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Protein

ICP47 protein

Gene

US12

Organism
Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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 – 139Combined sources
Beta strandi16 – 183Combined sources
Helixi22 – 3110Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MSWALEMADT FLDTMRVGPR TYADVRDEIN KRGREDREAA RTAVHDPERP
60 70 80
LLRSPGLLPE IAPNASLGVA HRRTGGTVTD SPRNPVTR
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2703441.

Miscellaneous databases

EvolutionaryTraceiP03170.

Family and domain databases

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

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: January 7, 2015
This is version 74 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.