ID   ICP47_CHV16             Reviewed;          78 AA.
AC   Q7TLC4;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   23-FEB-2022, entry version 60.
DE   RecName: Full=ICP47 protein;
DE   AltName: Full=Immediate-early protein IE12;
DE   AltName: Full=Immediate-early-5;
DE   AltName: Full=Infected cell protein 47;
DE   AltName: Full=US12 protein;
DE   AltName: Full=Vmw12;
GN   Name=US12;
OS   Cercopithecine herpesvirus 16 (CeHV-16) (Herpesvirus papio 2).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX   NCBI_TaxID=340907;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9541; Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OH   NCBI_TaxID=90387; Macaca leonina (Northern pig-tailed macaque) (Macaca nemestrina leonina).
OH   NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
OH   NCBI_TaxID=9545; Macaca nemestrina (Pig-tailed macaque).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Isolate 860;
RX   PubMed=12771408; DOI=10.1099/vir.0.19053-0;
RA   Bigger J.E., Martin D.W.;
RT   "The genome of herpesvirus papio 2 is closely related to the genomes of
RT   human herpes simplex viruses.";
RL   J. Gen. Virol. 84:1411-1414(2003).
CC   -!- FUNCTION: Plays a role in the inhibition of host immune response. Binds
CC       specifically to transporters associated with antigen processing (TAP),
CC       thereby blocking peptide-binding and translocation by TAP as well as
CC       subsequent loading of peptides onto MHC class I molecules. Empty MHC I
CC       molecules are retained in the endoplasmic reticulum and ultimately
CC       directed to proteasomal degradation. In consequence, infected cells are
CC       masked for immune recognition by cytotoxic T-lymphocytes.
CC       {ECO:0000250|UniProtKB:P03170}.
CC   -!- SUBUNIT: Interacts with host TAP1 and TAP2; these interactions inhibit
CC       the loading of peptides onto MHC class I molecules.
CC       {ECO:0000250|UniProtKB:P03170}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250|UniProtKB:P03170}.
CC       Host nucleus {ECO:0000250|UniProtKB:P03170}.
CC   -!- DOMAIN: The N-terminal active domain blocks peptide binding to and
CC       peptide transport by TAP. {ECO:0000250|UniProtKB:P14345}.
CC   -!- SIMILARITY: Belongs to the herpesviridae US12 family. {ECO:0000305}.
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DR   EMBL; AY288071; AAP37045.1; -; Genomic_DNA.
DR   RefSeq; YP_443919.1; NC_007653.1.
DR   SMR; Q7TLC4; -.
DR   TCDB; 8.A.72.1.2; the immune evasion protein, icp47 (icp47) family.
DR   GeneID; 3850189; -.
DR   KEGG; vg:3850189; -.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0039588; P:suppression by virus of host antigen processing and presentation; IEA:UniProtKB-KW.
DR   InterPro; IPR008026; Herpes_ICP47.
DR   Pfam; PF05363; Herpes_US12; 1.
PE   3: Inferred from homology;
KW   Early protein; Host cytoplasm; Host nucleus; Host-virus interaction;
KW   Inhibition of host adaptive immune response by virus;
KW   Inhibition of host TAP by virus; Viral immunoevasion.
FT   CHAIN           1..78
FT                   /note="ICP47 protein"
FT                   /id="PRO_0000115813"
FT   REGION          3..36
FT                   /note="Active domain"
FT                   /evidence="ECO:0000250|UniProtKB:P14345"
FT   REGION          38..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..67
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   78 AA;  8567 MW;  C92AF46C479107E0 CRC64;
     MSSLYLAEVD AFLQSPRTRH RTCADLRREL DAYADEERRE AAKAIAHPDR PLLAPPSAPP
     DRSRPAPRGT AHPPAASP