ID   E3GL_ADE03              Reviewed;         172 AA.
AC   P11323;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   23-FEB-2022, entry version 87.
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=Early E3 19.2 kDa glycoprotein;
DE   AltName: Full=GP19K;
DE   Flags: Precursor;
OS   Human adenovirus B serotype 3 (HAdV-3) (Human adenovirus 3).
OC   Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC   Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus B.
OX   NCBI_TaxID=45659;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3582978; DOI=10.1016/0378-1119(86)90322-7;
RA   Signaes C., Akusjaervi G., Pettersson U.;
RT   "Region E3 of human adenoviruses; differences between the oncogenic
RT   adenovirus-3 and the non-oncogenic adenovirus-2.";
RL   Gene 50:173-184(1986).
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   -!- 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; M15952; AAA42483.1; -; Genomic_DNA.
DR   PIR; D29500; ERAD33.
DR   SMR; P11323; -.
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   2: Evidence at transcript level;
KW   Disulfide bond; Early protein; Glycoprotein; Host endoplasmic reticulum;
KW   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..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..172
FT                   /note="Early E3 18.5 kDa glycoprotein"
FT                   /id="PRO_0000036483"
FT   TOPO_DOM        20..136
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        137..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        158..172
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOTIF           168..172
FT                   /note="Di-lysine motif"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        36
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        68
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        72
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        102
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        37..55
FT                   /evidence="ECO:0000250"
FT   DISULFID        49..111
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   172 AA;  19239 MW;  E63ABB427092B295 CRC64;
     MGAILVVLAL LSLLGLGSAN LNPLDHDPCL DFDPENCTLT FAPDTSRLCG VLIKCGWDCR
     SVEITHNNKT WNNTLSTTWE PGVPQWYTVS VRGPDGSIRI SNNTFIFSEM CDLAMFMSRQ
     YDLWPPSKEN IVAFSIAYCL VTCIITAIIC VCIHLLIVIR PRQSNEEKEK MP