US03_HCMVM
ID US03_HCMVM Reviewed; 186 AA.
AC F5HEU0;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Membrane glycoprotein US3;
DE Flags: Precursor;
GN Name=US3;
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: Retains, but does not degrade MHC class I heterodimers in the
CC endoplasmic reticulum during the immediate-early period of virus
CC infection, thereby impairing their transport and maturation. Forms a
CC complex with beta-2-microglobulin-associated class I heavy chains,
CC which accumulate in the ER. In consequence, infected cells are masked
CC for immune recognition by cytotoxic T-lymphocytes.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane
CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed at immediate-early period of virus
CC infection and at reduced levels at early-late times.
CC -!- PTM: The signal sequence is not cleaved. {ECO:0000250}.
CC -!- PTM: N-glycosylated; mostly exists in a high-mannose form.
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; AAR31694.1; -; Genomic_DNA.
DR RefSeq; YP_081590.1; NC_006273.2.
DR SMR; F5HEU0; -.
DR BioGRID; 1678085; 2.
DR PRIDE; F5HEU0; -.
DR DNASU; 3077532; -.
DR GeneID; 3077532; -.
DR KEGG; vg:3077532; -.
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 GO; GO:0005537; F:mannose binding; 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; Lectin;
KW Mannose-binding; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Viral immunoevasion.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..186
FT /note="Membrane glycoprotein US3"
FT /id="PRO_0000416721"
FT TOPO_DOM 21..160
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..186
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 44..129
FT /evidence="ECO:0000250"
SQ SEQUENCE 186 AA; 21556 MW; 34D58C17BE5EA06B CRC64;
MKPVLVLAIL AVLFLRLADS VPRPLNVVVS EIKSAHFRVE ENQCWFHMGM LYFKGRMSGN
FTKKHFVNVG IVSQSYMDRL QVSGEQYHHD ERGAYFEWNI GGYPVSHTVD MVDITLSTRW
GDPKKYAACV PQVRMDYSSQ TINWYLQRSM RDDNWGLLFR TLLVYLFSLV VLVLLTVGVS
ARLRFI
