MCP_HHV11
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 02-JUN-2021, entry version 106.
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; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
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 PRIDE; 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; SSF103417; 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
