ID   MCP_HHV11               Reviewed;        1374 AA.
AC   P06491;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   24-JAN-2024, entry version 109.
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   Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Simplexvirus;
OC   Simplexvirus humanalpha1; Human herpesvirus 1.
OX   NCBI_TaxID=10299;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2839594; DOI=10.1099/0022-1317-69-7-1531;
RA   McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., McNab D.,
RA   Perry L.J., Scott J.E., Taylor P.;
RT   "The complete DNA sequence of the long unique region in the genome of
RT   herpes simplex virus type 1.";
RL   J. Gen. Virol. 69:1531-1574(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3020164; DOI=10.1099/0022-1317-67-10-2279;
RA   Davison B.A.J., Scott J.E.;
RT   "DNA sequence of the major capsid protein gene of herpes simplex virus type
RT   1.";
RL   J. Gen. Virol. 67:2279-2286(1986).
RN   [3]
RP   PROTEIN SEQUENCE OF 202-211 AND 607-616.
RX   PubMed=1328483; DOI=10.1099/0022-1317-73-10-2709;
RA   Davison M.D., Rixon F.J., Davison A.J.;
RT   "Identification of genes encoding two capsid proteins (VP24 and VP26) of
RT   herpes simplex virus type 1.";
RL   J. Gen. Virol. 73:2709-2713(1992).
RN   [4]
RP   FUNCTION.
RX   PubMed=8393939; DOI=10.1006/jmbi.1993.1406;
RA   Newcomb W.W., Trus B.L., Booy F.P., Steven A.C., Wall J.S., Brown J.C.;
RT   "Structure of the herpes simplex virus capsid. Molecular composition of the
RT   pentons and the triplexes.";
RL   J. Mol. Biol. 232:499-511(1993).
RN   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=8176370; DOI=10.1099/0022-1317-75-5-1091;
RA   Nicholson P., Addison C., Cross A.M., Kennard J., Preston V.G., Rixon F.J.;
RT   "Localization of the herpes simplex virus type 1 major capsid protein VP5
RT   to the cell nucleus requires the abundant scaffolding protein VP22a.";
RL   J. Gen. Virol. 75:1091-1099(1994).
RN   [6]
RP   INTERACTION WITH SCAFFOLD PROTEIN.
RX   PubMed=8523566; DOI=10.1128/jvi.70.1.533-540.1996;
RA   Hong Z., Beaudet-Miller M., Durkin J., Zhang R., Kwong A.D.;
RT   "Identification of a minimal hydrophobic domain in the herpes simplex virus
RT   type 1 scaffolding protein which is required for interaction with the major
RT   capsid protein.";
RL   J. Virol. 70:533-540(1996).
RN   [7]
RP   INTERACTION WITH TRX1/VP19C AND TRX2/VP23.
RX   PubMed=8811025; DOI=10.1099/0022-1317-77-9-2251;
RA   Rixon F.J., Addison C., McGregor A., Macnab S.J., Nicholson P.,
RA   Preston V.G., Tatman J.D.;
RT   "Multiple interactions control the intracellular localization of the herpes
RT   simplex virus type 1 capsid proteins.";
RL   J. Gen. Virol. 77:2251-2260(1996).
RN   [8]
RP   INTERACTION WITH CVC2/UL25.
RX   PubMed=11152516; DOI=10.1128/jvi.75.3.1427-1436.2001;
RA   Ogasawara M., Suzutani T., Yoshida I., Azuma M.;
RT   "Role of the UL25 gene product in packaging DNA into the herpes simplex
RT   virus capsid: location of UL25 product in the capsid and demonstration that
RT   it binds DNA.";
RL   J. Virol. 75:1427-1436(2001).
RN   [9]
RP   INTERACTION WITH SCP/VP26.
RC   STRAIN=KOS;
RX   PubMed=12477844; DOI=10.1128/jvi.77.1.391-404.2003;
RA   Desai P., Akpa J.C., Person S.;
RT   "Residues of VP26 of herpes simplex virus type 1 that are required for its
RT   interaction with capsids.";
RL   J. Virol. 77:391-404(2003).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 451-1054.
RX   PubMed=12574112; DOI=10.1093/emboj/cdg086;
RA   Bowman B.R., Baker M.L., Rixon F.J., Chiu W., Quiocho F.A.;
RT   "Structure of the herpesvirus major capsid protein.";
RL   EMBO J. 22:757-765(2003).
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, ECO:0000269|PubMed:8393939}.
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       ECO:0000269|PubMed:11152516, ECO:0000269|PubMed:12477844,
CC       ECO:0000269|PubMed:8523566, ECO:0000269|PubMed:8811025}.
CC   -!- INTERACTION:
CC       P06491; P10210: UL26; NbExp=3; IntAct=EBI-7608705, EBI-8621986;
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04016,
CC       ECO:0000269|PubMed:8176370}. Host nucleus {ECO:0000255|HAMAP-
CC       Rule:MF_04016, ECO:0000269|PubMed:8176370}.
CC   -!- SIMILARITY: Belongs to the herpesviridae major capsid protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04016}.
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DR   EMBL; X14112; CAA32332.1; -; Genomic_DNA.
DR   EMBL; X04467; CAA28154.1; -; Genomic_DNA.
DR   PIR; A27239; VCBE17.
DR   PDB; 1NO7; X-ray; 2.90 A; A/B=451-1054.
DR   PDBsum; 1NO7; -.
DR   SMR; P06491; -.
DR   BioGRID; 971410; 3.
DR   DIP; DIP-57212N; -.
DR   IntAct; P06491; 4.
DR   MINT; P06491; -.
DR   EvolutionaryTrace; P06491; -.
DR   Proteomes; UP000009294; 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; Major capsid protein VP5; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Capsid protein; Direct protein sequencing; Host nucleus;
KW   Reference proteome; T=16 icosahedral capsid protein; Virion.
FT   CHAIN           1..1374
FT                   /note="Major capsid protein"
FT                   /id="PRO_0000115702"
FT   HELIX           487..489
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   HELIX           498..506
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   HELIX           510..514
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   STRAND          548..550
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   STRAND          572..574
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   HELIX           579..581
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   TURN            584..586
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   HELIX           589..600
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   HELIX           608..619
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   HELIX           626..633
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   HELIX           638..643
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   HELIX           645..658
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   HELIX           668..676
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   HELIX           679..681
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   HELIX           684..706
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   HELIX           714..716
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   HELIX           719..723
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   STRAND          737..739
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   HELIX           740..746
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   TURN            750..752
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   STRAND          764..767
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   STRAND          771..773
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   STRAND          782..784
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   STRAND          789..793
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   STRAND          796..798
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   HELIX           803..814
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   HELIX           816..821
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   STRAND          826..830
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   HELIX           832..839
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   TURN            857..859
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   HELIX           867..869
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   HELIX           875..881
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   HELIX           888..892
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   HELIX           893..898
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   STRAND          907..912
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   STRAND          928..939
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   TURN            948..952
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   STRAND          953..957
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   HELIX           967..971
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   TURN            978..980
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   HELIX           981..984
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   HELIX           992..994
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   HELIX           997..999
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   STRAND          1000..1002
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   HELIX           1004..1012
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   HELIX           1017..1027
FT                   /evidence="ECO:0007829|PDB:1NO7"
FT   HELIX           1033..1042
FT                   /evidence="ECO:0007829|PDB:1NO7"
SQ   SEQUENCE   1374 AA;  149084 MW;  859C76E2EADE05B7 CRC64;
     MAAPNRDPPG YRYAAAMVPT GSLLSTIEVA SHRRLFDFFS RVRSDANSLY DVEFDALLGS
     YCNTLSLVRF LELGLSVACV CTKFPELAYM NEGRVQFEVH QPLIARDGPH PIEQPTHNYM
     TKIIDRRALN AAFSLATEAI ALLTGEALDG TGIGAHRQLR AIQQLARNVQ AVLGAFERGT
     ADQMLHVLLE KAPPLALLLP MQRYLDNGRL ATRVARATLV AELKRSFCET SFFLGKAGHR
     REAVEAWLVD LTTATQPSVA VPRLTHADTR GRPVDGVLVT TAPIKQRLLQ SFLKVEDTEA
     DVPVTYGEMV LNGANLVTAL VMGKAVRSLD DVGRHLLEMQ EEQLDLNRQT LDELESAPQT
     TRVRADLVSI GEKLVFLEAL EKRIYAATNV PYPLVGAMDL TFVLPLGLFN PVMERFAAHA
     GDLVPAPGHP DPRAFPPRQL FFWGKDRQVL RLSLEHAIGT VCHPSLMNVD AAVGGLNRDP
     VEAANPYGAY VAAPAGPAAD MQQLFLNAWG QRLAHGRVRW VAEGQMTPEQ FMQPDNANLA
     LELHPAFDFF VGVADVELPG GDVPPAGPGE IQATWRVVNG NLPLALCPAA FRDARGLELG
     VGRHAMAPAT IAAVRGAFDD RNYPAVFYLL QAAIHGSEHV FCALARLVVQ CITSYWNNTR
     CAAFVNDYSL VSYVVTYLGG DLPEECMAVY RDLVAHVEAL AQLVDDFTLT GPELGGQAQA
     ELNHLMRDPA LLPPLVWDCD ALMRRAALDR HRDCRVSAGG HDPVYAAACN VATADFNRND
     GQLLHNTQAR AADAADDRPH RGADWTVHHK IYYYVMVPAF SRGRCCTAGV RFDRVYATLQ
     NMVVPEIAPG EECPSDPVTD PAHPLHPANL VANTVNAMFH NGRVVVDGPA MLTLQVLAHN
     MAERTTALLC SAAPDAGANT ASTTNMRIFD GALHAGILLM APQHLDHTIQ NGDYFYPLPV
     HALFAGADHV ANAPNFPPAL RDLSRQVPLV PPALGANYFS SIRQPVVQHV RESAAGENAL
     TYALMAGYFK ISPVALHHQL KTGLHPGFGF TVVRQDRFVT ENVLFSERAS EAYFLGQLQV
     ARHETGGGVN FTLTQPRANV DLGVGYTAVV ATATVRNPVT DMGNLPQNFY LGRGAPPLLD
     NAAAVYLRNA VVAGNRLGPA QPVPVFGCAQ VPRRAGMDHG QDAVCEFIAT PVSTDVNYFR
     RPCNPRGRAA GGVYAGDKEG DVTALMYDHG QSDPSRAFAA TANPWASQRF SYGDLLYNGA
     YHLNGASPVL SPCFKFFTSA DIAAKHRCLE RLIVETGSAV STATAASDVQ FKRPPGCREL
     VEDPCGLFQE AYPLTCASDP ALLRSARNGE AHARETHFAQ YLVYDASPLK GLAL
//