US06_HCMVA
ID US06_HCMVA Reviewed; 183 AA.
AC P14334; Q7M6G5;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 23-FEB-2022, entry version 82.
DE RecName: Full=Unique short US6 glycoprotein;
DE AltName: Full=Protein HXLF6;
DE AltName: Full=gpUS6;
DE Flags: Precursor;
GN Name=US6;
OS Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX NCBI_TaxID=10360;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3031311; DOI=10.1016/0022-2836(86)90359-1;
RA Weston K.M., Barrell B.G.;
RT "Sequence of the short unique region, short repeats, and part of the long
RT repeats of human cytomegalovirus.";
RL J. Mol. Biol. 192:177-208(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=2161319; DOI=10.1007/978-3-642-74980-3_6;
RA Chee M.S., Bankier A.T., Beck S., Bohni R., Brown C.M., Cerny R.,
RA Horsnell T., Hutchison C.A. III, Kouzarides T., Martignetti J.A.,
RA Preddie E., Satchwell S.C., Tomlinson P., Weston K.M., Barrell B.G.;
RT "Analysis of the protein-coding content of the sequence of human
RT cytomegalovirus strain AD169.";
RL Curr. Top. Microbiol. Immunol. 154:125-169(1990).
RN [3]
RP GENOME REANNOTATION.
RX PubMed=12533697; DOI=10.1099/vir.0.18606-0;
RA Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA McGeoch D.J., Hayward G.S.;
RT "The human cytomegalovirus genome revisited: comparison with the chimpanzee
RT cytomegalovirus genome.";
RL J. Gen. Virol. 84:17-28(2003).
RN [4]
RP ERRATUM OF PUBMED:12533697.
RA Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA McGeoch D.J., Hayward G.S.;
RL J. Gen. Virol. 84:1053-1053(2003).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9175839; DOI=10.1016/s1074-7613(00)80349-0;
RA Ahn K., Gruhler A., Galocha B., Jones T.R., Wiertz E.J.H.J., Ploegh H.L.,
RA Peterson P.A., Yang Y., Frueh K.;
RT "The ER-luminal domain of the HCMV glycoprotein US6 inhibits peptide
RT translocation by TAP.";
RL Immunity 6:613-621(1997).
RN [6]
RP FUNCTION.
RX PubMed=11157746; DOI=10.1093/emboj/20.3.387;
RA Hewitt E.W., Gupta S.S., Lehner P.J.;
RT "The human cytomegalovirus gene product US6 inhibits ATP binding by TAP.";
RL EMBO J. 20:387-396(2001).
RN [7]
RP INTERACTION WITH UL18.
RX PubMed=18688275; DOI=10.1371/journal.ppat.1000123;
RA Kim Y., Park B., Cho S., Shin J., Cho K., Jun Y., Ahn K.;
RT "Human cytomegalovirus UL18 utilizes US6 for evading the NK and T-cell
RT responses.";
RL PLoS Pathog. 4:E1000123-E1000123(2008).
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. {ECO:0000269|PubMed:11157746, ECO:0000269|PubMed:9175839}.
CC -!- SUBUNIT: Interacts with UL18. {ECO:0000269|PubMed:18688275}.
CC -!- SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:9175839}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:9175839}.
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.
CC -!- SIMILARITY: Belongs to the cytomegalovirus US6 family. {ECO:0000305}.
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DR EMBL; X17403; CAA35273.1; -; Genomic_DNA.
DR EMBL; X04650; CAB37098.1; -; Genomic_DNA.
DR EMBL; BK000394; DAA00223.1; -; Genomic_DNA.
DR PIR; G26078; QQBEC7.
DR Proteomes; UP000008991; Genome.
DR Proteomes; UP000008992; 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 1: Evidence at protein 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..183
FT /note="Unique short US6 glycoprotein"
FT /id="PRO_0000037438"
FT TOPO_DOM 20..144
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..183
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..131
FT /note="Ig-like H-type"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 39..127
FT /evidence="ECO:0000250"
SQ SEQUENCE 183 AA; 20639 MW; C3722E9F011C0023 CRC64;
MDLLIRLGFL LMCALPTPGE RSSRDPKTLL SLSPRQQACV PRTKSHRPVC YNDTGDCTDA
DDSWKQLGED FAHQCLQAAK KRPKTHKSRP NDRNLEGRLT CQRVRRLLPC DLDIHPSHRL
LTLMNNCVCD GAVWNAFRLI ERHGFFAVTL YLCCGITLLV VILALLCSIT YESTGRGIRR
CGS
