E3CR1_ADE02
ID E3CR1_ADE02 Reviewed; 61 AA.
AC Q910M3;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Early 3 Conserved Region 1-alpha protein;
DE Short=E3 CR1-alpha;
DE AltName: Full=Early 3 6.7K protein;
DE Short=E3-6.7k;
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].
RC STRAIN=134, 352, 358, Prei, and R05;
RA Borcherding F., Pring-Akerblom P.;
RT "Adenoviruses of subgenus c with different organ tropism.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP CHARACTERIZATION.
RX PubMed=1697127; DOI=10.1016/0042-6822(90)90395-8;
RA Wilson-Rawls J., Saha S.K., Krajcsi P., Tollefson A.E., Gooding L.R.,
RA Wold W.S.;
RT "A 6700 MW membrane protein is encoded by region E3 of adenovirus type 2.";
RL Virology 178:204-212(1990).
RN [3]
RP SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX PubMed=8317108; DOI=10.1006/viro.1993.1341;
RA Wilson-Rawls J., Wold W.S.;
RT "The E3-6.7K protein of adenovirus is an Asn-linked integral membrane
RT glycoprotein localized in the endoplasmic reticulum.";
RL Virology 195:6-15(1993).
RN [4]
RP INTERACTION WITH E3 RID ALPHA AND E3 RID BETA, AND SUBCELLULAR LOCATION.
RX PubMed=11050095; DOI=10.1074/jbc.m008218200;
RA Benedict C.A., Norris P.S., Prigozy T.I., Bodmer J.L., Mahr J.A.,
RA Garnett C.T., Martinon F., Tschopp J., Gooding L.R., Ware C.F.;
RT "Three adenovirus E3 proteins cooperate to evade apoptosis by tumor
RT necrosis factor-related apoptosis-inducing ligand receptor-1 and -2.";
RL J. Biol. Chem. 276:3270-3278(2001).
RN [5]
RP FUNCTION.
RX PubMed=15507617; DOI=10.1128/jvi.78.22.12297-12307.2004;
RA Lichtenstein D.L., Doronin K., Toth K., Kuppuswamy M., Wold W.S.,
RA Tollefson A.E.;
RT "Adenovirus E3-6.7K protein is required in conjunction with the E3-RID
RT protein complex for the internalization and degradation of TRAIL receptor
RT 2.";
RL J. Virol. 78:12297-12307(2004).
RN [6]
RP FUNCTION.
RX PubMed=17538121; DOI=10.1128/cvi.00058-07;
RA Grant J.R., Moise A.R., Jefferies W.A.;
RT "Identification of a novel immunosubversion mechanism mediated by a
RT virologue of the B-lymphocyte receptor TACI.";
RL Clin. Vaccine Immunol. 14:907-917(2007).
RN [7]
RP REVIEW.
RX PubMed=14690856; DOI=10.1080/08830180490265556;
RA Lichtenstein D.L., Toth K., Doronin K., Tollefson A.E., Wold W.S.;
RT "Functions and mechanisms of action of the adenovirus E3 proteins.";
RL Int. Rev. Immunol. 23:75-111(2004).
RN [8]
RP REVIEW.
RX PubMed=14674598; DOI=10.1007/978-3-662-05599-1_2;
RA Windheim M., Hilgendorf A., Burgert H.G.;
RT "Immune evasion by adenovirus E3 proteins: exploitation of intracellular
RT trafficking pathways.";
RL Curr. Top. Microbiol. Immunol. 273:29-85(2004).
CC -!- FUNCTION: Prevents infected cell apoptosis induced by the host immune
CC system. May act by down-regulating host TRAIL receptors. May act in
CC complex with E3 RID alpha and beta. May play a role on cellular
CC apoptosis regulation in the ER. {ECO:0000269|PubMed:15507617,
CC ECO:0000269|PubMed:17538121}.
CC -!- SUBUNIT: Interacts with E3 RID alpha and E3 RID beta.
CC {ECO:0000269|PubMed:11050095}.
CC -!- SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane; Single-pass
CC membrane protein. Host cell membrane; Single-pass membrane protein.
CC -!- PTM: Only 1 of 3 three potential glycosylation sites is glycosylated.
CC Oligosaccharides are not processed from high mannose to the complex
CC type because the protein is retained in the endoplasmic reticulum.
CC {ECO:0000269|PubMed:8317108}.
CC -!- SIMILARITY: Belongs to the adenoviridae E3-CR1 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; AJ293912; CAC67694.1; -; Genomic_DNA.
DR EMBL; AJ293913; CAC67702.1; -; Genomic_DNA.
DR EMBL; AJ293914; CAC67711.1; -; Genomic_DNA.
DR EMBL; AJ293916; CAC67727.1; -; Genomic_DNA.
DR EMBL; AJ293917; CAC67735.1; -; Genomic_DNA.
DR RefSeq; AP_000183.1; AC_000007.1.
DR SMR; Q910M3; -.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Glycoprotein; Host cell membrane; Host endoplasmic reticulum;
KW Host membrane; Host-virus interaction; Membrane; Transmembrane;
KW Transmembrane helix; Viral immunoevasion.
FT CHAIN 1..61
FT /note="Early 3 Conserved Region 1-alpha protein"
FT /id="PRO_0000421688"
FT TOPO_DOM 1..14
FT /note="Lumenal"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..61
FT /note="Cytoplasmic"
FT CARBOHYD 3
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 6
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 12
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 61 AA; 6671 MW; 7DE0079C6DB01A43 CRC64;
MSNSSNSTSL SNFSGIGVGV ILTLVILFIL ILALLCLRVA ACCTHVCTYC QLFKRWGQHP
R
