ID   MCP_HHV7J               Reviewed;        1345 AA.
AC   P52347;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   02-DEC-2020, entry version 77.
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=U57;
OS   Human herpesvirus 7 (strain JI) (HHV-7) (Human T lymphotropic virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX   NCBI_TaxID=57278;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=8709220; DOI=10.1128/jvi.70.9.5975-5989.1996;
RA   Nicholas J.;
RT   "Determination and analysis of the complete nucleotide sequence of human
RT   herpesvirus.";
RL   J. Virol. 70:5975-5989(1996).
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; U43400; AAC54720.1; -; Genomic_DNA.
DR   PIR; T41960; T41960.
DR   RefSeq; YP_073799.1; NC_001716.2.
DR   SMR; P52347; -.
DR   GeneID; 3289517; -.
DR   KEGG; vg:3289517; -.
DR   Proteomes; UP000009246; 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   3: Inferred from homology;
KW   Capsid protein; Host nucleus; Reference proteome;
KW   T=16 icosahedral capsid protein; Virion.
FT   CHAIN           1..1345
FT                   /note="Major capsid protein"
FT                   /id="PRO_0000115706"
SQ   SEQUENCE   1345 AA;  152932 MW;  93F4D3FF9BF4977E CRC64;
     MENWRTAEIF PKLDVSPNVF DDIRTQTAEQ LFENLRLYYG DDSDRYNISF EALLGIYCNR
     TEWIDFFHTS IAVAANVIRF NDLDKMSLGK ILFYIQLPRV ATGNDVTAPK ETTVLVTKYS
     EKHPINISFE LSAACLAHLE NTFKNTILDQ MLNINAIHTV LRSLKNSADS LQRGLIYAFI
     KTILKKAPPQ FILKTMLENK VNSKQILSKV QRSNMFQNFK NKLINSLFFL NRTSNVSFIY
     RYLCEMVDST TESILNNTNS YVLKDGTPIN GVLLGTPNTI QILSNALSQH ISQMTMSVPV
     SYGTFVMGKE NAVTAIAYQA IMADFSNYTK NVATETQDQN KKSEIFENQT QHADLKTNII
     QLSDKTVVLD HLKKVYKNTN IEDPLEQKLE LTFFFPMGLY ISKDSGFSTM DSRLKLNDTM
     ENNLPTSIYF YNKDKLLQRI DYSDLLPSLC HPIIFDCSVS ERIFKNAAKP TGESFNQLCQ
     VEFVREPPST FLSNLYNLYE MKKEIPKTTN MLKNELTTED FYKSENFTLK TELHPFFDFT
     YIQKNRSTDV LCSPRILLGN IPLPLAPSSF HEARTNQMIE QAKTNNLNYD YTLKLVVESL
     TNTAYPELAY IIELLIHGNK TAFQILKDVV SQCITYWYNI KHILLFCNNF EMIWLITTYL
     GDESIPGIAY THYKNIISIL KLVKRTISIS NFNEQLCGEP LVGFVNALFD NRLFPPFLNS
     LPKNEANAII TAGNTPLTQN TVKLRNYEVS DLNRMNLLDS TEIFTDVDRP SFETIVLSKI
     FYFCFLPALT NNKMCGAGFD VKSFILDFFY TEPFILPDDN FCELPITNNV LIELITEAVG
     PSHALTDLSC IGKQLFKSIL YLTENTKILE IESSLDPSQR HGSSSNFKSL QHVLYNGLCL
     VSPINVLKRY FKPIPFNRFF SDPIICGLMN IEVQTYLNIF PHYQRNDGGF PLPQALSHEF
     HNWQRTPFFV YASCCSNSLL SIMTLATMHC KLSPIAIILQ SRQKIHPGFA ATLVRTDCFD
     INCLLYSSKS ATSIMIDDPT VSTEVKDIST TYNLTQHISF LDMGLGFSSS TAIANLKRVK
     TDMGSKVQDL FSVFPMHAYT NPTVNSWVRH HVGIEKPNPS ETDALNILSF GKINKQSQSI
     LLHGQQAICE VVITPVTSDI NFYKTPKNPR GRASCMMGVD PHNESEARKS LYDHSRVDSD
     AFVATTNPWA SQEGSLSDVL YNINHRDQLG YNPKSYSPNA VFFTDTEIFK TNKFMFKLIS
     DYSIKTKTCL DSDTDIQYSC SEGTDDVTHR PCQFLQIAFP IHCSSNQALL ESRSKNGMTQ
     LSETHFANFA IGECIPLQNI IESLL