ID   US11_HCMVM              Reviewed;         215 AA.
AC   Q6SVZ5; D2K3V6;
DT   11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   23-FEB-2022, entry version 58.
DE   RecName: Full=Membrane glycoprotein US11;
DE   Flags: Precursor;
GN   Name=US11;
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: 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:0000250|UniProtKB:P09727}.
CC   -!- SUBUNIT: Interacts with host TRAM1. {ECO:0000250|UniProtKB:P09727}.
CC   -!- SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane
CC       {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Expressed at early and late period of virus
CC       infection.
CC   -!- PTM: N-glycosylated. {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytomegalovirus US6 family. {ECO:0000305}.
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DR   EMBL; AY446894; AAR31700.1; -; Genomic_DNA.
DR   RefSeq; YP_081596.1; NC_006273.2.
DR   BioGRID; 1678043; 4.
DR   PRIDE; Q6SVZ5; -.
DR   DNASU; 3077490; -.
DR   GeneID; 3077490; -.
DR   KEGG; vg:3077490; -.
DR   Reactome; R-HSA-9609690; HCMV Early Events.
DR   Proteomes; UP000000938; 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: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   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 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                   /evidence="ECO:0000255"
FT   CHAIN           18..215
FT                   /note="Membrane glycoprotein US11"
FT                   /id="PRO_0000418320"
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:0000250"
FT   DISULFID        56..142
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   215 AA;  25288 MW;  6872C1A2B7C1D21F CRC64;
     MNLVMLILAL WAPVAGSMPE LSLTLFDEPP PLVETEPLPP LPDVSEYRVE YSEARCVLRS
     GGRLEALWTL RGNLSVPTPT PRVYYQTLEG YADRVPTPVE DISESLVAKR YWLRDYRVPQ
     RTKLVLFYFS PCHQCQTYYV ECEPRCLVPW VPLWSSLEDI ERLLFEDRRL MAYYALTIKS
     AQYTLMMVAV IQVFWGLYVK GWLHRHFPWM FSDQW