ID   MCP_EHV1B               Reviewed;        1376 AA.
AC   P28920; Q6DLG8;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   23-FEB-2022, entry version 80.
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}; OrderedLocusNames=42;
OS   Equine herpesvirus 1 (strain Ab4p) (EHV-1) (Equine abortion virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=31520;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=1318606; DOI=10.1016/0042-6822(92)90706-u;
RA   Telford E.A.R., Watson M.S., McBride K., Davison A.J.;
RT   "The DNA sequence of equine herpesvirus-1.";
RL   Virology 189:304-316(1992).
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; AY665713; AAT67300.1; -; Genomic_DNA.
DR   PIR; H36799; VCBED6.
DR   RefSeq; YP_053088.1; NC_001491.2.
DR   SMR; P28920; -.
DR   GeneID; 1487526; -.
DR   KEGG; vg:1487526; -.
DR   Proteomes; UP000001189; 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..1376
FT                   /note="Major capsid protein"
FT                   /id="PRO_0000115703"
SQ   SEQUENCE   1376 AA;  152183 MW;  C3E866EFAE80AEDB CRC64;
     MDRRSEAFKI PVPEVIPAGQ ILSTIEVSSH RTLFDFFKQI RSDDNGLYAA QFDVLLGTYC
     NTLTLVRFLE LGLSVSCVCT KFPELNYVND GTIQFEVQQP MIARDGPHPV DQPTHTYMMK
     HIEQRSLSAA FAIAAEALGL IGGTTLDGTQ ISSSLRVRAI QQLARNVQTV LDSFERGTAD
     QLLRVLLEKA PPLTLLAPLQ IYRDEGRLAS RVNRAVLVSE LKRRVIEDTF FLTKHERNRK
     ELVVARLAEL VNCTAPSVAV TRMTHSDTKG RPVDGVVVTT AGVRQRLLQG ILTLEDMAAD
     VPVTYGEMMI TGTNLVTALV MGKAVRNLDD VAHHLLGMQR DQVRANEKLI KDYEDVPSTA
     RVRADLVLVG DRLVFLEALE KRVYQATNVP YPLVGNLDLT FIIPLGIFKP ATDRYSRHAG
     SFTPTPGQPD PRTYPPQTVY FFNKDGNLVQ LSFDSAAGTV CHSSFLDVDS VLVAIRREPH
     ELHCAFGAYV TLPPAGTLLD QMRRFFERWH MLMPARPRWT AEALMTIDQL LSPGNANLRL
     ELHPAFDFFV APADVVIPGP FDMPNVMPTV MAMPRLINGN IPLPLCPVEF RDSRGFELSV
     DRHRLNPATV LAVRGAFRDA NYPMVFYILE AVIHGSERTF CALARLIIQC IVSYWRNTHQ
     VAFVNNFYMI MYINAYLGNG ELPEECTAIY RDLLEHVQAL RRLVAEYTVP GEAVGGQGHD
     ALNNVLLDPA LLPPLIWDCD PILHRADMGR ARAQELWVDG VDYAAIPWVE MAEVNFGNTG
     GHLVHNRPIR GENKRNPIVP HHDPEWSVLS KIYYYAVVPA FSRGNCCTMG VRYDRVYPLV
     QTVVIPDLGA EEIAPTSPSD PRHPLNPRHL VPNTLNILFH NARVAVDTDA LLLLQEVVTN
     MAERTTPVLA TAAPDAGTAT AVTQEMRTFD GTLHHGILMM AYQRNDETLL EGTFFYPAPV
     NALFACPEHL GALPGLNAEV LEAARDVPPV PHFFGGNYYA TVRQPVAQHA VQSRADENTL
     TYALMAGYFK LGPIALSHQF ATGFHPGFAF TVVRQDRFLT ENILFAEKAS ESYFMGQLQV
     NRHEAVGGVN FVLTQPRANV DLGVGFTAAY AAAALRTPVT DMGNLPQNLY LTRGTIPMLD
     GDADAYLRRV VNTGNRLGPQ GPRPIFGQLM PATPAGVAHG QAAVCEFIVT PVSADLNYFR
     RPCNPRGRSA GPVYACDGEA DAVDVMYDHT QGDPAYPSRA TVNPWASQRN SYGDRLYNGK
     YNLNGASPVY SPCFKFFTPT EVEAKGRNMT QLIADVGASV APSTSNTEIQ FKRPHGSTDL
     VEDPCSLFQE AYPLLSSTDT ALLRTPHIGE IGADEGHFAQ YLIRDESPLK GCFPRI