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P03170

- ICP47_HHV11

UniProt

P03170 - ICP47_HHV11

Protein

ICP47 protein

Gene

US12

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
  1. Functioni

    Binds specifically to transporters associated with antigen processing (TAP), thereby blocking peptide-binding and translocation by TAP as well as subsequent loading of peptides onto MHC class I molecules in the endoplasmic reticulum. In consequence, infected cells are masked for immune recognition by cytotoxic T-lymphocytes.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei22 – 221Binding to TAP-1 subunitBy similarity

    GO - Biological processi

    1. suppression by virus of host TAP complex Source: UniProtKB-KW

    Keywords - Biological processi

    Host-virus interaction, Inhibition of host adaptive immune response by virus, Inhibition of host TAP by virus, Viral immunoevasion

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ICP47 protein
    Alternative name(s):
    Immediate-early protein IE12
    Immediate-early-5
    Infected cell protein 47
    US12 protein
    Vmw12
    Gene namesi
    Name:US12
    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

    GO - Cellular componenti

    1. host cell cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Host cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi24 – 241D → G: Reduced ability to inhibit peptide-binding to TAP. 1 Publication
    Mutagenesisi31 – 311K → G: Reduced ability to inhibit peptide-binding to TAP. 1 Publication
    Mutagenesisi32 – 321R → G: Reduced ability to inhibit peptide-binding to TAP. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 8888ICP47 proteinPRO_0000115810Add
    BLAST

    Expressioni

    Keywords - Developmental stagei

    Early protein

    Structurei

    Secondary structure

    1
    88
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 139
    Beta strandi16 – 183
    Helixi22 – 3110

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1QLONMR-A1-34[»]
    ProteinModelPortaliP03170.
    SMRiP03170. Positions 1-34.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP03170.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 3534Active domainAdd
    BLAST

    Domaini

    The N-terminal active domain blocks peptide binding to and peptide transport by TAP.

    Sequence similaritiesi

    Belongs to the herpesviridae US12 family.Curated

    Family and domain databases

    InterProiIPR008026. Herpes_ICP47.
    [Graphical view]
    PfamiPF05363. Herpes_US12. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P03170-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSWALEMADT FLDTMRVGPR TYADVRDEIN KRGREDREAA RTAVHDPERP   50
    LLRSPGLLPE IAPNASLGVA HRRTGGTVTD SPRNPVTR 88
    Length:88
    Mass (Da):9,793
    Last modified:March 1, 2004 - v2
    Checksum:iC5D2EA8C35006612
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti14 – 141T → N(PubMed:6278443)Curated
    Sequence conflicti14 – 141T → N(PubMed:11117552)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02220 Genomic DNA. Translation: AAA45795.1.
    L00036 Genomic DNA. Translation: AAA96676.1.
    X00428 Genomic RNA. Translation: CAA25124.1.
    X02138 Genomic DNA. Translation: CAA26066.1.
    X14112 Genomic DNA. Translation: CAA32277.1.
    V00462 Genomic DNA. Translation: CAA23737.1.
    AF290017 Genomic DNA. Translation: AAG33133.1.
    AF290018 Genomic DNA. Translation: AAG33134.1.
    AF324428 Genomic DNA. Translation: AAK12110.1.
    PIRiA93454. EDBE51.
    RefSeqiNP_044675.1. NC_001806.1.

    Genome annotation databases

    GeneIDi2703441.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02220 Genomic DNA. Translation: AAA45795.1 .
    L00036 Genomic DNA. Translation: AAA96676.1 .
    X00428 Genomic RNA. Translation: CAA25124.1 .
    X02138 Genomic DNA. Translation: CAA26066.1 .
    X14112 Genomic DNA. Translation: CAA32277.1 .
    V00462 Genomic DNA. Translation: CAA23737.1 .
    AF290017 Genomic DNA. Translation: AAG33133.1 .
    AF290018 Genomic DNA. Translation: AAG33134.1 .
    AF324428 Genomic DNA. Translation: AAK12110.1 .
    PIRi A93454. EDBE51.
    RefSeqi NP_044675.1. NC_001806.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1QLO NMR - A 1-34 [» ]
    ProteinModelPortali P03170.
    SMRi P03170. Positions 1-34.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 2703441.

    Miscellaneous databases

    EvolutionaryTracei P03170.

    Family and domain databases

    InterProi IPR008026. Herpes_ICP47.
    [Graphical view ]
    Pfami PF05363. Herpes_US12. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "DNA sequence of an immediate-early gene (IEmRNA-5) of herpes simplex virus type I."
      Watson R.J., Vande Woude G.F.
      Nucleic Acids Res. 10:979-991(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "DNA sequence analysis of an immediate-early gene region of the herpes simplex virus type 1 genome (map coordinates 0.950 to 0.978)."
      Murchie M.-J., McGeoch D.J.
      J. Gen. Virol. 62:1-15(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "A 3' co-terminal family of mRNAs from the herpes simplex virus type 1 short region: two overlapping reading frames encode unrelated polypeptide one of which has highly reiterated amino acid sequence."
      Rixon F.J., McGeoch D.J.
      Nucleic Acids Res. 12:2473-2487(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Sequence determination and genetic content of the short unique region in the genome of herpes simplex virus type 1."
      McGeoch D.J., Dolan A., Donald S., Rixon F.J.
      J. Mol. Biol. 181:1-13(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "The DNA sequences of the long repeat region and adjoining parts of the long unique region in the genome of herpes simplex virus type 1."
      Perry L.J., McGeoch D.J.
      J. Gen. Virol. 69:2831-2846(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. "Reiterated sequences within the intron of an immediate-early gene of herpes simplex virus type 1."
      Watson R.J., Umene K., Enquist L.W.
      Nucleic Acids Res. 9:4189-4199(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-55.
    7. "Herpes simplex virus type 1 (HSV-1)-induced retinitis following herpes simplex encephalitis: indications for brain-to-eye transmission of HSV-1."
      Maertzdorf J., Van der Lelij A., Baarsma G.S., Osterhaus A.D.M.E., Verjans G.M.G.M.
      Ann. Neurol. 48:936-939(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.
    8. "Herpes simplex virus type 1 transmission through corneal transplantation."
      Remeijer L., Maertzdorf J., Doornenbal P., Verjans G.M.G.M., Osterhaus A.D.M.E.
      Lancet 357:442-442(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.
      Strain: Isolates D and R.
    9. "A viral inhibitor of peptide transporters for antigen presentation."
      Frueh K., Ahn K., Djaballah H., Sempe P., van Endert P.M., Tampe R., Peterson P.A., Yang Y.
      Nature 375:415-418(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: Strain F.
    10. "Molecular mechanism and species specificity of TAP inhibition by herpes simplex virus ICP47."
      Ahn K., Meyer T.H., Uebel S., Sempe P., Djaballah H., Yang Y., Peterson P.A., Frueh K., Tampe R.
      EMBO J. 15:3247-3255(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: Strain F.
    11. "The active domain of the herpes simplex virus protein ICP47: a potent inhibitor of the transporter associated with antigen processing (TAP)."
      Neumann L., Kraas W., Uebel S., Jung G., Tampe R.
      J. Mol. Biol. 272:484-492(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE DOMAIN, MUTAGENESIS.
      Strain: Strain F.
    12. "Inhibition of antigen transport by expression of infected cell peptide 47 (ICP47) prevents cell surface expression of HLA in choriocarcinoma cell lines."
      Easterfield A.J., Austen B.M., Westwood O.M.R.
      J. Reprod. Immunol. 50:19-40(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: Strain F.
    13. "Structure of the active domain of the herpes simplex virus protein ICP47 in water/sodium dodecyl sulfate solution determined by nuclear magnetic resonance spectroscopy."
      Pfaender R., Neumann L., Zweckstetter M., Seger C., Holak T.A., Tampe R.
      Biochemistry 38:13692-13698(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 2-34.

    Entry informationi

    Entry nameiICP47_HHV11
    AccessioniPrimary (citable) accession number: P03170
    Secondary accession number(s): Q99BW2, Q9E0N0, Q9E0N1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: March 1, 2004
    Last modified: October 1, 2014
    This is version 71 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, 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