US03_HCMVA
ID US03_HCMVA Reviewed; 186 AA.
AC P09712; Q7M6H1;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Membrane glycoprotein US3;
DE AltName: Full=Glycoprotein E;
DE AltName: Full=Protein HQLF1;
DE AltName: Full=gpUS3 IE;
GN Name=US3;
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 [GENOMIC DNA].
RX PubMed=2829427; DOI=10.1016/0042-6822(88)90481-3;
RA Weston K.M.;
RT "An enhancer element in the short unique region of human cytomegalovirus
RT regulates the production of a group of abundant immediate early
RT transcripts.";
RL Virology 162:406-416(1988).
RN [3]
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 [4]
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 [5]
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 [6]
RP FUNCTION.
RX PubMed=8876135; DOI=10.1073/pnas.93.21.11327;
RA Jones T.R., Wiertz E.J.H.J., Sun L., Fish K.N., Nelson J.A., Ploegh H.L.;
RT "Human cytomegalovirus US3 impairs transport and maturation of major
RT histocompatibility complex class I heavy chains.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:11327-11333(1996).
RN [7]
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).
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 {ECO:0000269|PubMed:8855296, ECO:0000269|PubMed:8876135}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:8855296}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:8855296}.
CC -!- DEVELOPMENTAL STAGE: Expressed at immediate-early period of virus
CC infection and at reduced levels at early-late times.
CC {ECO:0000269|PubMed:8855296}.
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}.
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DR EMBL; X17403; CAA35314.1; -; Genomic_DNA.
DR EMBL; X04650; CAB37097.1; -; Genomic_DNA.
DR EMBL; M18921; AAA45958.1; -; Genomic_DNA.
DR EMBL; BK000394; DAA00217.1; -; Genomic_DNA.
DR PIR; F26078; QQBEC6.
DR PRIDE; P09712; -.
DR Proteomes; UP000008991; Genome.
DR Proteomes; UP000008992; 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 CHAIN 1..186
FT /note="Membrane glycoprotein US3"
FT /id="PRO_0000223277"
FT SIGNAL 1..?
FT /note="Not cleaved"
FT /evidence="ECO:0000250"
FT TOPO_DOM 1..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 DOMAIN 35..133
FT /note="Ig-like H-type"
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; 21574 MW; 671753C1AA75920D CRC64;
MKPVLVLAIL AVLFLRLADS VPRPLDVVVS EIRSAHFRVE ENQCWFHMGM LYFKGRMSGN
FTEKHFVNVG IVSQSYMDRL QVSGEQYHHD ERGAYFEWNI GGHPVTHTVD MVDITLSTRW
GDPKKYAACV PQVRMDYSSQ TINWYLQRSM RDDNWGLLFR TLLVYLFSLV VLVLLTVGVS
ARLRFI
