDEQE HNGGDDPLEV HTRQPRFVDV NPTQAPVIQL VHAVYDSMLQ
SDLRSLGSLF LEQNLNIEEF IWMCMTVRHR CQAIRQKPLP IDKQRRWKLL SPYRTWRMGY
RTQTLNVNSF ETGGDKVHPL LVTATLGCEE GLRHAITYSA GIVQLPRMSD QNQKIETAFL
MARRARSLSA ERYTLFFDLV SSGNTLYAIW IGLGTRNRVA FVEFVGWLCK KDHTHIREWF
RQCTGRPSPS KPWMRAHPVA VPYDDPLTSE ETDLAYARGL AMSIEAARLP DDPIIVEDDD
ESEEIEDKCD KDEEESGTED VTSIPQTLPH SPTVYGRPSV FYRKPDTKST KKCRAIVTDL
SIIKVIEDEH RKKKTARTEQ PRAKPDSPAP TVVLRRPPTQ KVTGPAGSLS VQAQLEPWQP
LSWPHETRVI LHGPPTQGDQ AHGSMLDLLE KDDQHMEQQV MATLLPPEPH QPRSGRRAPC
VYTADLDIES DEPATSEPVL DQLLPAPGLG PLAIQPLTSP TTSQLRSSAP SHAQTPWPVT
HPSQTPGGPT TQSLAPETEA PRQWPMPLRP IPLHPLRMQP ISFNPAVRPT PHQPPQVEPT
FYQSTWVKPP QQYQPQMGHI PYQPRPTGHS TMLRPQWAPT TMQPPPRAPT PMPPPQGPPT
AMQRPQGAPT PMPPPQGPPT AMQRPRGAPT PMPPPQGPPT AMQLSPRALT GQKGPAKHIL
RQLLTGGVKS GRPSLKFKAA LERQAAAGLR PSPGSGTGAK IVQAPVFYPP VLQPIQVMWQ
VGSSKAVAAS TVTQAPTEYT GERRLGGPMS PTDIPPSKRV KKKAYPERKT PHGGPSHSST
VMWENVSQGQ QQTLECGGTD KQERNMLGMG DIAVSSPSSS ETSNDE