US11_HCMVA
ID US11_HCMVA Reviewed; 215 AA.
AC P09727; Q7M6I9;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 23-FEB-2022, entry version 94.
DE RecName: Full=Unique short US11 glycoprotein;
DE AltName: Full=Protein HXLF1;
DE AltName: Full=gpUS11;
DE Flags: Precursor;
GN Name=US11;
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=8625414; DOI=10.1016/s0092-8674(00)81054-5;
RA Wiertz E.J.H.J., Jones T.R., Sun L., Bogyo M., Geuze H.J., Ploegh H.L.;
RT "The human cytomegalovirus US11 gene product dislocates MHC class I heavy
RT chains from the endoplasmic reticulum to the cytosol.";
RL Cell 84:769-779(1996).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=8855296; DOI=10.1073/pnas.93.20.10990;
RA Ahn K., Angulo A., Ghazal P., Peterson P.A., Yang Y., Frueh K.;
RT "Human cytomegalovirus inhibits antigen presentation by a sequential
RT multistep process.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:10990-10995(1996).
RN [7]
RP DELAYED CLEAVAGE OF SIGNAL PEPTIDE, AND GLYCOSYLATION.
RX PubMed=11285222; DOI=10.1093/emboj/20.7.1573;
RA Rehm A., Stern P., Ploegh H.L., Tortorella D.;
RT "Signal peptide cleavage of a type I membrane protein, HCMV US11, is
RT dependent on its membrane anchor.";
RL EMBO J. 20:1573-1582(2001).
RN [8]
RP REVIEW ON FUNCTION.
RX PubMed=12224515; DOI=10.1007/978-3-642-59421-2_3;
RA van der Wal F.J., Kikkert M., Wiertz E.;
RT "The HCMV gene products US2 and US11 target MHC class I molecules for
RT degradation in the cytosol.";
RL Curr. Top. Microbiol. Immunol. 269:37-55(2002).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF GLN-192.
RX PubMed=15823579; DOI=10.1016/j.bbrc.2005.03.112;
RA Lee S.O., Hwang S., Park J., Park B., Jin B.S., Lee S., Kim E., Cho S.,
RA Kim Y., Cho K., Shin J., Ahn K.;
RT "Functional dissection of HCMV US11 in mediating the degradation of MHC
RT class I molecules.";
RL Biochem. Biophys. Res. Commun. 330:1262-1267(2005).
RN [10]
RP FUNCTION, AND INTERACTION WITH HOST TRAM1.
RX PubMed=19121997; DOI=10.1074/jbc.m807568200;
RA Oresic K., Ng C.L., Tortorella D.;
RT "TRAM1 participates in human cytomegalovirus US2- and US11-mediated
RT dislocation of an endoplasmic reticulum membrane glycoprotein.";
RL J. Biol. Chem. 284:5905-5914(2009).
CC -!- FUNCTION: Participates in the inhibition of the host immune response.
CC Redirects newly synthesized major histocompatibility complex (MHC)
CC class I heavy chains via the SEC61 translocon to the cytosol where they
CC undergo proteasome-dependent destruction. In consequence, infected
CC cells are masked for immune recognition by cytotoxic T-lymphocytes.
CC {ECO:0000269|PubMed:15823579, ECO:0000269|PubMed:19121997,
CC ECO:0000269|PubMed:8625414, ECO:0000269|PubMed:8855296}.
CC -!- SUBUNIT: Interacts with host TRAM1. {ECO:0000269|PubMed:19121997}.
CC -!- SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:8625414, ECO:0000269|PubMed:8855296}; Single-pass
CC type I membrane protein {ECO:0000269|PubMed:8625414,
CC ECO:0000269|PubMed:8855296}.
CC -!- DEVELOPMENTAL STAGE: Expressed at early and late period of virus
CC infection. {ECO:0000269|PubMed:8855296}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:11285222}.
CC -!- PTM: A fraction of newly synthesized molecules retain the signal
CC peptide after the N-linked glycan has been attached and translation of
CC the polypeptide has been completed. Delayed cleavage of the signal
CC peptide is determined by the first four residues, as well as by the
CC transmembrane region. {ECO:0000269|PubMed:11285222}.
CC -!- SIMILARITY: Belongs to the cytomegalovirus US6 family. {ECO:0000305}.
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DR EMBL; X17403; CAA35278.1; -; Genomic_DNA.
DR EMBL; X04650; CAB37103.1; -; Genomic_DNA.
DR EMBL; BK000394; DAA00199.1; -; Genomic_DNA.
DR PIR; C27230; QQBEF3.
DR IntAct; P09727; 1.
DR iPTMnet; P09727; -.
DR Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR Proteomes; UP000008991; Genome.
DR Proteomes; UP000008992; Genome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0044386; C:integral to host endoplasmic reticulum membrane; IEA:InterPro.
DR GO; GO:0042786; P:evasion of host immune response via regulation of host antigen processing and presentation; TAS:UniProtKB.
DR GO; GO:0046776; P:suppression by virus of host antigen processing and presentation of peptide antigen via MHC class I; IEA:UniProtKB-KW.
DR InterPro; IPR012536; CMV_US.
DR Pfam; PF08001; CMV_US; 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 MHC class I molecule presentation by virus;
KW Late protein; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Viral immunoevasion.
FT SIGNAL 1..17
FT /note="Partially cleaved"
FT CHAIN 18..215
FT /note="Unique short US11 glycoprotein"
FT /id="PRO_0000037444"
FT TOPO_DOM 18..182
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..215
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 47..146
FT /note="Ig-like H-type"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000305|PubMed:11285222"
FT DISULFID 56..142
FT /evidence="ECO:0000250"
FT MUTAGEN 192
FT /note="Q->V: Loss of the capacity to induce the degradation
FT of MHC class I molecules."
FT /evidence="ECO:0000269|PubMed:15823579"
SQ SEQUENCE 215 AA; 25264 MW; 6484695627C068E2 CRC64;
MNLVMLILAL WAPVAGSMPE LSLTLFDEPP PLVETEPLPP LSDVSEYRVE YSEARCVLRS
GGRLEALWTL RGNLSVPTPT PRVYYQTLEG YADRVPTPVE DVSESLVAKR YWLRDYRVPQ
RTKLVLFYFS PCHQCQTYYV ECEPRCLVPW VPLWSSLEDI ERLLFEDRRL MAYYALTIKS
AQYTLMMVAV IQVFWGLYVK GWLHRHFPWM FSDQW
