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P03170 (ICP47_HHV11) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ICP47 protein
Alternative name(s):
Immediate-early protein IE12
Immediate-early-5
Infected cell protein 47
US12 protein
Vmw12
Gene names
Name:US12
OrganismHuman herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) [Reference proteome]
Taxonomic identifier10299 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeSimplexvirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length88 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9 Ref.10 Ref.12

Subcellular location

Host cytoplasm.

Domain

The N-terminal active domain blocks peptide binding to and peptide transport by TAP. Ref.11

Sequence similarities

Belongs to the herpesviridae US12 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 8888ICP47 protein
PRO_0000115810

Regions

Region2 – 3534Active domain

Sites

Site221Binding to TAP-1 subunit By similarity

Experimental info

Mutagenesis241D → G: Reduced ability to inhibit peptide-binding to TAP.
Mutagenesis311K → G: Reduced ability to inhibit peptide-binding to TAP.
Mutagenesis321R → G: Reduced ability to inhibit peptide-binding to TAP.
Sequence conflict141T → N Ref.1
Sequence conflict141T → N Ref.7

Secondary structure

....... 88
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P03170 [UniParc].

Last modified March 1, 2004. Version 2.
Checksum: C5D2EA8C35006612

FASTA889,793
        10         20         30         40         50         60 
MSWALEMADT FLDTMRVGPR TYADVRDEIN KRGREDREAA RTAVHDPERP LLRSPGLLPE 

        70         80 
IAPNASLGVA HRRTGGTVTD SPRNPVTR 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIREDBE51. A93454.
RefSeqNP_044675.1. NC_001806.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QLONMR-A1-34[»]
ProteinModelPortalP03170.
SMRP03170. Positions 1-34.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2703441.

Family and domain databases

InterProIPR008026. Herpes_ICP47.
[Graphical view]
PfamPF05363. Herpes_US12. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP03170.

Entry information

Entry nameICP47_HHV11
AccessionPrimary (citable) accession number: P03170
Secondary accession number(s): Q99BW2, Q9E0N0, Q9E0N1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: March 1, 2004
Last modified: April 3, 2013
This is version 70 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references