US02_HCMVM
ID US02_HCMVM Reviewed; 199 AA.
AC F5HE05;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Unique short US2 glycoprotein;
DE AltName: Full=Protein HQLF2;
DE AltName: Full=gpUS2;
GN Name=US2;
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 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 -!- DEVELOPMENTAL STAGE: Expressed at early period of virus infection.
CC -!- DOMAIN: The lumenal domain allows tight interaction with class I
CC molecules encoded by the HLA-A locus.
CC -!- PTM: The signal sequence is not cleaved. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cytomegalovirus US2 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY446894; AAR31693.1; -; Genomic_DNA.
DR RefSeq; YP_081589.1; NC_006273.2.
DR SMR; F5HE05; -.
DR BioGRID; 1678095; 1.
DR PRIDE; F5HE05; -.
DR DNASU; 3077542; -.
DR GeneID; 3077542; -.
DR KEGG; vg:3077542; -.
DR Reactome; R-HSA-9609690; HCMV Early Events.
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 InterPro; IPR009237; Herpes_US2/US3.
DR InterPro; IPR014756; Ig_E-set.
DR Pfam; PF05963; Cytomega_US3; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Early protein; Glycoprotein; Host endoplasmic reticulum;
KW Host membrane; Host-virus interaction; Immunoglobulin domain; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Viral immunoevasion.
FT CHAIN 1..199
FT /note="Unique short US2 glycoprotein"
FT /id="PRO_0000418292"
FT SIGNAL 1..?
FT /note="Not cleaved"
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; 23112 MW; 201A43BDE87793E6 CRC64;
MNNLWKAWVG LWTSMGPLIR LPDGITKAGE DALRPWKSTA KHPWFEIEDN RCYIDNGKLF
ARGSIVGNMS RFVFDPKADY GGVGENLYVH ADDVEFVPGE SLKWNVRNLD VMPIFETLAL
RLVLQGDVIW LRCVPELRVD YTSSAYMWNM QYGMVRKSYT HVAWTIVFYS INITLLVLFI
VYVTVDCNLS MMWMRFFVC
