EBNA3_EBVB9
ID EBNA3_EBVB9 Reviewed; 944 AA.
AC P12977; P03202; Q66540; Q69021; Q8AZJ8;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 114.
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 B95-8) (HHV-4) (Human herpesvirus 4).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX NCBI_TaxID=10377;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=6087149; DOI=10.1038/310207a0;
RA Baer R., Bankier A.T., Biggin M.D., Deininger P.L., Farrell P.J.,
RA Gibson T.J., Hatfull G., Hudson G.S., Satchwell S.C., Seguin C.,
RA Tuffnell P.S., Barrell B.G.;
RT "DNA sequence and expression of the B95-8 Epstein-Barr virus genome.";
RL Nature 310:207-211(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3008094; DOI=10.1093/nar/14.6.2611;
RA Bodescot M., Brison O., Perricaudet M.;
RT "An Epstein-Barr virus transcription unit is at least 84 kilobases long.";
RL Nucleic Acids Res. 14:2611-2620(1986).
RN [3]
RP CHARACTERIZATION.
RX PubMed=3016714; DOI=10.1073/pnas.83.15.5693;
RA Hennessy K., Wang F., Bushman E.W., Kieff E.;
RT "Definitive identification of a member of the Epstein-Barr virus nuclear
RT protein 3 family.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:5693-5697(1986).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=2161150; DOI=10.1016/0042-6822(90)90027-o;
RA Petti L., Sample C., Kieff E.;
RT "Subnuclear localization and phosphorylation of Epstein-Barr virus latent
RT infection nuclear proteins.";
RL Virology 176:563-574(1990).
RN [5]
RP INTERACTION WITH HUMAN RBPJ.
RX PubMed=8627785; DOI=10.1128/jvi.70.5.3068-3074.1996;
RA Robertson E.S., Lin J., Kieff E.;
RT "The amino-terminal domains of Epstein-Barr virus nuclear proteins 3A, 3B,
RT and 3C interact with RBPJ(kappa).";
RL J. Virol. 70:3068-3074(1996).
RN [6]
RP INTERACTION WITH HUMAN UCKL1.
RC TISSUE=Heart;
RX PubMed=12199906; DOI=10.1186/1471-2121-3-23;
RA Kashuba E., Kashuba V., Sandalova T., Klein G., Szekely L.;
RT "Epstein-Barr virus encoded nuclear protein EBNA-3 binds a novel human
RT uridine kinase/uracil phosphoribosyltransferase.";
RL BMC Cell Biol. 3:23-23(2002).
RN [7]
RP INTERACTION WITH HUMAN CTBP1.
RX PubMed=12372828; DOI=10.1074/jbc.m208116200;
RA Hickabottom M., Parker G.A., Freemont P., Crook T., Allday M.J.;
RT "Two nonconsensus sites in the Epstein-Barr virus oncoprotein EBNA3A
RT cooperate to bind the co-repressor carboxyl-terminal-binding protein
RT (CtBP).";
RL J. Biol. Chem. 277:47197-47204(2002).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 325-333.
RX PubMed=12391232; DOI=10.4049/jimmunol.169.9.5153;
RA Kjer-Nielsen L., Clements C.S., Brooks A.G., Purcell A.W., Fontes M.R.,
RA McCluskey J., Rossjohn J.;
RT "The structure of HLA-B8 complexed to an immunodominant viral determinant:
RT peptide-induced conformational changes and a mode of MHC class I
RT dimerization.";
RL J. Immunol. 169:5153-5160(2002).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 406-414.
RX PubMed=17057332; DOI=10.1107/s0907444906027636;
RA Roder G., Blicher T., Justesen S., Johannesen B., Kristensen O.,
RA Kastrup J., Buus S., Gajhede M.;
RT "Crystal structures of two peptide-HLA-B*1501 complexes; structural
RT characterization of the HLA-B62 supertype.";
RL Acta Crystallogr. D 62:1300-1310(2006).
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.
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. {ECO:0000269|PubMed:12199906,
CC ECO:0000269|PubMed:12372828, ECO:0000269|PubMed:8627785}.
CC -!- INTERACTION:
CC P12977; P35869: AHR; Xeno; NbExp=5; IntAct=EBI-993115, EBI-80780;
CC P12977; Q06330: RBPJ; Xeno; NbExp=4; IntAct=EBI-993115, EBI-632552;
CC P12977; Q9NWZ5: UCKL1; Xeno; NbExp=4; IntAct=EBI-993115, EBI-2466660;
CC -!- SUBCELLULAR LOCATION: Host nucleus matrix {ECO:0000269|PubMed:2161150}.
CC Note=Associated with the nuclear matrix.
CC -!- SIMILARITY: Belongs to the herpesviridae EBNA-3 family. {ECO:0000305}.
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DR EMBL; V01555; CAB56341.1; ALT_SEQ; Genomic_DNA.
DR EMBL; V01555; CAA24856.1; ALT_TERM; Genomic_DNA.
DR EMBL; AJ507799; CAD53419.1; -; Genomic_DNA.
DR EMBL; X04060; CAA27693.1; ALT_SEQ; mRNA.
DR PIR; A24938; A24938.
DR PIR; C43042; QQBE23.
DR RefSeq; YP_401669.1; NC_007605.1.
DR PDB; 1M05; X-ray; 1.90 A; E/F=325-333.
DR PDB; 1XR8; X-ray; 2.30 A; C=406-414.
DR PDB; 5WMO; X-ray; 1.62 A; C=379-387.
DR PDB; 6VMX; X-ray; 3.10 A; C/H=379-387.
DR PDBsum; 1M05; -.
DR PDBsum; 1XR8; -.
DR PDBsum; 5WMO; -.
DR PDBsum; 6VMX; -.
DR SMR; P12977; -.
DR BioGRID; 3509104; 3.
DR IntAct; P12977; 4.
DR MINT; P12977; -.
DR DNASU; 3783762; -.
DR GeneID; 3783762; -.
DR KEGG; vg:3783762; -.
DR EvolutionaryTrace; P12977; -.
DR Proteomes; UP000153037; Genome.
DR GO; GO:0044204; C:host cell nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0039695; P:DNA-templated viral transcription; IDA:UniProtKB.
DR IDEAL; IID90029; -.
DR InterPro; IPR007706; EBNA-3/4/6.
DR Pfam; PF05009; EBV-NA3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Host nucleus; Host-virus interaction; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..944
FT /note="Epstein-Barr nuclear antigen 3"
FT /id="PRO_0000116177"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 944 AA; 103494 MW; 3413D9EA6BA7F06F CRC64;
MDKDRPGPPA LDDNMEEEVP STSVVQEQVS AGDWENVLIE LSDSSSEKEA EDAHLEPAQK
GTKRKRVDHD AGGSAPARPM LPPQPDLPGR EAILRRFPLD LRTLLQAIGA AATRIDTRAI
DQFFGSQISN TEMYIMYAMA IRQAIRDRRR NPASRRDQAK WRLQTLAAGW PMGYQAYSSW
MYSYTDHQTT PTFVHLQATL GCTGGRRCHV TFSAGTFKLP RCTPGDRQWL YVQSSVGNIV
QSCNPRYSIF FDYMAIHRSL TKIWEEVLTP DQRVSFMEFL GFLQRTDLSY IKSFVSDALG
TTSIQTPWID DNPSTETAQA WNAGFLRGRA YGIDLLRTEG EHVEGATGET REESEDTESD
GDDEDLPCIV SRGGPKVKRP PIFIRRLHRL LLMRAGKRTE QGKEVLEKAR GSTYGTPRPP
VPKPRPEVPQ SDETATSHGS AQVPEPPTIH LAAQGMAYPL HEQHGMAPCP VAQAPPTPLP
PVSPGDQLPG VFSDGRVACA PVPAPAGPIV RPWEPSLTQA AGQAFAPVRP QHMPVEPVPV
PTVALERPVY PKPVRPAPPK IAMQGPGETS GIRRARERWR PAPWTPNPPR SPSQMSVRDR
LARLRAEAQV KQASVEVQPP QLTQVSPQQP MEGPLVPEQQ MFPGAPFSQV ADVVRAPGVP
AMQPQYFDLP LIQPISQGAP VAPLRASMGP VPPVPATQPQ YFDIPLTEPI NQGASAAHFL
PQQPMEGPLV PEQWMFPGAA LSQSVRPGVA QSQYFDLPLT QPINHGAPAA HFLHQPPMEG
PWVPEQWMFQ GAPPSQGTDV VQHQLDALGY TLHGLNHPGV PVSPAVNQYH LSQAAFGLPI
DEDESGEGSD TSEPCEALDL SIHGRPCPQA PEWPVQEEGG QDATEVLDLS IHGRPRPRTP
EWPVQGEGGQ NVTGPETRRV VVSAVVHMCQ DDEFPDLQDP PDEA
