ID   MCP_EHV2                Reviewed;        1381 AA.
AC   Q66628;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   23-FEB-2022, entry version 60.
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=25;
OS   Equine herpesvirus 2 (strain 86/87) (EHV-2).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Percavirus.
OX   NCBI_TaxID=82831;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=7783207; DOI=10.1006/jmbi.1995.0314;
RA   Telford E.A.R., Watson M.S., Aird H.C., Perry J., Davison A.J.;
RT   "The DNA sequence of equine herpesvirus 2.";
RL   J. Mol. Biol. 249:520-528(1995).
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; U20824; AAC13812.1; -; Genomic_DNA.
DR   PIR; S55619; S55619.
DR   RefSeq; NP_042621.1; NC_001650.2.
DR   SMR; Q66628; -.
DR   GeneID; 1461080; -.
DR   KEGG; vg:1461080; -.
DR   Proteomes; UP000007083; 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..1381
FT                   /note="Major capsid protein"
FT                   /id="PRO_0000406033"
SQ   SEQUENCE   1381 AA;  153203 MW;  D6CD6C9AEC555185 CRC64;
     MEPVAIENRP YPYFATEANL LKGIKESAAE GLFKSFQLLL GKDVRENGVK FEVLLGVYSN
     VIQYIKFLET SLAVGCINTE FKDLRRMTNG KIQFKINVPT IAHGDGRRPT KQRQYIVLKT
     ANKHHISTEM ELAVLDLEIL HSSQETALDV TEYIGAVKTI TSALQFGVDA LERGLVDTVL
     HVKLRSAPPM FIYKTLNDPT IVERGMKKTV KSDLVAMFKA HLVEHTFFLD KAQYASQSVQ
     YVMTMLSDMA ATVCNETVFK GIASYTTPSG EVVDGVLETT DNVMRKLLAM LGQSGNSIVG
     PASYASYVVR GDNLVTAVSY GRAMVAFDQF VSRLVDNPNA TPSSVEDDLN AISSAAGLGQ
     QNRMAIPSSV IRVGDKTIAV ESLQNMYTEA QVPFPLNRRL QYSYYFPVGL HMPKPKYSTS
     NVIRGAENPL YQPVEAWVVN KNNTLLRFDY TCALRSLCHP KVHNPNPCAG ALQAAFPEAP
     ERMEAHGLEY EQPPHMNAHR LMFDYYNGKN VAHVTHIARK TSMSTDDLLH PSAHELLKLE
     VHPLFDFYAV GAPGARGVAY RATHRGMVGN IPQSLAPAGF QECRGDQFET AACLSHVVDA
     ATIEVVQQSA FDPNYPVICY LIEAMVHGQE EKFVMNAQLI ALVIESYWTN TGRLAFVNSF
     HMIKFICQHL GGAAVSKEVY GLYRRIYGEI VALEQALVKV AGHDDINRRH VGEYTNSLLD
     PSLLPPFVYN NVFGAFFNRV DRHAEVHVGN YAVDSYNDMA GILNVTDRME DLVGRFVNLY
     NNRVDDDHEH RFQLDVGVFR DAENILVLEK IFYYVFLPVC TNGHVCGMGV DFNNLALALA
     YNGPVYAPAV NGADPILDHL ENGTLRDLLQ ASDVAPTVDM IRTLATSFLT CPVNTQHARV
     KTRRDPGQAV ATHERAKLVG QTLLVNGFAA FAISERNRPA CETMFFPVPF HKFYSDPMVA
     ATLQPMIADY VNQIPSQRDV LAFNVPPTIM AEYEEWHKSP MAQYARSCAP TPLSLSTMVC
     MHNKLSPVAF VNQAKNRIHP GFALTVVRTD EVLSENILYS SRASTSVFVG LPSVTRKEVR
     SDAVTFEIHH ELATLNTSLG YSSILVPAHV ASITTDMGVH CQDLFAMYPG EQFADREMHN
     YLKKKVGAAQ GQHNGPDARH LLNAGFACHG PPGLSHGQLA TCEVILTPVT ADVSYFQSSN
     SPRGRASCVV SCEPYNAESA ENFIYNHSLS DPAYEFRATV NPWASQLGSL GDVMYNASYK
     QMMAPGLYSP CRQFFNKEDL LKNNRGLYGL VNEYITRLGG APATSGTDLQ FVVINGTDVF
     LEQPCLFLQE AFPTLSASHR ALIDEYMSYK QTHAPVHFNQ HLIEEVAPVK RLFKQGNKLV
     Y