ID   MCP_HCMVM               Reviewed;        1370 AA.
AC   F5HGT1;
DT   11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   23-FEB-2022, entry version 30.
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}; Synonyms=UL86;
OS   Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX   NCBI_TaxID=295027;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15105547; DOI=10.1099/vir.0.79888-0;
RA   Dolan A., Cunningham C., Hector R.D., Hassan-Walker A.F., Lee L.,
RA   Addison C., Dargan D.J., McGeoch D.J., Gatherer D., Emery V.C.,
RA   Griffiths P.D., Sinzger C., McSharry B.P., Wilkinson G.W.G., Davison A.J.;
RT   "Genetic content of wild-type human cytomegalovirus.";
RL   J. Gen. Virol. 85:1301-1312(2004).
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   -!- 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; AY446894; AAR31638.1; -; Genomic_DNA.
DR   RefSeq; YP_081534.1; NC_006273.2.
DR   SMR; F5HGT1; -.
DR   PRIDE; F5HGT1; -.
DR   GeneID; 3077538; -.
DR   KEGG; vg:3077538; -.
DR   Reactome; R-HSA-9609690; HCMV Early Events.
DR   Reactome; R-HSA-9610379; HCMV Late Events.
DR   Proteomes; UP000000938; 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:0019028; C:viral capsid; TAS:Reactome.
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   3: Inferred from homology;
KW   Capsid protein; Host nucleus; Reference proteome;
KW   T=16 icosahedral capsid protein; Virion.
FT   CHAIN           1..1370
FT                   /note="Major capsid protein"
FT                   /id="PRO_0000418237"
SQ   SEQUENCE   1370 AA;  153872 MW;  5EEFCEE4D7498E8D CRC64;
     MENWSALELL PKVGIPTDFL THVKTSAGEE MFEALRIYYG DDPERYNIHF EAIFGTFCNR
     LEWVYFLTSG LAAAAHAIKF HDLNKLTTGK MLFHVQVPRV ASGAGLPTSR QTTIMVTKYS
     EKSPITIPFE LSAACLTYLR ETFEGTILDK ILNVEAMHTV LRALKNTADA MERGLIHSFL
     QTLLRKAPPY FVVQTLVENA TLARQALNRI QRSNILQSFK AKMLATLFLL NRTRDRDYVL
     KFLTRLAEAA TDSILDNPTT YTTSSGAKIS GVMVSTANVM QIIMSLLSSH ITKETVSAPA
     TYGNFVLSPE NAVTAISYHS ILADFNSYKA HLTSGQPHLP NDSLSQAGAH SLTPLSMDVI
     RLGEKTVIME NLRRVYKNTD TKDPLERNVD LTFFFPVGLY LPEDRGYTTV ESKVKLNDTV
     RNALPTTAYL LNRDRAVQKI DFVDALKTLC HPVLHEPAPC LQTFTERGPP SEPAMQRLLE
     CRFQQEPMGG AARRIPHFYR VRREVPRTVN EMKQDFVVTD FYKVGNITLY TELHPFFDFT
     HCQENSETVA LCTPRIVIGN LPDGLAPGPF HELRTWEIME HMRLRPPPDY EETLRLFKTT
     VTSPNYPELC YLVDVLVHGN VDAFLLIRTF VARCIVNMFH TRQLLVFAHS YALVTLIAEH
     LADGALPPQL LFHYRNLVAV LRLVTRISAL PGLNNGQLAE EPLSAYVNAL HDHRLWPPFV
     THLPRNMEGV QVVADRQPLN PANIEARHHG VSDVPRLGAM DADEPLFVDD YRATDDEWTL
     QKVFYLCLMP AMTNNRACGL GLNLKTLLVD LFYRPAFLLM PAATAVSTSG TTSKESTSGV
     TPEDSIAAQR QAVGEMLTEL VEDVATDAHT PLLQACRELF LAVQFVGEHV KVLEVRAPLD
     HAQRQGLPDF ISRQHVLYNG CCVVTAPKTL IEYSLPVPFH RFYSNPTICA ALSDDIKRYV
     TEFPHYHRHD GGFPLPTAFA HEYHNWLRSP FSRYSATCPN VLHSVMTLAA MLYKISPVSL
     VLQTKAHIHP GFALTAVRTD TFEVDMLLYS GKSCTSVIIN NPIVTKEERD ISTTYHVTQN
     INTVDMGLGY TSNTCVAYVN RVRTDMGVRV QDLFRVFPMN VYRHDEVDRW IRHAAGVERP
     QLLDTETISM LTFGSMSERN AAATVHGQKA ACELILTPVT MDVNYFKIPN NPRGRASCML
     AVDPYDTEAA TKAIYDHREA DAQTFAATHN PWASQAGCLS DVLYNTRHRE RLGYNSKFYS
     PCAQYFNTEE IIAANKTLFK TIDEYLLRAK DCIRGDTDTQ YVCVEGTEQL IENPCRLTQE
     ALPILSTTTL ALMETKLKGG AGAFATSETH FGNYVVGEII PLQQSMLFNS