ID   US02_HCMVT              Reviewed;         199 AA.
AC   P60503;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Unique short US2 glycoprotein;
DE   AltName: Full=HQLF2;
DE   AltName: Full=gpUS2;
GN   Name=US2;
OS   Human cytomegalovirus (strain Towne) (HHV-5) (Human herpesvirus 5).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX   NCBI_TaxID=10363;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12535225; DOI=10.1034/j.1399-3089.2003.01116.x;
RA   Crew M.D., Phanavanh B.;
RT   "Exploiting virus stealth technology for xenotransplantation: reduced human
RT   T cell responses to porcine cells expressing herpes simplex virus ICP47.";
RL   Xenotransplantation 10:50-59(2003).
CC   -!- FUNCTION: Participates in the inhibition of the host immune response.
CC       Early protein that redirects newly synthesized major histocompatibility
CC       complex (MHC) class I heavy chains via the SEC61 translocon to the
CC       cytosol where they undergo proteasome-dependent destruction. In
CC       consequence, infected cells are masked for immune recognition by
CC       cytotoxic T lymphocytes. Seems so far to be specific for HLA-A, HLA-B,
CC       and HFE loci products. Does not interact with HLA-DR or HLA-DM.
CC       {ECO:0000250|UniProtKB:P09713}.
CC   -!- SUBUNIT: Monomer. Interacts with host TRAM1.
CC       {ECO:0000250|UniProtKB:P09713}.
CC   -!- SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane
CC       {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC   -!- DOMAIN: The lumenal domain allows tight interaction with class I
CC       molecules encoded by the HLA-A locus. {ECO:0000250}.
CC   -!- PTM: The signal sequence is not cleaved. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytomegalovirus US2 family. {ECO:0000305}.
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DR   EMBL; AY072773; AAL67141.1; -; Genomic_DNA.
DR   SMR; P60503; -.
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   InterPro; IPR009237; Herpes_US2/US3.
DR   InterPro; IPR014756; Ig_E-set.
DR   Pfam; PF05963; Cytomega_US3; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Early protein; Glycoprotein; Host endoplasmic reticulum;
KW   Host membrane; Host-virus interaction; Immunoglobulin domain; Membrane;
KW   Signal; Transmembrane; Transmembrane helix; Viral immunoevasion.
FT   CHAIN           1..199
FT                   /note="Unique short US2 glycoprotein"
FT                   /id="PRO_0000223276"
FT   SIGNAL          1..?
FT                   /note="Not cleaved"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        1..161
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        162..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        183..199
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          43..137
FT                   /note="Ig-like H-type"
FT   CARBOHYD        68
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P09713"
FT   DISULFID        52..133
FT                   /evidence="ECO:0000250|UniProtKB:P09713"
SQ   SEQUENCE   199 AA;  23111 MW;  4DD2DF3D692393F3 CRC64;
     MNNLWKAWVG LWTSMGPLIR LPDGITKAGE DALRPWKSTA KHPWFQIEDN RCYIDNGKLF
     ARGSIVGNMS RFVFDPKADY GGVGENLYVH ADDVEFVPGE SLKWNVRNLD VMPIFETLAL
     RLVLQGDVIW LRCVPELRVD YTSSAYMWNM QYGMVRKSYT HVAWTIVFYS INITLLVLFI
     VYVTVDCNLS MMWMRFFVC