E3GL_ADE02
ID E3GL_ADE02 Reviewed; 159 AA.
AC P68978; P03251;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 76.
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 2 (HAdV-2) (Human adenovirus 2).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus.
OX NCBI_TaxID=10515;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6253880; DOI=10.1093/nar/8.10.2173;
RA Herisse J., Courtois G., Galibert F.;
RT "Nucleotide sequence of the EcoRI D fragment of adenovirus 2 genome.";
RL Nucleic Acids Res. 8:2173-2192(1980).
RN [2]
RP PROTEIN SEQUENCE OF N-TERMINUS, AND GLYCOSYLATION.
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 DI-LYSINE MOTIF.
RX PubMed=2120038; DOI=10.1002/j.1460-2075.1990.tb07513.x;
RA Jackson M.R., Nilsson T., Peterson P.A.;
RT "Identification of a consensus motif for retention of transmembrane
RT proteins in the endoplasmic reticulum.";
RL EMBO J. 9:3153-3162(1990).
RN [4]
RP DISULFIDE BONDS, AND MUTAGENESIS OF CYS-28; CYS-39; CYS-45; CYS-100;
RP CYS-118; CYS-126 AND CYS-139.
RX PubMed=8057424; DOI=10.1128/jvi.68.9.5423-5432.1994;
RA Sester M., Burgert H.-G.;
RT "Conserved cysteine residues within the E3/19K protein of adenovirus type 2
RT are essential for binding to major histocompatibility complex antigens.";
RL J. Virol. 68:5423-5432(1994).
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 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P68978; Q96WV5: SPBPJ4664.04; Xeno; NbExp=2; IntAct=EBI-4407041, EBI-8503699;
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.
CC -!- PTM: Both disulfide bonds are absolutely critical for the interaction
CC with MHC antigens.
CC -!- PTM: N-glycosylated; high-mannose. {ECO:0000269|PubMed:3882694}.
CC -!- SIMILARITY: Belongs to the adenoviridae E19 family. {ECO:0000305}.
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DR EMBL; J01917; AAA92221.1; -; Genomic_DNA.
DR PIR; A03821; Q6ADE.
DR RefSeq; AP_000184.1; AC_000007.1.
DR RefSeq; NP_040531.1; NC_001405.1.
DR SMR; P68978; -.
DR ELM; P68978; -.
DR IntAct; P68978; 8.
DR MINT; P68978; -.
DR GeneID; 2652987; -.
DR KEGG; vg:2652987; -.
DR Proteomes; UP000008167; 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; IEA:UniProtKB-KW.
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 Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Viral immunoevasion.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:3882694"
FT CHAIN 18..159
FT /note="Early E3 18.5 kDa glycoprotein"
FT /id="PRO_0000036482"
FT TOPO_DOM 18..123
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..159
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 156..159
FT /note="Di-lysine motif"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 28..45
FT /evidence="ECO:0000269|PubMed:8057424"
FT DISULFID 39..100
FT /evidence="ECO:0000269|PubMed:8057424"
FT MUTAGEN 28
FT /note="C->S: Complete loss of binding to Tw1.3 epitope."
FT /evidence="ECO:0000269|PubMed:8057424"
FT MUTAGEN 39
FT /note="C->A,S: 60% loss of binding to Tw1.3 epitope."
FT /evidence="ECO:0000269|PubMed:8057424"
FT MUTAGEN 45
FT /note="C->S: Complete loss of binding to Tw1.3 epitope."
FT /evidence="ECO:0000269|PubMed:8057424"
FT MUTAGEN 100
FT /note="C->S: 60% loss of binding to Tw1.3 epitope."
FT /evidence="ECO:0000269|PubMed:8057424"
FT MUTAGEN 118
FT /note="C->S: No effect."
FT /evidence="ECO:0000269|PubMed:8057424"
FT MUTAGEN 126
FT /note="C->S: No effect."
FT /evidence="ECO:0000269|PubMed:8057424"
FT MUTAGEN 139
FT /note="C->S: No effect."
FT /evidence="ECO:0000269|PubMed:8057424"
SQ SEQUENCE 159 AA; 18438 MW; ED2519547E18AEB0 CRC64;
MRYMILGLLA LAAVCSAAKK VEFKEPACNV TFKSEANECT TLIKCTTEHE KLIIRHKDKI
GKYAVYAIWQ PGDTNDYNVT VFQGENRKTF MYKFPFYEMC DITMYMSKQY KLWPPQKCLE
NTGTFCSTAL LITALALVCT LLYLKYKSRR SFIDEKKMP
