US06_HCMVM
ID US06_HCMVM Reviewed; 182 AA.
AC Q6SW00; D2K3V1;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 23-FEB-2022, entry version 52.
DE RecName: Full=Unique short US6 glycoprotein;
DE Flags: Precursor;
GN Name=US6;
OS Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX NCBI_TaxID=295027;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15105547; DOI=10.1099/vir.0.79888-0;
RA Dolan A., Cunningham C., Hector R.D., Hassan-Walker A.F., Lee L.,
RA Addison C., Dargan D.J., McGeoch D.J., Gatherer D., Emery V.C.,
RA Griffiths P.D., Sinzger C., McSharry B.P., Wilkinson G.W.G., Davison A.J.;
RT "Genetic content of wild-type human cytomegalovirus.";
RL J. Gen. Virol. 85:1301-1312(2004).
CC -!- FUNCTION: Inhibits peptide loading of MHC class I molecules by
CC transporters associated with antigen processing (TAP). Does not prevent
CC peptide binding to TAP, but binds to the lumenal side of the TAP
CC complex and inhibits peptide translocation by specifically blocking
CC ATP-binding to TAP1, but not TAP2. Also prevents the conformational
CC rearrangement of TAP induced by peptide binding. In consequence,
CC infected cells are masked for immune recognition by cytotoxic T-
CC lymphocytes (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with UL18. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane; Single-pass
CC type I membrane protein.
CC -!- DEVELOPMENTAL STAGE: Expressed at early period of virus infection.
CC -!- DOMAIN: The ER-lumenal domain is responsible for TAP inhibition. It is
CC sufficient to inhibit ATP binding to TAP (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cytomegalovirus US6 family. {ECO:0000305}.
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DR EMBL; AY446894; AAR31695.1; -; Genomic_DNA.
DR RefSeq; YP_081591.1; NC_006273.2.
DR PRIDE; Q6SW00; -.
DR DNASU; 3077555; -.
DR GeneID; 3077555; -.
DR KEGG; vg:3077555; -.
DR Proteomes; UP000000938; Genome.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0039588; P:suppression by virus of host antigen processing and presentation; IEA:UniProtKB-KW.
DR InterPro; IPR035129; US6.
DR Pfam; PF17616; US6; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Early protein; Glycoprotein; Host endoplasmic reticulum;
KW Host membrane; Host-virus interaction; Immunoglobulin domain;
KW Inhibition of host adaptive immune response by virus;
KW Inhibition of host TAP by virus; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Viral immunoevasion.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..182
FT /note="Unique short US6 glycoprotein"
FT /id="PRO_0000417852"
FT TOPO_DOM 20..143
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..182
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..130
FT /note="Ig-like H-type"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 38..126
FT /evidence="ECO:0000250"
SQ SEQUENCE 182 AA; 20511 MW; 4D0567C4F8C74AFB CRC64;
MDLLIRLGFL LMCALPTPGE RSSRDPKTLL SLSPRQACVP RTKSHRPVCY NDTGDCTDAD
DSWKQLGEDF AHQCLQAAKK RPKTHKSRPN DRNLEGRLTC QRVRRLLPCD LDIHPSHRLL
TLMNNCVCDG AVWNAFRLIE RHGFFAVTLY LCCGITLLVV ILALLCSITY ESTGRGIRRC
GS