ID   MTP_EBVB9               Reviewed;        1318 AA.
AC   P03179; Q777H3;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   23-FEB-2022, entry version 108.
DE   RecName: Full=Major tegument protein;
DE            Short=MTP;
DE   AltName: Full=Protein p140;
GN   ORFNames=BNRF1;
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 [GENOMIC DNA].
RX   PubMed=2998073; DOI=10.1016/0042-6822(85)90229-6;
RA   Hudson G.S., Bankier A.T., Satchwell S.C., Barrell B.G.;
RT   "The short unique region of the B95-8 Epstein-Barr virus genome.";
RL   Virology 147:81-98(1985).
RN   [2]
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   [3]
RP   SUBCELLULAR LOCATION.
RX   PubMed=15534216; DOI=10.1073/pnas.0407320101;
RA   Johannsen E., Luftig M., Chase M.R., Weicksel S., Cahir-McFarland E.,
RA   Illanes D., Sarracino D., Kieff E.;
RT   "Proteins of purified Epstein-Barr virus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:16286-16291(2004).
RN   [4]
RP   FUNCTION.
RX   PubMed=3035208; DOI=10.1128/jvi.61.7.2063-2070.1987;
RA   Cameron K.R., Stamminger T., Craxton M., Bodemer W., Honess R.W.,
RA   Fleckenstein B.;
RT   "The 160,000-Mr virion protein encoded at the right end of the herpesvirus
RT   saimiri genome is homologous to the 140,000-Mr membrane antigen encoded at
RT   the left end of the Epstein-Barr virus genome.";
RL   J. Virol. 61:2063-2070(1987).
RN   [5]
RP   FUNCTION.
RX   PubMed=15927339; DOI=10.1016/j.biochi.2005.04.009;
RA   Lopez R., Urquiza M., Patino H., Suarez J., Reyes C., Patarroyo M.A.,
RA   Patarroyo M.E.;
RT   "A B-lymphocyte binding peptide from BNRF1 induced antibodies inhibiting
RT   EBV-invasion of B-lymphocytes.";
RL   Biochimie 87:985-992(2005).
RN   [6]
RP   FUNCTION.
RX   PubMed=16973549; DOI=10.1128/jvi.00473-06;
RA   Feederle R., Neuhierl B., Baldwin G., Bannert H., Hub B., Mautner J.,
RA   Behrends U., Delecluse H.J.;
RT   "Epstein-Barr virus BNRF1 protein allows efficient transfer from the
RT   endosomal compartment to the nucleus of primary B lymphocytes.";
RL   J. Virol. 80:9435-9443(2006).
RN   [7]
RP   FUNCTION, INTERACTION WITH HOST DAXX, AND SUBCELLULAR LOCATION.
RX   PubMed=22102817; DOI=10.1371/journal.ppat.1002376;
RA   Tsai K., Thikmyanova N., Wojcechowskyj J.A., Delecluse H.J.,
RA   Lieberman P.M.;
RT   "EBV tegument protein BNRF1 disrupts DAXX-ATRX to activate viral early gene
RT   transcription.";
RL   PLoS Pathog. 7:E1002376-E1002376(2011).
RN   [8]
RP   FUNCTION, AND INTERACTION WITH HOST DAXX.
RX   PubMed=25275136; DOI=10.1128/jvi.01895-14;
RA   Tsai K., Chan L., Gibeault R., Conn K., Dheekollu J., Domsic J.,
RA   Marmorstein R., Schang L.M., Lieberman P.M.;
RT   "Viral reprogramming of the Daxx histone H3.3 chaperone during early
RT   Epstein-Barr virus infection.";
RL   J. Virol. 88:14350-14363(2014).
CC   -!- FUNCTION: Tegument protein that plays a role in the inhibition of host
CC       intrinsic defenses to promote viral early gene activation. Interacts
CC       with host DAXX and thereby disrupts the complex between DAXX and ATRX.
CC       Suppresses the DAXX-ATRX dependent deposition of histone H3.3 on viral
CC       chromatin allowing viral transcription. May also play a role in virus
CC       entry at attachment or membrane fusion steps.
CC       {ECO:0000269|PubMed:15927339, ECO:0000269|PubMed:16973549,
CC       ECO:0000269|PubMed:22102817, ECO:0000269|PubMed:25275136,
CC       ECO:0000269|PubMed:3035208}.
CC   -!- SUBUNIT: Interacts with host DAXX; this interaction disrupts the
CC       chromatin remodeling complex ATRX:DAXX and thus allows viral
CC       transcription. {ECO:0000269|PubMed:22102817,
CC       ECO:0000269|PubMed:25275136}.
CC   -!- INTERACTION:
CC       P03179; Q9UER7: DAXX; Xeno; NbExp=5; IntAct=EBI-9349301, EBI-77321;
CC   -!- SUBCELLULAR LOCATION: Virion tegument {ECO:0000269|PubMed:15534216}.
CC       Host nucleus {ECO:0000269|PubMed:22102817}. Note=Colocalizes with host
CC       DAXX at PML nuclear bodies. {ECO:0000269|PubMed:22102817}.
CC   -!- SIMILARITY: Belongs to the herpesviridae MTP family. {ECO:0000305}.
CC   -!- CAUTION: Controvertial experiments have localized MTP at the virion
CC       surface. {ECO:0000305}.
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DR   EMBL; M11924; AAA45899.1; -; Genomic_DNA.
DR   EMBL; V01555; CAA24862.1; -; Genomic_DNA.
DR   EMBL; AJ507799; CAD53384.1; -; Genomic_DNA.
DR   PIR; A03740; QQBE1.
DR   RefSeq; YP_401633.1; NC_007605.1.
DR   SMR; P03179; -.
DR   IntAct; P03179; 44.
DR   MINT; P03179; -.
DR   PRIDE; P03179; -.
DR   DNASU; 3783722; -.
DR   GeneID; 3783722; -.
DR   KEGG; vg:3783722; -.
DR   Proteomes; UP000153037; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019033; C:viral tegument; IEA:UniProtKB-SubCell.
DR   GO; GO:0075733; P:intracellular transport of virus; IEA:InterPro.
DR   Gene3D; 3.30.1330.10; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.90.650.10; -; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR010077; Herpes_virus_tegument.
DR   InterPro; IPR010918; PurM-like_C_dom.
DR   InterPro; IPR036676; PurM-like_C_sf.
DR   InterPro; IPR036921; PurM-like_N_sf.
DR   InterPro; IPR024346; Tegument_herpes_virus_N.
DR   Pfam; PF02769; AIRS_C; 1.
DR   Pfam; PF12818; Tegument_dsDNA; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   SUPFAM; SSF55326; SSF55326; 1.
DR   SUPFAM; SSF56042; SSF56042; 1.
DR   TIGRFAMs; TIGR01739; tegu_FGAM_synt; 1.
PE   1: Evidence at protein level;
KW   Host nucleus; Host-virus interaction; Late protein; Reference proteome;
KW   Virion; Virion tegument.
FT   CHAIN           1..1318
FT                   /note="Major tegument protein"
FT                   /id="PRO_0000116188"
SQ   SEQUENCE   1318 AA;  142844 MW;  58D1DC644EB84BE6 CRC64;
     MEERGRETQM PVARYGGPFI MVRLFGQDGE ANIQEERLYE LLSDPRSALG LDPGPLIAEN
     LLLVALRGTN NDPRPQRQER ARELALVGIL LGNGEQGEHL GTESALEASG NNYVYAYGPD
     WMARPSTWSA EIQQFLRLLG ATYVLRVEMG RQFGFEVHRS RPSFRQFQAI NHLVLFDNAL
     RKYDSGQVAA GFQRALLVAG PETADTRPDL RKLNEWVFGG RAAGGRQLAD ELKIVSALRD
     TYSGHLVLQP TETLDTWKVL SRDTRTAHSL EHGFIHAAGT IQANCPQLFM RRQHPGLFPF
     VNAIASSLGW YYQTATGPGA DARAAARRQQ AFQTRAAAEC HAKSGVPVVA GFYRTINATL
     KGGEGLQPTM FNGELGAIKH QALDTVRYDY GHYLIMLGPF QPWSGLTAPP CPYAESSWAQ
     AAVQTALELF SALYPAPCIS GYARPPGPSA VIEHLGSLVP KGGLLLFLSH LPDDVKDGLG
     EMGPARATGP GMQQFVSSYF LNPACSNVFI TVRQRGEKIN GRTVLQALGR ACDMAGCQHY
     VLGSTVPLGG LNFVNDLASP VSTAEMMDDF SPFFTVEFPP IQEEGASSPV PLDVDESMDI
     SPSYELPWLS LESCLTSILS HPTVGSKEHL VRHTDRVSGG RVAQQPGVGP LDLPLADYAF
     VAHSQVWTRP GGAPPLPYRT WDRMTEKLLV SAKPGGENVK VSGTVITLGE QGYKVSLDLR
     EGTRLAMAEA LLNAACAPIL DPEDVLLTLH LHLDPRRADN SAVMEAMTAA SDYARGLGVK
     LTFGSASCPE TGSSASNFMT VVASVSAPGE FSGPLITPVL QKTGSLLIAV RCGDGKIQGG
     SLFEQLFSDV ATTPRAPEAL SLKNLFRAVQ QLVKSGIVLS GHDISDGGLV TCLVEMALAG
     QRGVTITMPV ASDYLPEMFA EHPGLVFEVE ERSVGEVLQT LRSMNMYPAV LGRVGEQGPD
     QMFEVQHGPE TVLRQSLRLL LGTWSSFASE QYECLRPDRI NRSMHVSDYG YNEALAVSPL
     TGKNLSPRRL VTEPDPRCQV AVLCAPGTRG HESLLAAFTN AGCLCRRVFF REVRDNTFLD
     KYVGLAIGGV HGARDSALAG RATVALINRF PALRDAILKF LNRPDTFSVA LGELGVQVLA
     GLGAVGSTDN PPAPGVEVNV QRSPLILAPN ASGMFESRWL NISIPATTSS VMLRGLRGCV
     LPCWVQGSCL GLQFTNLGMP YVLQNAHQIA CHFHSNGTDA WRFAMNYPRN PTEQGNIAGL
     CSRDGRHLAL LCDPSLCTDF WQWEHIPPAF GHPTGCSPWT LMFQAAHLWS LRHGRPSE