ID   ADP_ADE02               Reviewed;         101 AA.
AC   P24935;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   23-FEB-2022, entry version 84.
DE   RecName: Full=Adenovirus death protein;
DE            Short=ADP;
DE   AltName: Full=Early-3 11.6 kDa glycoprotein;
DE            Short=E3-11.6K;
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   IDENTIFICATION, AND SUBCELLULAR LOCATION.
RX   PubMed=1448922; DOI=10.1016/0042-6822(92)90250-s;
RA   Scaria A., Tollefson A.E., Saha S.K., Wold W.S.M.;
RT   "The E3-11.6K protein of adenovirus is an Asn-glycosylated integral
RT   membrane protein that localizes to the nuclear membrane.";
RL   Virology 191:743-753(1992).
RN   [3]
RP   PALMITOYLATION.
RX   PubMed=9601505; DOI=10.1006/viro.1998.9135;
RA   Hausmann J., Ortmann D., Witt E., Veit M., Seidel W.;
RT   "Adenovirus death protein, a transmembrane protein encoded in the E3
RT   region, is palmitoylated at the cytoplasmic tail.";
RL   Virology 244:343-351(1998).
RN   [4]
RP   INTERACTION WITH HOST MAD2L2/MAD2B.
RX   PubMed=12951035; DOI=10.1016/s0042-6822(03)00287-3;
RA   Ying B., Wold W.S.M.;
RT   "Adenovirus ADP protein (E3-11.6K), which is required for efficient cell
RT   lysis and virus release, interacts with human MAD2B.";
RL   Virology 313:224-234(2003).
RN   [5]
RP   FUNCTION.
RC   STRAIN=Human adenovirus C serotype 5;
RX   PubMed=24198418; DOI=10.1128/jvi.01675-13;
RA   Murali V.K., Ornelles D.A., Gooding L.R., Wilms H.T., Huang W.,
RA   Tollefson A.E., Wold W.S., Garnett-Benson C.;
RT   "Adenovirus death protein (ADP) is required for lytic infection of human
RT   lymphocytes.";
RL   J. Virol. 88:903-912(2014).
CC   -!- FUNCTION: Promotes the release of progeny virus from the host cell
CC       nucleus by accelerating the lysis and death of the host cell.
CC       {ECO:0000269|PubMed:24198418}.
CC   -!- SUBUNIT: May interact with host MAD2L2/MAD2B.
CC       {ECO:0000269|PubMed:12951035}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus membrane; Single-pass type I
CC       membrane protein {ECO:0000269|PubMed:1448922}. Host endoplasmic
CC       reticulum membrane; Single-pass type I membrane protein
CC       {ECO:0000269|PubMed:1448922}. Host Golgi apparatus membrane; Single-
CC       pass type I membrane protein {ECO:0000269|PubMed:1448922}.
CC       Note=Initially associates with the endoplasmic reticulum and Golgi
CC       apparatus and ultimately localizes to the nuclear membrane.
CC       {ECO:0000269|PubMed:1448922}.
CC   -!- PTM: Glycosylated by host.
CC   -!- PTM: Palmitoylated at cytoplasmic tail. {ECO:0000269|PubMed:9601505}.
CC   -!- SIMILARITY: Belongs to the adenoviridae ADP family. {ECO:0000305}.
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DR   EMBL; J01917; AAA92222.1; -; Genomic_DNA.
DR   RefSeq; AP_000185.1; AC_000007.1.
DR   RefSeq; NP_040532.1; NC_001405.1.
DR   SMR; P24935; -.
DR   GeneID; 2652987; -.
DR   Proteomes; UP000008167; Genome.
DR   GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0044200; C:host cell nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0044659; P:viral release from host cell by cytolysis; IDA:UniProtKB.
DR   InterPro; IPR008652; Adenovirus_Type-2_E3A.
DR   Pfam; PF05393; Hum_adeno_E3A; 1.
PE   1: Evidence at protein level;
KW   Early protein; Glycoprotein; Host endoplasmic reticulum;
KW   Host Golgi apparatus; Host membrane; Host nucleus; Lipoprotein; Membrane;
KW   Palmitate; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..101
FT                   /note="Adenovirus death protein"
FT                   /id="PRO_0000221736"
FT   TOPO_DOM        1..40
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        41..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        63..101
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        14
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   101 AA;  11644 MW;  FB89FCC6E921E84B CRC64;
     MTGSTIAPTT DYRNTTATGL TSALNLPQVH AFVNDWASLD MWWFSIALMF VCLIIMWLIC
     CLKRRRARPP IYRPIIVLNP HNEKIHRLDG LKPCSLLLQY D