ID   MCP_SHV21               Reviewed;        1371 AA.
AC   Q00999;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   23-FEB-2022, entry version 66.
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   Saimiriine herpesvirus 2 (strain 11) (SaHV-2) (Herpesvirus saimiri).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX   NCBI_TaxID=10383;
OH   NCBI_TaxID=9521; Saimiri sciureus (Common squirrel monkey).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=1321287; DOI=10.1128/jvi.66.8.5047-5058.1992;
RA   Albrecht J.-C., Nicholas J., Biller D., Cameron K.R., Biesinger B.,
RA   Newman C., Wittmann S., Craxton M.A., Coleman H., Fleckenstein B.,
RA   Honess R.W.;
RT   "Primary structure of the herpesvirus saimiri genome.";
RL   J. Virol. 66:5047-5058(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; X64346; CAA45648.1; -; Genomic_DNA.
DR   RefSeq; NP_040227.1; NC_001350.1.
DR   SMR; Q00999; -.
DR   GeneID; 1682518; -.
DR   KEGG; vg:1682518; -.
DR   Proteomes; UP000000587; 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..1371
FT                   /note="Major capsid protein"
FT                   /id="PRO_0000115709"
SQ   SEQUENCE   1371 AA;  154355 MW;  5F99FA9553A201C1 CRC64;
     MEVENRPYPY MVSDANLLQQ IKESSAEGLF KSFSLLLGKD VRESGVKFEA LLGVYTNATQ
     FVKFLETSLA VSCVNTEFKD LKRMTDGKIQ FKINVPTIAH GDGRRPQKQK QFIIMKATNK
     HHIGAEIELS TQDLELLFLS KETPLDVTEY VGAVKTITSA LQFGIDALER GLIDTVLTVK
     LRHAPPLFIL KTLADPTYTE RGLKKNVKSD LISMFKTHLV NNSFFLDKSE HLPHSRQYVL
     GILTEMIGAV CKETVFKGIS TYSTANGQPI SGVLETTDKV MRKLVNVIGQ ADNSIMGPAA
     YANYVVRGEN LVTAISYGKA MRNFDHFMSK LVDNPTSNLD NDAVDTFEST GSIQKTPIST
     SVVMVGNKLI ALESLQRMYN ETQLPYPLNR RMHYTYYFPV GLHLPSPKYS TSMSVKGTEN
     VLHQSVEAWI VNKNNTLQCF NYQNALKSIC HPRMNSPILC ARALGEAFPD VHNLNIYGIR
     SEDAHTMNLY QIVYDYYDNK HVAHVHSLAQ KSMMTHEEVL HPTNHEILRT EVHPFFDVYA
     ERHQGAAVQY RATHRNLSGN LPPPLAPYSF QECRGYQFEV ASGLNHVIDS TTMEIIQETA
     FDPAYPLLCY IVESMIHGQE EKFVMNIPLI ALCIQTYWNN SGRLAFINSF YMLKFICTHM
     GNGHISKDAY SCYRKIYGEL IAIEQSLYRL AGHENVANEN IGQLINAILD KDLLPPFAYN
     DIFTNLLRKS SRHPVVKIGM EEYDDDNDQQ NCINIREKME DLVGNMVNIY QQRNNTDHSR
     RYVLDVGELQ ENTYNSVLEK IFYYVLLPVC TNGHVCGMGV DFENVALTLT YNGPVFASAV
     NQDADILDHL ENGTLRDVLV ASEIRPTVGM IRRLCTSFLT CPFITQAARI KTDRDPGQNI
     VTHTDGKYVH QTVLVNGFAA FAIADKSRDA AHCLFYPVPF NKLYCDPMVA ATLHPIVAEF
     ITEIPSQRNA VVFNLPPRLI AEYEEWHKSP MSSYVSTCSQ TPLSLSTMIA MHLKLSPVSF
     ICQSRHKIHP GFALTAVRTD EVVAEHIMYS SKASTSVFIG QPTVHRKEVR SDAVVFDINH
     ELASLDTALG YSSTIVPAHA AAITTDMGIH CQDLFAMFPS EAYSNQQLNE YIKQKIGSDR
     VYGMPLRDPR EYMGGNRRVT LPGLSHGQLA TCEVIMTPVT ADITYFQSSN SPRGRASCVV
     SCDAYNNESA EKFLYDHSLP DPCYEFRSTI NPWASQIGSL GDVFFNSQHR QMAGPTLYSP
     CKQFFNKEAI LKNNKLFYTL VTEYVNRLTG APATSNTDFQ YVVINGTDVF LEQPCQFLQE
     AYPTLSASHR ALLDEYMSHK TTHAPVHVNQ YLVEEVAPMK RLLKVGNKTV Y