ID   MCP_SUHVS               Reviewed;        1330 AA.
AC   Q00705;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, 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};
OS   Suid herpesvirus 1 (strain Indiana S) (SuHV-1) (Pseudorabies virus (strain
OS   Indiana S)).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=31522;
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1718089; DOI=10.1016/0042-6822(91)90753-x;
RA   Yamada S., Imada T., Watanabe W., Honda Y., Nakajima-Iijima S., Shimizu Y.,
RA   Sekikawa K.;
RT   "Nucleotide sequence and transcriptional mapping of the major capsid
RT   protein gene of pseudorabies virus.";
RL   Virology 185:56-66(1991).
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   PIR; A40777; VCBES5.
DR   SMR; Q00705; -.
DR   DIP; DIP-62100N; -.
DR   PRIDE; Q00705; -.
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; T=16 icosahedral capsid protein; Virion.
FT   CHAIN           1..1330
FT                   /note="Major capsid protein"
FT                   /id="PRO_0000115708"
SQ   SEQUENCE   1330 AA;  145938 MW;  4E228145F773A522 CRC64;
     MERPAILPSG QILSNIEVHS HRALFDIFKR FRSDDNNLYG AEFDALLGTY CSTLSLVRFL
     ELGLSVACVC TKFPELSYVA EGTIQFEVQQ PMIARDGPHP ADQPVHNYMI KRLDRRSLNA
     AFSIAVEALG LISGENLDGT HISSAMRLRA IQQLARNVQA VLDSFERGTA DQMLRVLMEK
     APPLSLLAPF TLYEGRLADR VACAALVSEL KRRVRDDTFF LTKHERNKDA VLDRLSDLVN
     CTAPSVAVAR MTHADTQGRP VDGVLVTTAG VRQRLLHHVL TLADTHADVP VTYGEMVIAN
     TNLVTALVMG KAVSNMDDVA RYLLGGEPAP DDGKPVGSAR VRADLVVVGD RLVFLEALEK
     RVYQATQVPY PLVGNLDVTF VMPLGVFKPA ADRYARHAGS FAPTPGLPDP RTHPPRAVHF
     FNKDGVPCHV TFEHAMGTLC HPSFLDVDAT LAALRQEPAE VQCAFGAYVA DARPDALVGL
     MQRFLEEWPG MMPVRPRWAA PAAADQLLAP GNADLRLELH PAFDFFVAPE VDVPGPFAVP
     QVMGQVRAMP RIINGNIPLA LCPVDFRDAR GFELSVDRHR LAPATVAAVR GAFRDANYPM
     VFYIIEAVIH GSERTFCALA RLVAQCIQSY WRNTHNAAFV NNFYMVMYIN TYLGNGELPE
     DCAAVYKDLL EHVHALRRLI GEFTLPGDPL GNQPQEELNH ALADATLLPP LIWDCDPILY
     RDGLAERLPE LRVNGAHFQH ILWVEMAQVN FRNVGGGLVH NRPVRNENQP LHPHHDAEWS
     VLSKIYYYAV VPAFSRGNCC TMGVRYDRVY QLVQTMVVPE TDEEVGTDDP RHPLHPRNLV
     PNSLNVLFHN ACVAVDADAM LILQETVTNM AERTTPLLAS VAPDAGMATV ATRDMRTHDG
     SLHHGLLMMA YQPNDATLLE GAFFYPAPVN ALFACADHLG AMRDVGAEVR AAAQHVPCVP
     HFLGANYYAT VRQPVAQHAA QSRADENTLS YALMAGYFKM SPVAFTHQLR RQLHPGFALT
     VVRQDRFATE NVLFAEKASE SYFMGQMQVA RTESGGGLHL QLTQPRANVD LGVGFTAAYA
     AAALRAPVTD MGNLPQNLFA TRGAPPMLDA DADDYLRRTV NAGNRLAPVP VFGQMLPQVP
     AGLARGQQSV CEFIATPVSV DLAYFRRACN PRGRAAGEVH GEEGLMFDHS HADPAHPHRA
     TANPWASQRH SYADRLYNGQ YNMSGPAYSP CFKFFTPAEA VAKSRGLARL IADTGAAASP
     TSNGEYQFKR PVGAGELVED PCALFQEAYP PLCASDSALL RTPLGAEEHF AQYLIRDESP
     LKGCFQHASA