ID   MCP_HHV2H               Reviewed;        1374 AA.
AC   P89442;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   29-SEP-2021, 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=UL19;
OS   Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX   NCBI_TaxID=10315;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=1662697; DOI=10.1099/0022-1317-72-12-3057;
RA   McGeoch D.J., Cunningham C., McIntyre G., Dolan A.;
RT   "Comparative sequence analysis of the long repeat regions and adjoining
RT   parts of the long unique regions in the genomes of herpes simplex viruses
RT   types 1 and 2.";
RL   J. Gen. Virol. 72:3057-3075(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Z86099; CAB06743.1; -; Genomic_DNA.
DR   PDB; 6M6G; EM; 5.39 A; B/C/D/E/F/I=1-1374.
DR   PDB; 6M6H; EM; 4.50 A; A/B/C/D/E/F=1-1374.
DR   PDB; 6M6I; EM; 4.05 A; A/B/C/D/E/F=1-1374.
DR   PDBsum; 6M6G; -.
DR   PDBsum; 6M6H; -.
DR   PDBsum; 6M6I; -.
DR   SMR; P89442; -.
DR   PRIDE; P89442; -.
DR   Proteomes; UP000001874; 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   1: Evidence at protein level;
KW   3D-structure; Capsid protein; Host nucleus; Reference proteome;
KW   T=16 icosahedral capsid protein; Virion.
FT   CHAIN           1..1374
FT                   /note="Major capsid protein"
FT                   /id="PRO_0000406185"
SQ   SEQUENCE   1374 AA;  149238 MW;  ECEE85351E4C1939 CRC64;
     MAAPARDPPG YRYAAAILPT GSILSTIEVA SHRRLFDFFA AVRSDENSLY DVEFDALLGS
     YCNTLSLVRF LELGLSVACV CTKFPELAYM NEGRVQFEVH QPLIARDGPH PVEQPVHNYM
     TKVIDRRALN AAFSLATEAI ALLTGEALDG TGISLHRQLR AIQQLARNVQ AVLGAFERGT
     ADQMLHVLLE KAPPLALLLP MQRYLDNGRL ATRVARATLV AELKRSFCDT SFFLGKAGHR
     REAIEAWLVD LTTATQPSVA VPRLTHADTR GRPVDGVLVT TAAIKQRLLQ SFLKVEDTEA
     DVPVTYGEMV LNGANLVTAL VMGKAVRSLD DVGRHLLDMQ EEQLEANRET LDELESAPQT
     TRVRADLVAI GDRLVFLEAL ERRIYAATNV PYPLVGAMDL TFVLPLGLFN PAMERFAAHA
     GDLVPAPGHP EPRAFPPRQL FFWGKDHQVL RLSMENAVGT VCHPSLMNID AAVGGVNHDP
     VEAANPYGAY VAAPAGPGAD MQQRFLNAWR QRLAHGRVRW VAECQMTAEQ FMQPDNANLA
     LELHPAFDFF AGVADVELPG GEVPPAGPGA IQATWRVVNG NLPLALCPVA FRDARGLELG
     VGRHAMAPAT IAAVRGAFED RSYPAVFYLL QAAIHGNEHV FCALARLVTQ CITSYWNNTR
     CAAFVNDYSL VSYIVTYLGG DLPEECMAVY RDLVAHVEAL AQLVDDFTLP GPELGGQAQA
     ELNHLMRDPA LLPPLVWDCD GLMRHAALDR HRDCRIDAGG HEPVYAAACN VATADFNRND
     GRLLHNTQAR AADAADDRPH RPADWTVHHK IYYYVLVPAF SRGRCCTAGV RFDRVYATLQ
     NMVVPEIAPG EECPSDPVTD PAHPLHPANL VANTVKRMFH NGRVVVDGPA MLTLQVLAHN
     MAERTTALLC SAAPDAGANT ASTANMRIFD GALHAGVLLM APQHLDHTIQ NGEYFYVLPV
     HALFAGADHV ANAPNFPPAL RDLARDVPLV PPALGANYFS SIRQPVVQHA RESAAGENAL
     TYALMAGYFK MSPVALYHQL KTGLHPGFGF TVVRQDRFVT ENVLFSERAS EAYFLGQLQV
     ARHETGGGVN FTLTQPRGNV DLGVGYTAVA ATGTVRNPVT DMGNLPQNFY LGRGAPPLLD
     NAAAVYLRNA VVAGNRLGPA QPLPVFGCAQ VPRRAGMDHG QDAVCEFIAT PVATDINYFR
     RPCNPRGRAA GGVYAGDKEG DVIALMYDHG QSDPARPFAA TANPWASQRF SYGDLLYNGA
     YHLNGASPVL SPCFKFFTAA DITAKHRCLE RLIVETGSAV STATAASDVQ FKRPPGCREL
     VEDPCGLFQE AYPITCASDP ALLRSARDGE AHARETHFTQ YLIYDASPLK GLSL