ID   EBNA3_EBVA8             Reviewed;         925 AA.
AC   Q69138;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   29-SEP-2021, entry version 72.
DE   RecName: Full=Epstein-Barr nuclear antigen 3;
DE            Short=EBNA-3;
DE            Short=EBV nuclear antigen 3;
DE   AltName: Full=Epstein-Barr nuclear antigen 3A;
DE            Short=EBNA-3A;
DE            Short=EBV nuclear antigen 3A;
GN   Name=EBNA3; ORFNames=BLRF3-BERF1;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2166806; DOI=10.1128/jvi.64.9.4084-4092.1990;
RA   Sample J., Young L., Martin B., Chatman T., Kieff E.D., Rickinson A.;
RT   "Epstein-Barr virus types 1 and 2 differ in their EBNA-3A, EBNA-3B, and
RT   EBNA-3C genes.";
RL   J. Virol. 64:4084-4092(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1370413; DOI=10.1002/eji.1830220127;
RA   Apolloni A., Moss D., Stumm R., Burrows S., Suhrbier A., Misko I.,
RA   Schmidt C., Sculley T.;
RT   "Sequence variation of cytotoxic T cell epitopes in different isolates of
RT   Epstein-Barr virus.";
RL   Eur. J. Immunol. 22:183-189(1992).
CC   -!- FUNCTION: Plays an essential role for activation and immortalization of
CC       human B-cells. Represses transcription of viral promoters TP1 and Cp
CC       through interaction with host RBPJ, and inhibits EBNA2-mediated
CC       activation of these promoters. Since Cp is the promoter for all EBNA
CC       mRNAs, EBNA3A probably contributes to a negative autoregulatory control
CC       loop (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with human UCKL1. Interacts with host CTPB1; this
CC       interaction seems important for EBNA3-mediated transcriptional
CC       repression. Interacts with host RBPJ (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus matrix. Note=Associated with the
CC       nuclear matrix. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the herpesviridae EBNA-3 family. {ECO:0000305}.
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DR   EMBL; M34440; AAA45893.1; -; Genomic_DNA.
DR   EMBL; DQ279927; ABB89243.1; -; Genomic_DNA.
DR   PIR; S27920; S27920.
DR   RefSeq; YP_001129463.1; NC_009334.1.
DR   DIP; DIP-706N; -.
DR   PRIDE; Q69138; -.
DR   GeneID; 5176209; -.
DR   KEGG; vg:5176209; -.
DR   Proteomes; UP000007639; Genome.
DR   GO; GO:0044204; C:host cell nuclear matrix; 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..925
FT                   /note="Epstein-Barr nuclear antigen 3"
FT                   /id="PRO_0000375935"
FT   REGION          1..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          337..376
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          394..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          561..581
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          873..898
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..71
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        337..351
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..442
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   925 AA;  102423 MW;  B832E48B4A6EC7FE CRC64;
     MDKDRPGLPA PDDNIEEVPS TSGVQERASE GDWENVLIEI SDSSSEEEAE DAHLEPSQRG
     KKRKRVDDDA GGSAPAQHVP PPQLDHPGRE AILYRFPLDL RRFIQAIGAA ATHPDTRAID
     QFFGSQISNT DLYVMYAMAI RQAIRDRRRN PASRRSQVKW RMTTLAAGWP MGYQAYSSWM
     YSYTDPQVTA TIIHLQATLG CASGRRCHVT FSAGTFRPPR CSPGDRQWLY VQSRVGDLVQ
     SSNPCYSIFF DYMAIHRSLT KIWDEVVTPD QRVTFMEFLG FLQRTELVYI KSFVSYALGT
     TSIETPWMDE NPSTETAQAW NAGLLRGRAY GQDLLRTEGE HGEGATCETR EESEDTESDG
     DDEELPRVVS RDGTKHRRPP IFLRRLHRLL LMRAGKGKER ARETLAKAPR RTYGTPRPPV
     QKPRPEVPQS YETATSHGSA QVPEPPPTHP LHQQHSMAPC MVAQNPRAPL GDQLPGVPKD
     GRGACAPVPA LAGPIVRPWE SSLLQSPGRA FAPVSPQPMP VEPVPVPTVA LERPVCPAPP
     EIAMQGPGEP SGIKRTRERW RPAPWTPNPP RSPSQMSVRD RLARLRAEAQ ARQASVEVQP
     TQLTQVSPQQ PMERPLEPEQ QMFPGSPFSQ VADVARESGV PAMQPQYFDL PLTQPISQGA
     PAAPLRASMG PVPPVPATQP QYFDIPLTEP INQGASAAHF LPQQPMEGPL VPERWMFQGA
     TLSQSVRPGV AQSQYFDLPL TQPINHGAPA AHFLHQPPME GPWVPEQWMF QGAPPSQGTD
     VVQHQLDDLG YPLHDLNHPG VPVSPAVNQY HFSQAAFGLP IDEDESGERS DTSEPYEALD
     LSIHGRPCPQ APEWPVQGEG GQDATEVLDL SIHGRPRPRT PEWPVQGESG QNVTDHEPRR
     VVVSAIVHMC QDDEFPDLQD PPDEA