EBNA1_EBVA8
ID EBNA1_EBVA8 Reviewed; 641 AA.
AC Q1HVF7;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 23-FEB-2022, entry version 72.
DE RecName: Full=Epstein-Barr nuclear antigen 1;
DE Short=EBNA-1;
DE Short=EBV nuclear antigen 1;
GN Name=EBNA1; ORFNames=BKRF1;
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: Plays an essential role in replication and partitioning of
CC viral genomic DNA during latent viral infection. During this phase, the
CC circular double-stranded viral DNA undergoes replication once per cell
CC cycle and is efficiently partitioned to the daughter cells. EBNA1
CC activates the initiation of viral DNA replication through binding to
CC specific sites in the viral latent origin of replication, oriP.
CC Additionally, it governs the segregation of viral episomes by mediating
CC their attachment to host cell metaphase chromosomes. Also activates the
CC transcription of several viral latency genes. Finally, it can
CC counteract the stabilization of host p53/TP53 by host USP7, thereby
CC decreasing apoptosis and increasing host cell survival.
CC {ECO:0000250|UniProtKB:P03211}.
CC -!- SUBUNIT: Interacts with human USP7. Interacts with human EBP2; this
CC interaction is important for the stable segregation of EBV episomes
CC during cell division but not for the replication of the episomes.
CC Interacts with BGLF4; this interaction facilitates the switch from
CC latent to lytic DNA replication by down-regulating EBNA1 replication
CC function. Interacts with human PAX5; this interaction promotes EBNA1-
CC dependent transcription. {ECO:0000250|UniProtKB:P03211}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250|UniProtKB:P03211}.
CC -!- SIMILARITY: Belongs to the herpesviridae EBNA1 family. {ECO:0000305}.
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DR EMBL; DQ279927; ABB89251.1; -; Genomic_DNA.
DR RefSeq; YP_001129471.1; NC_009334.1.
DR PDB; 4PRB; X-ray; 1.75 A; C=407-417.
DR PDB; 4PRN; X-ray; 1.65 A; C=407-417.
DR PDBsum; 4PRB; -.
DR PDBsum; 4PRN; -.
DR SMR; Q1HVF7; -.
DR PRIDE; Q1HVF7; -.
DR GeneID; 5176225; -.
DR KEGG; vg:5176225; -.
DR Proteomes; UP000007639; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0006275; P:regulation of DNA replication; IEA:InterPro.
DR GO; GO:0039588; P:suppression by virus of host antigen processing and presentation; IEA:UniProtKB-KW.
DR GO; GO:0039644; P:suppression by virus of host NF-kappaB cascade; IEA:UniProtKB-KW.
DR GO; GO:0019042; P:viral latency; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.390; -; 1.
DR InterPro; IPR035975; E2/EBNA1_C_sf.
DR InterPro; IPR004186; EBNA1_DNA-bd.
DR InterPro; IPR037007; EBNA1_DNA-bd_sf.
DR Pfam; PF02905; EBV-NA1; 1.
DR SUPFAM; SSF54957; SSF54957; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; DNA-binding; Host nucleus; Host-virus interaction;
KW Inhibition of host adaptive immune response by virus;
KW Inhibition of host NF-kappa-B by virus;
KW Inhibition of host proteasome antigen processing by virus;
KW Reference proteome; Transcription; Transcription regulation;
KW Viral immunoevasion; Viral latency;
KW Viral latency initiation and maintenance.
FT CHAIN 1..641
FT /note="Epstein-Barr nuclear antigen 1"
FT /id="PRO_0000375933"
FT REGION 1..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..450
FT /note="Interaction with USP7"
FT /evidence="ECO:0000250"
FT REGION 612..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..641
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 413..415
FT /evidence="ECO:0007829|PDB:4PRN"
SQ SEQUENCE 641 AA; 56496 MW; 53A0B8451AC7A621 CRC64;
MSDEGPGTGP GNGLGQKEDT SGPDGSSGSG PQRRGGDNHG RGRGRGRGRG GGRPGAPGGS
GSGPRHRDGV RRPQKRPSCI GCKGAHGGTG AGGGAGAGGA GAGGAGAGGA GAGGAGAGGA
GAGGAGAGGA GAGGAGAGGA GAGGGAGAGG AGAGGAGAGG GAGAGGGAGA GGGAGAGGGA
GAGGGAGAGG GAGAGGGAGA GGGAGAGGGA GAGGAGAGGA GAGGGAGAGG GAGAGGGAGA
GGGAGAGGGA GAGGGAGAGG GAGAGGGAGA GGGAGAGGGA GAGGGAGAGG GAGAGGGAGA
GGGAGAGGGA GAGGGAGAGG GAGAGGGGRG RGGSGGRGRG GSGGRGRGGS GGRRGRGRER
ARGGSRERAR GRGRGRGEKR PRSPSSQSSS SGSPPRRPPP GRRPFFHPVA EADYFEYHQE
GGPDGEPDMP PGAIEQGPAD DPGEGPSTGP RGQGDGGRRK KGGWYGKHRG EGGSSQKFEN
IAEGLRLLLA RCHVERTTED GNWVAGVFVY GGSKTSLYNL RRGIGLAIPQ CRLTPLSRLP
FGMAPGPGPQ PGPLRESIVC YFIVFLQTHI FAEGLKDAIK DLVLPKPAPT CNIKVTVCSF
DDGVDLPPWF PPMVEGAAAE GDDGDDGDEG GDGDEGEEGQ E
