ID   MCP_VZVD                Reviewed;        1396 AA.
AC   P09245;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   02-DEC-2020, entry version 72.
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=40;
OS   Varicella-zoster virus (strain Dumas) (HHV-3) (Human herpesvirus 3).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=10338;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=3018124; DOI=10.1099/0022-1317-67-9-1759;
RA   Davison A.J., Scott J.E.;
RT   "The complete DNA sequence of varicella-zoster virus.";
RL   J. Gen. Virol. 67:1759-1816(1986).
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; X04370; CAA27923.1; -; Genomic_DNA.
DR   PIR; E27341; VCBE40.
DR   SMR; P09245; -.
DR   PRIDE; P09245; -.
DR   Proteomes; UP000002602; 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..1396
FT                   /note="Major capsid protein"
FT                   /id="PRO_0000115707"
SQ   SEQUENCE   1396 AA;  154980 MW;  E509272D8D77242F CRC64;
     MTTVSCPANV ITTTESDRIA GLFNIPAGII PTGNVLSTIE VCAHRCIFDF FKQIRSDDNS
     LYSAQFDILL GTYCNTLNFV RFLELGLSVA CICTKFPELA YVRDGVIQFE VQQPMIARDG
     PHPVDQPVHN YMVKRIHKRS LSAAFAIASE ALSLLSNTYV DGTEIDSSLR IRAIQQMARN
     LRTVLDSFER GTADQLLGVL LEKAPPLSLL SPINKFQPEG HLNRVARAAL LSDLKRRVCA
     DMFFMTRHAR EPRLISAYLS DMVSCTQPSV MVSRITHTNT RGRQVDGVLV TTATLKRQLL
     QGILQIDDTA ADVPVTYGEM VLQGTNLVTA LVMGKAVRGM DDVARHLLDI TDPNTLNIPS
     IPPQSNSDST TAGLPVNARV PADLVIVGDK LVFLEALERR VYQATRVAYP LIGNIDITFI
     MPMGVFQANS MDRYTRHAGD FSTVSEQDPR QFPPQGIFFY NKDGILTQLT LRDAMGTICH
     SSLLDVEATL VALRQQHLDR QCYFGVYVAE GTEDTLDVQM GRFMETWADM MPHHPHWVNE
     HLTILQFIAP SNPRLRFELN PAFDFFVAPG DVDLPGPQRP PEAMPTVNAT LRIINGNIPV
     PLCPISFRDC RGTQLGLGRH TMTPATIKAV KDTFEDRAYP TIFYMLEAVI HGNERNFCAL
     LRLLTQCIRG YWEQSHRVAF VNNFHMLMYI TTYLGNGELP EVCINIYRDL LQHVRALRQT
     ITDFTIQGEG HNGETSEALN NILTDDTFIA PILWDCDALI YRDEAARDRL PAIRVSGRNG
     YQALHFVDMA GHNFQRRDNV LIHGRPVRGD TGQGIPITPH HDREWGILSK IYYYIVIPAF
     SRGSCCTMGV RYDRLYPALQ AVIVPEIPAD EEAPTTPEDP RHPLHAHQLV PNSLNVYFHN
     AHLTVDGDAL LTLQELMGDM AERTTAILVS SAPDAGAATA TTRNMRIYDG ALYHGLIMMA
     YQAYDETIAT GTFFYPVPVN PLFACPEHLA SLRGMTNARR VLAKMVPPIP PFLGANHHAT
     IRQPVAYHVT HSKSDFNTLT YSLLGGYFKF TPISLTHQLR TGFHPGIAFT VVRQDRFATE
     QLLYAERASE SYFVGQIQVH HHDAIGGVNF TLTQPRAHVD LGVGYTAVCA TAALRCPLTD
     MGNTAQNLFF SRGGVPMLHD NVTESLRRIT ASGGRLNPTE PLPIFGGLRP ATSAGIARGQ
     ASVCEFVAMP VSTDLQYFRT ACNPRGRASG MLYMGDRDAD IEAIMFDHTQ SDVAYTDRAT
     LNPWASQKHS YGDRLYNGTY NLTGASPIYS PCFKFFTPAE VNTNCNTLDR LLMEAKAVAS
     QSSTDTEYQF KRPPGSTEMT QDPCGLFQEA YPPLCSSDAA MLRTAHAGET GADEVHLAQY
     LIRDASPLRG CLPLPR