E3GL_ADE05
ID E3GL_ADE05 Reviewed; 160 AA.
AC P04494;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Early E3 18.5 kDa glycoprotein;
DE AltName: Full=E3-19K;
DE AltName: Full=E3gp 19 kDa;
DE Short=E19;
DE AltName: Full=GP19K;
DE Flags: Precursor;
OS Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus.
OX NCBI_TaxID=28285;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2981456; DOI=10.1016/0042-6822(85)90443-x;
RA Cladaras C., Wold W.S.M.;
RT "DNA sequence of the early E3 transcription unit of adenovirus 5.";
RL Virology 140:28-43(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF N-TERMINUS.
RX PubMed=3882694; DOI=10.1016/s0021-9258(18)89571-0;
RA Wold W.S.M., Cladaras C., Deutscher S.L., Kapoor Q.S.;
RT "The 19-kDa glycoprotein coded by region E3 of adenovirus. Purification,
RT characterization, and structural analysis.";
RL J. Biol. Chem. 260:2424-2431(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=1727603; DOI=10.1016/0042-6822(92)90082-z;
RA Chroboczek J., Bieber F., Jacrot B.;
RT "The sequence of the genome of adenovirus type 5 and its comparison with
RT the genome of adenovirus type 2.";
RL Virology 186:280-285(1992).
RN [4]
RP FUNCTION.
RX PubMed=10227971;
RA Bennett E.M., Bennink J.R., Yewdell J.W., Brodsky F.M.;
RT "Adenovirus E19 has two mechanisms for affecting class I MHC expression.";
RL J. Immunol. 162:5049-5052(1999).
CC -!- FUNCTION: Binds and retains class I heavy chains in the endoplasmic
CC reticulum during the early period of virus infection, thereby impairing
CC their transport to the cell surface. Also delays the expression of
CC class I alleles that it cannot affect by direct retention. Binds
CC transporters associated with antigen processing (TAP) and acts as a
CC tapasin inhibitor, preventing class I/TAP association. In consequence,
CC infected cells are masked for immune recognition by cytotoxic T-
CC lymphocytes. {ECO:0000269|PubMed:10227971}.
CC -!- SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane; Single-pass
CC type I membrane protein.
CC -!- DEVELOPMENTAL STAGE: Expressed at early period of virus infection.
CC -!- DOMAIN: The lumenal domain binds directly to the peptide-binding domain
CC of class I molecules.
CC -!- DOMAIN: The di-lysine motif confers endoplasmic reticulum localization
CC for type I membrane proteins. {ECO:0000250}.
CC -!- PTM: Both disulfide bonds are absolutely critical for the interaction
CC with MHC antigens. {ECO:0000250}.
CC -!- PTM: N-glycosylated; high-mannose. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the adenoviridae E19 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; M73260; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X03002; CAA26783.1; -; Genomic_DNA.
DR EMBL; M12406; AAA42492.1; -; Genomic_DNA.
DR PIR; A03822; ERADA5.
DR RefSeq; AP_000220.1; AC_000008.1.
DR SMR; P04494; -.
DR IntAct; P04494; 4.
DR MINT; P04494; -.
DR Proteomes; UP000004992; 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 GO; GO:0046776; P:suppression by virus of host antigen processing and presentation of peptide antigen via MHC class I; IDA:GO_Central.
DR Gene3D; 2.60.40.3530; -; 1.
DR InterPro; IPR006965; Adenovirus_Gp19K.
DR InterPro; IPR038710; Adenovirus_Gp19K_sf.
DR Pfam; PF04881; Adeno_GP19K; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Early protein; Glycoprotein;
KW Host endoplasmic reticulum; Host membrane; Host-virus interaction;
KW Inhibition of host adaptive immune response by virus;
KW Inhibition of host tapasin by virus; Lectin; Mannose-binding; Membrane;
KW Signal; Transmembrane; Transmembrane helix; Viral immunoevasion.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:3882694"
FT CHAIN 18..160
FT /note="Early E3 18.5 kDa glycoprotein"
FT /id="PRO_0000036484"
FT TOPO_DOM 18..124
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 157..160
FT /note="Di-lysine motif"
FT /evidence="ECO:0000305"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 29..46
FT /evidence="ECO:0000250"
FT DISULFID 40..101
FT /evidence="ECO:0000250"
SQ SEQUENCE 160 AA; 18502 MW; B1F0D2AC4D6330E0 CRC64;
MIRYIILGLL TLASAHGTTQ KVDFKEPACN VTFAAEANEC TTLIKCTTEH EKLLIRHKNK
IGKYAVYAIW QPGDTTEYNV TVFQGKSHKT FMYTFPFYEM CDITMYMSKQ YKLWPPQNCV
ENTGTFCCTA MLITVLALVC TLLYIKYKSR RSFIEEKKMP
