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P06491

- MCP_HHV11

UniProt

P06491 - MCP_HHV11

Protein

Major capsid protein

Gene

UL19

Organism
Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 1 (01 Jan 1988)
      Previous versions | rss
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    Functioni

    Self-assembles to form an icosahedral capsid with a T=16 symmetry, about 200 nm in diameter, and consisting of 150 hexons and 12 pentons (total of 162 capsomers). Hexons form the edges and faces of the capsid and are each composed of six MCP molecules. In contrast, one penton is found at each of the 12 vertices. Eleven of the pentons are MCP pentamers, while the last vertex is occupied by the portal complex. The capsid is surrounded by a layer of proteinaceous material designated the tegument which, in turn, is enclosed in an envelope of host cell-derived lipids containing virus-encoded glycoproteins.1 Publication

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. structural molecule activity Source: InterPro

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Major capsid protein
    Short name:
    MCP
    Alternative name(s):
    Capsid protein VP5
    Gene namesi
    Name:UL19
    OrganismiHuman herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
    Taxonomic identifieri10299 [NCBI]
    Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeSimplexvirus
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000009294: Genome

    Subcellular locationi

    Virion 1 Publication. Host nucleus 1 Publication

    GO - Cellular componenti

    1. host cell nucleus Source: UniProtKB-SubCell
    2. T=16 icosahedral viral capsid Source: UniProtKB-KW

    Keywords - Cellular componenti

    Capsid protein, Host nucleus, T=16 icosahedral capsid protein, Virion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13741374Major capsid proteinPRO_0000115702Add
    BLAST

    Interactioni

    Subunit structurei

    Homomultimer. Makes the hexons and eleven out of twelve pentons. Interacts with VP19C and VP23; Adjacent capsomers are linked together in groups of three by triplexes, heterotrimeric complexes composed of one molecule of VP19C and two molecules of VP23. Interacts with VP22A; this interaction allows efficient MCP transport to the host nucleus. Interacts with VP26. Interacts with virion-packaging protein UL25.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    UL26P102103EBI-7608705,EBI-8621986

    Protein-protein interaction databases

    IntActiP06491. 4 interactions.
    MINTiMINT-6732551.

    Structurei

    Secondary structure

    1
    1374
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi487 – 4893
    Helixi498 – 5069
    Helixi510 – 5145
    Beta strandi548 – 5503
    Beta strandi572 – 5743
    Helixi579 – 5813
    Turni584 – 5863
    Helixi589 – 60012
    Helixi608 – 61912
    Helixi626 – 6338
    Helixi638 – 6436
    Helixi645 – 65814
    Helixi668 – 6769
    Helixi679 – 6813
    Helixi684 – 70623
    Helixi714 – 7163
    Helixi719 – 7235
    Beta strandi737 – 7393
    Helixi740 – 7467
    Turni750 – 7523
    Beta strandi764 – 7674
    Beta strandi771 – 7733
    Beta strandi782 – 7843
    Beta strandi789 – 7935
    Beta strandi796 – 7983
    Helixi803 – 81412
    Helixi816 – 8216
    Beta strandi826 – 8305
    Helixi832 – 8398
    Turni857 – 8593
    Helixi867 – 8693
    Helixi875 – 8817
    Helixi888 – 8925
    Helixi893 – 8986
    Beta strandi907 – 9126
    Beta strandi928 – 93912
    Turni948 – 9525
    Beta strandi953 – 9575
    Helixi967 – 9715
    Turni978 – 9803
    Helixi981 – 9844
    Helixi992 – 9943
    Helixi997 – 9993
    Beta strandi1000 – 10023
    Helixi1004 – 10129
    Helixi1017 – 102711
    Helixi1033 – 104210

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NO7X-ray2.90A/B451-1054[»]
    ProteinModelPortaliP06491.
    SMRiP06491. Positions 484-1045.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06491.

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    InterProiIPR000912. Herpes_MCP.
    IPR023233. Herpes_MCP_upper.
    [Graphical view]
    PfamiPF03122. Herpes_MCP. 1 hit.
    [Graphical view]
    PRINTSiPR00235. HSVCAPSIDMCP.
    SUPFAMiSSF103417. SSF103417. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P06491-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAPNRDPPG YRYAAAMVPT GSLLSTIEVA SHRRLFDFFS RVRSDANSLY     50
    DVEFDALLGS YCNTLSLVRF LELGLSVACV CTKFPELAYM NEGRVQFEVH 100
    QPLIARDGPH PIEQPTHNYM TKIIDRRALN AAFSLATEAI ALLTGEALDG 150
    TGIGAHRQLR AIQQLARNVQ AVLGAFERGT ADQMLHVLLE KAPPLALLLP 200
    MQRYLDNGRL ATRVARATLV AELKRSFCET SFFLGKAGHR REAVEAWLVD 250
    LTTATQPSVA VPRLTHADTR GRPVDGVLVT TAPIKQRLLQ SFLKVEDTEA 300
    DVPVTYGEMV LNGANLVTAL VMGKAVRSLD DVGRHLLEMQ EEQLDLNRQT 350
    LDELESAPQT TRVRADLVSI GEKLVFLEAL EKRIYAATNV PYPLVGAMDL 400
    TFVLPLGLFN PVMERFAAHA GDLVPAPGHP DPRAFPPRQL FFWGKDRQVL 450
    RLSLEHAIGT VCHPSLMNVD AAVGGLNRDP VEAANPYGAY VAAPAGPAAD 500
    MQQLFLNAWG QRLAHGRVRW VAEGQMTPEQ FMQPDNANLA LELHPAFDFF 550
    VGVADVELPG GDVPPAGPGE IQATWRVVNG NLPLALCPAA FRDARGLELG 600
    VGRHAMAPAT IAAVRGAFDD RNYPAVFYLL QAAIHGSEHV FCALARLVVQ 650
    CITSYWNNTR CAAFVNDYSL VSYVVTYLGG DLPEECMAVY RDLVAHVEAL 700
    AQLVDDFTLT GPELGGQAQA ELNHLMRDPA LLPPLVWDCD ALMRRAALDR 750
    HRDCRVSAGG HDPVYAAACN VATADFNRND GQLLHNTQAR AADAADDRPH 800
    RGADWTVHHK IYYYVMVPAF SRGRCCTAGV RFDRVYATLQ NMVVPEIAPG 850
    EECPSDPVTD PAHPLHPANL VANTVNAMFH NGRVVVDGPA MLTLQVLAHN 900
    MAERTTALLC SAAPDAGANT ASTTNMRIFD GALHAGILLM APQHLDHTIQ 950
    NGDYFYPLPV HALFAGADHV ANAPNFPPAL RDLSRQVPLV PPALGANYFS 1000
    SIRQPVVQHV RESAAGENAL TYALMAGYFK ISPVALHHQL KTGLHPGFGF 1050
    TVVRQDRFVT ENVLFSERAS EAYFLGQLQV ARHETGGGVN FTLTQPRANV 1100
    DLGVGYTAVV ATATVRNPVT DMGNLPQNFY LGRGAPPLLD NAAAVYLRNA 1150
    VVAGNRLGPA QPVPVFGCAQ VPRRAGMDHG QDAVCEFIAT PVSTDVNYFR 1200
    RPCNPRGRAA GGVYAGDKEG DVTALMYDHG QSDPSRAFAA TANPWASQRF 1250
    SYGDLLYNGA YHLNGASPVL SPCFKFFTSA DIAAKHRCLE RLIVETGSAV 1300
    STATAASDVQ FKRPPGCREL VEDPCGLFQE AYPLTCASDP ALLRSARNGE 1350
    AHARETHFAQ YLVYDASPLK GLAL 1374
    Length:1,374
    Mass (Da):149,084
    Last modified:January 1, 1988 - v1
    Checksum:i859C76E2EADE05B7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14112 Genomic DNA. Translation: CAA32332.1.
    X04467 Genomic DNA. Translation: CAA28154.1.
    PIRiA27239. VCBE17.
    RefSeqiNP_044620.1. NC_001806.1.

    Genome annotation databases

    GeneIDi2703368.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14112 Genomic DNA. Translation: CAA32332.1 .
    X04467 Genomic DNA. Translation: CAA28154.1 .
    PIRi A27239. VCBE17.
    RefSeqi NP_044620.1. NC_001806.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1NO7 X-ray 2.90 A/B 451-1054 [» ]
    ProteinModelPortali P06491.
    SMRi P06491. Positions 484-1045.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P06491. 4 interactions.
    MINTi MINT-6732551.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 2703368.

    Miscellaneous databases

    EvolutionaryTracei P06491.

    Family and domain databases

    InterProi IPR000912. Herpes_MCP.
    IPR023233. Herpes_MCP_upper.
    [Graphical view ]
    Pfami PF03122. Herpes_MCP. 1 hit.
    [Graphical view ]
    PRINTSi PR00235. HSVCAPSIDMCP.
    SUPFAMi SSF103417. SSF103417. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The complete DNA sequence of the long unique region in the genome of herpes simplex virus type 1."
      McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., McNab D., Perry L.J., Scott J.E., Taylor P.
      J. Gen. Virol. 69:1531-1574(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "DNA sequence of the major capsid protein gene of herpes simplex virus type 1."
      Davison B.A.J., Scott J.E.
      J. Gen. Virol. 67:2279-2286(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Identification of genes encoding two capsid proteins (VP24 and VP26) of herpes simplex virus type 1."
      Davison M.D., Rixon F.J., Davison A.J.
      J. Gen. Virol. 73:2709-2713(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 202-211 AND 607-616.
    4. "Structure of the herpes simplex virus capsid. Molecular composition of the pentons and the triplexes."
      Newcomb W.W., Trus B.L., Booy F.P., Steven A.C., Wall J.S., Brown J.C.
      J. Mol. Biol. 232:499-511(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "Localization of the herpes simplex virus type 1 major capsid protein VP5 to the cell nucleus requires the abundant scaffolding protein VP22a."
      Nicholson P., Addison C., Cross A.M., Kennard J., Preston V.G., Rixon F.J.
      J. Gen. Virol. 75:1091-1099(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    6. "Identification of a minimal hydrophobic domain in the herpes simplex virus type 1 scaffolding protein which is required for interaction with the major capsid protein."
      Hong Z., Beaudet-Miller M., Durkin J., Zhang R., Kwong A.D.
      J. Virol. 70:533-540(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VP22A.
    7. "Multiple interactions control the intracellular localization of the herpes simplex virus type 1 capsid proteins."
      Rixon F.J., Addison C., McGregor A., Macnab S.J., Nicholson P., Preston V.G., Tatman J.D.
      J. Gen. Virol. 77:2251-2260(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VP19C AND VP23.
    8. "Role of the UL25 gene product in packaging DNA into the herpes simplex virus capsid: location of UL25 product in the capsid and demonstration that it binds DNA."
      Ogasawara M., Suzutani T., Yoshida I., Azuma M.
      J. Virol. 75:1427-1436(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UL25.
    9. "Residues of VP26 of herpes simplex virus type 1 that are required for its interaction with capsids."
      Desai P., Akpa J.C., Person S.
      J. Virol. 77:391-404(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VP26.
      Strain: KOS.
    10. "Structure of the herpesvirus major capsid protein."
      Bowman B.R., Baker M.L., Rixon F.J., Chiu W., Quiocho F.A.
      EMBO J. 22:757-765(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 451-1054.

    Entry informationi

    Entry nameiMCP_HHV11
    AccessioniPrimary (citable) accession number: P06491
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 1, 1988
    Last modified: October 1, 2014
    This is version 76 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3