ID   MCP_EBVA8               Reviewed;        1381 AA.
AC   P0C703; Q3KSQ5;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   23-FEB-2022, entry version 39.
DE   RecName: Full=Major capsid protein {ECO:0000255|HAMAP-Rule:MF_04016};
DE            Short=MCP {ECO:0000255|HAMAP-Rule:MF_04016};
GN   Name=MCP {ECO:0000255|HAMAP-Rule:MF_04016}; ORFNames=BcLF1;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Akata;
RA   Ahuja M.K., Hutt-Fletcher L.M.;
RL   Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Self-assembles to form an icosahedral capsid with a T=16
CC       symmetry, about 200 nm in diameter, and consisting of 150 hexons and 12
CC       pentons (total of 162 capsomers). Hexons form the edges and faces of
CC       the capsid and are each composed of six MCP molecules. In contrast, one
CC       penton is found at each of the 12 vertices. Eleven of the pentons are
CC       MCP pentamers, while the last vertex is occupied by the portal complex.
CC       The capsid is surrounded by a layer of proteinaceous material
CC       designated the tegument which, in turn, is enclosed in an envelope of
CC       host cell-derived lipids containing virus-encoded glycoproteins.
CC       {ECO:0000255|HAMAP-Rule:MF_04016}.
CC   -!- SUBUNIT: Homomultimer. Makes the hexons and eleven out of twelve
CC       pentons. Interacts with triplex proteins 1/TRX1 and 2/TRX2; adjacent
CC       capsomers are linked together in groups of three by triplexes,
CC       heterotrimeric complexes composed of one molecule of TRX1 and two
CC       molecules of TRX2. Interacts with scaffold protein; this interaction
CC       allows efficient MCP transport to the host nucleus. Interacts with
CC       capsid vertex component 2/CVC2. Interacts with the small capsomere-
CC       interacting protein/SCP. {ECO:0000255|HAMAP-Rule:MF_04016}.
CC   -!- INTERACTION:
CC       P0C703; P14348: SCP; Xeno; NbExp=2; IntAct=EBI-9645180, EBI-2620158;
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04016}. Host
CC       nucleus {ECO:0000255|HAMAP-Rule:MF_04016}.
CC   -!- SIMILARITY: Belongs to the herpesviridae major capsid protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04016}.
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DR   EMBL; DQ279927; ABB89273.1; -; Genomic_DNA.
DR   EMBL; FJ594486; ACL99814.1; -; Genomic_DNA.
DR   RefSeq; YP_001129493.1; NC_009334.1.
DR   SMR; P0C703; -.
DR   IntAct; P0C703; 4.
DR   MINT; P0C703; -.
DR   PRIDE; P0C703; -.
DR   GeneID; 5176226; -.
DR   KEGG; vg:5176226; -.
DR   Proteomes; UP000007639; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0039622; C:T=16 icosahedral viral capsid; IEA:UniProtKB-UniRule.
DR   GO; GO:0005198; F:structural molecule activity; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_04016; HSV_MCP; 1.
DR   InterPro; IPR000912; Herpes_MCP.
DR   InterPro; IPR023233; Herpes_MCP_upper_sf.
DR   Pfam; PF03122; Herpes_MCP; 1.
DR   PRINTS; PR00235; HSVCAPSIDMCP.
DR   SUPFAM; SSF103417; SSF103417; 1.
PE   1: Evidence at protein level;
KW   Capsid protein; Host nucleus; Reference proteome;
KW   T=16 icosahedral capsid protein; Virion.
FT   CHAIN           1..1381
FT                   /note="Major capsid protein"
FT                   /id="PRO_0000375971"
SQ   SEQUENCE   1381 AA;  153931 MW;  CF1901F68A06F5C5 CRC64;
     MASNEGVENR PFPYLTVDAD LLSNLRQSAA EGLFHSFDLL VGKDAREAGI KFEVLLGVYT
     NAIQYVRFLE TALAVSCVNT EFKDLSRMTD GKIQFRISVP TIAHGDGRRP SKQRTFIVVK
     NCHKHHISTE MELSMLDLEI LHSIPETPVE YAEYVGAVKT VASALQFGVD ALERGLINTV
     LSVKLRHAPP MFILQTLADP TFTERGFSKT VKSDLIAMFK RHLLEHSFFL DRAENMGSGF
     SQYVRSRLSE MVAAVSGESV LKGVSTYTTA KGGEPVGGVF IVTDNVLRQL LTFLGEEADN
     QIMGPSSYAS FVVRGENLVT AVSYGRVMRT FEHFMARIVD SPEKAGSTKS DLPAVAAGVE
     DQPRVPISAA VIKLGNHAVA VESLQKMYND TQSPYPLNRR MQYSYYFPVG LFMPNPKYTT
     SAAIKMLDNP TQQLPVEAWI VNKNNLLLAF NLQNALKVLC HPRLHTPAHT LNSLNAAPAP
     RDRRETYSLQ HRRPNHMNVL VIVDEFYDNK YAAPVTDIAL KCGLPTEDFL HPSNYDLLRL
     ELHPLYDIYI GRDAGERARH RAVHRLMVGN LPTPLAPAAF QEARGQQFET ATSLAHVVDQ
     AVIETVQDTA YDTAYPAFFY VVEAMIHGFE EKFVMNVPLV SLCINTYWER AGRLAFVNSF
     SMIKFICRHL GNNAISKEAY SMYRKIYGEL IALEQALMRL AGSDVVGDES VGQYVCALLD
     PNLLPPVAYT DIFTHLLTVS DRAPQIIIGN EVYADTLAAP QFIERVGNMD EMAAQFVALY
     GYRVNGDHDH DFRLHLGPYV DEGHADVLEK IFYYVFLPTC TNAHMCGLGV DFQHVAQTLA
     YNGPAFSHHF TRDEDILDNL ENGTLRDLLE ISDLRPTVGM IRDLSASFMT CPTFTRTVRV
     SVDNDVTQQL APNPADKRTE QTVLVNGLVA FAFSERTRAV TQCLFHAIPF HMFYGDPRVA
     ATMHQDVATF VMRNPQQRAV EAFNRPEQLF AEYREWHRSP MGKYAAECLP SLVSISGMTA
     MHIKMSPMAY IAQAKLKIHP GVAMTVVRTD EILSENILFS SRASTSMFIG TPNVSRREAR
     VDAVTFEVHH EMASIDTGLS YSSTMTPARV AAITTDMGIH TQDFFSVFPA EAFGNQQVND
     YIKAKVGAQR NGTLLRDPRT YLAGMTNVNG APGLCHGQQA TCEIIVTPVT ADVAYFQKSN
     SPRGRAACVV SCENYNQEVA EGLIYDHSRP DAAYEYRSTV NPWASQLGSL GDIMYNSSYR
     QTAVPGLYSP CRAFFNKEEL LRNNRGLYNM VNEYSQRLGG HPATSNTEVQ FVVIAGTDVF
     LEQPCSFLQE AFPALSASSR ALIDEFMSVK QTHAPIHYGH YIIEEVAPVR RILKFGNKVV
     F