ID   MCP_GAHVM               Reviewed;        1393 AA.
AC   Q9E6P8;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   23-FEB-2022, entry version 61.
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=MDV031;
OS   Gallid herpesvirus 2 (strain Chicken/Md5/ATCC VR-987) (GaHV-2) (Marek's
OS   disease herpesvirus type 1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Mardivirus.
OX   NCBI_TaxID=10389;
OH   NCBI_TaxID=9031; Gallus gallus (Chicken).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10933706; DOI=10.1128/jvi.74.17.7980-7988.2000;
RA   Tulman E.R., Afonso C.L., Lu Z., Zsak L., Rock D.L., Kutish G.F.;
RT   "The genome of a very virulent Marek's disease virus.";
RL   J. Virol. 74:7980-7988(2000).
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; AF243438; AAG14211.1; -; Genomic_DNA.
DR   RefSeq; YP_001033947.1; NC_002229.3.
DR   SMR; Q9E6P8; -.
DR   PRIDE; Q9E6P8; -.
DR   GeneID; 4811492; -.
DR   KEGG; vg:4811492; -.
DR   Proteomes; UP000008072; 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..1393
FT                   /note="Major capsid protein"
FT                   /id="PRO_0000406506"
SQ   SEQUENCE   1393 AA;  154849 MW;  3892D4C02D177836 CRC64;
     MAGCHCPPAG DCPPVAPCTF STPFNIGATL APTGRLLSTI EMSSHRCMFD YFKQFSSDDN
     GRYAAQFDLL LGTYCNTLSL IRFLETGLSV ACVCTRAPDL MYMREGTVQF EIQQPMIARE
     GPHPADQPIH TYMVKRLCRR SLSAAFVVAA EALALLSEVS LDGTAISTHL RMRAIQQLAR
     NVRTILDSFE RGTVDQMLRI LLEKAPPAPL LIPLSRSQAE GRIAGQVMRA NLVSELKRTV
     RTESFIMNKT NANRDTIISF LTKMVNCTHQ TISMPRLTHS DSKGRLVDGV LVTTTMVRQK
     LLSGILDVVD TSARVPVTYG EMIISGTNLV TAVVMGKAVR NMDDIARYIL NLKEDNIIDR
     TDEIVRGDDD RPQTAEISAE LVTIGDKLIF LESMERRVYQ ATQVQYPLIG HVDLTFIMPL
     GIYQKRGDRY ARHIGDYAPG PGCNVGDIRI FPPREIYFYN KDNQVISLSL SDAIGTLCHS
     SFLDVEATVG NLRNGKYTLS CVLGAYVTNP PALPLADASR QFFENIGEFL RDPPRWIDEC
     HMTVEQFLST GNPYLSMELH PAFDFFVVPG DVDLPGPHNV PQVMASISAS LRVCNCNIPL
     PLCNSDFRDA LGQELASTHH KMSDATINAV SATFSDISYP TAFYIIEAVI HGSERNFGLL
     MRLVIQCIRS YWDNCKRVAF VNNFHMVAFI DTYLCSGELP EECTNVYKDL MHHVRALRSI
     VRNYTVQTDP LYGQSHEELN HVLIDRTILP PLLWDCDPLI YQAEGMRDRD LYLNVGSENN
     YAVRPWLELQ DADFQRTGNV LIHNRPIRDA DRQTFVPHHA QEWTTLSKIY YYVMVPSFSR
     GQCCTMGIRF DNIYATSQSV IIPDLQPDEE PPLGPEDPRH PLNGRNLVPN TFNVMLHNAR
     ISVDADALLT LQETVNNMAE RTTAILYGST PDIGSSSSST RHMRTFDGAL HHGLLMMAYP
     CNDETVAAGT YFYPVPVNAL FACHDHLAAV RDLPGNSRTL LYRAPPVPPF LGANYYSTFR
     QPVAQYVKES RCGPNEISYA LMAGYFKLSP IGLYHQLRTG LHPGIAFTVI RQDRFLADMG
     LFAERASESY FLGQVSVTKR PHAGGVQFSL TQPRANVDLG VGYTATCTPL LLRNAITDMG
     NTVQSLHLTR GSPPLLHQEA DEFLRKVTTR GQRAAPQRTV PFLGTLMPNL PSGLEHGQMS
     ICEFIPTPVS ADLEYFRTPC NPRGRAAGAI HSGEEASDID DVMYDHQQGD PAYPFRATNN
     PWASQRLSYA DKLYNGVYNL SGASPLFSPT YKFFTPAEVC CKTRCLDKLI GEAGSALASF
     ASDGEVQFKR PIGSTELTED PCSLFQEAYP ILCATDKALL RAYSTGTTDN PETHLAQYLI
     RDASPIGGCL PIC