ID   E3GL_ADE35              Reviewed;         166 AA.
AC   P68981; P15140; P35772;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   23-FEB-2022, entry version 64.
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 B serotype 35 (HAdV-35) (Human adenovirus 35).
OC   Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC   Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus B.
OX   NCBI_TaxID=10522;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Holden;
RX   PubMed=3172347; DOI=10.1128/jvi.62.11.4431-4437.1988;
RA   Flomenberg P.R., Chen M., Horwitz M.S.;
RT   "Sequence and genetic organization of adenovirus type 35 early region 3.";
RL   J. Virol. 62:4431-4437(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION TO 46-53.
RC   STRAIN=Holden;
RX   PubMed=8666254; DOI=10.1016/0378-1119(95)00898-5;
RA   Basler C.F., Droguett G., Horwitz M.S.;
RT   "Sequence of the immunoregulatory early region 3 and flanking sequences of
RT   adenovirus type 35.";
RL   Gene 170:249-254(1996).
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}.
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DR   EMBL; M23195; AAA42435.1; -; Genomic_DNA.
DR   EMBL; U32664; AAA75325.1; -; Genomic_DNA.
DR   PIR; JC4768; ERAD85.
DR   RefSeq; AP_000594.1; AC_000019.1.
DR   SMR; P68981; -.
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..166
FT                   /note="Early E3 18.5 kDa glycoprotein"
FT                   /id="PRO_0000036488"
FT   TOPO_DOM        20..131
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        132..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        153..166
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOTIF           162..166
FT                   /note="Di-lysine motif"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        31
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        63
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        67
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        97
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        32..50
FT                   /evidence="ECO:0000250"
FT   DISULFID        44..106
FT                   /evidence="ECO:0000250"
FT   CONFLICT        46..53
FT                   /note="VLIKCGWE -> FLLSADGK (in Ref. 1; AAA42435)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   166 AA;  18576 MW;  D99C6325FBBE178D CRC64;
     MGPILVLLVL LSLLEPGSAN YDPCLDFDPE NCTLTFAPDT SRICGVLIKC GWECRSVEIT
     HNNKTWNNTL STTWEPGVPE WYTVSVRGPD GSIRISNNTF IFSEMCDLAM FMSKQYSLWP
     PSKDNIVTFS IAYCLCACLL TALLCVCIHL LVTTRIKNAN NKEKMP