DPV22_DPV83
ID DPV22_DPV83 Reviewed; 179 AA.
AC Q08FX8;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 29-SEP-2021, entry version 45.
DE RecName: Full=Apoptosis regulator DPV022;
GN Name=DPV022;
OS Deerpox virus (strain Mule deer/United States/W-848-83/1983) (DPV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Cervidpoxvirus.
OX NCBI_TaxID=305674 {ECO:0000312|Proteomes:UP000000866};
OH NCBI_TaxID=9872; Odocoileus hemionus (Mule deer) (Cervus hemionus).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15613325; DOI=10.1128/jvi.79.2.966-977.2005;
RA Afonso C.L., Delhon G., Tulman E.R., Lu Z., Zsak A., Becerra V.M., Zsak L.,
RA Kutish G.F., Rock D.L.;
RT "Genome of deerpox virus.";
RL J. Virol. 79:966-977(2005).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HOST BAX AND BAK1.
RX PubMed=21159883; DOI=10.1128/jvi.01959-10;
RA Banadyga L., Lam S.C., Okamoto T., Kvansakul M., Huang D.C., Barry M.;
RT "Deerpox virus encodes an inhibitor of apoptosis that regulates Bak and
RT Bax.";
RL J. Virol. 85:1922-1934(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-155.
RX PubMed=26249341; DOI=10.1107/s1399004715009402;
RA Burton D.R., Caria S., Marshall B., Barry M., Kvansakul M.;
RT "Structural basis of Deerpox virus-mediated inhibition of apoptosis.";
RL Acta Crystallogr. D 71:1593-1603(2015).
CC -!- FUNCTION: Plays a role in the inhibition of host apoptosis by
CC sequestering and inactivating several proapoptotic BCL-2 proteins,
CC including BAK1 and BAX. Prevents the conformational activation of both
CC of them. {ECO:0000269|PubMed:21159883}.
CC -!- SUBUNIT: Interacts with host BAX and BAK1.
CC -!- SUBCELLULAR LOCATION: Host mitochondrion {ECO:0000269|PubMed:21159883}.
CC Host membrane {ECO:0000255}; Single-pass membrane protein
CC {ECO:0000255}.
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DR EMBL; AY689436; ABI99179.1; -; Genomic_DNA.
DR RefSeq; YP_227399.1; NC_006966.1.
DR PDB; 4UF1; X-ray; 2.30 A; A=1-155.
DR PDB; 4UF2; X-ray; 3.00 A; A=1-155.
DR PDB; 4UF3; X-ray; 2.70 A; A=1-155.
DR PDBsum; 4UF1; -.
DR PDBsum; 4UF2; -.
DR PDBsum; 4UF3; -.
DR SMR; Q08FX8; -.
DR GeneID; 3346328; -.
DR KEGG; vg:3346328; -.
DR Proteomes; UP000000866; Genome.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033650; C:host cell mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019050; P:suppression by virus of host apoptotic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.437.10; -; 1.
DR InterPro; IPR036834; Bcl-2-like_sf.
DR InterPro; IPR021119; Poxvirus_F1/C10.
DR Pfam; PF11099; M11L; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Host membrane; Host mitochondrion; Host-virus interaction;
KW Inhibition of host apoptosis by viral BCL2-like protein; Membrane;
KW Modulation of host cell apoptosis by virus; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..179
FT /note="Apoptosis regulator DPV022"
FT /id="PRO_0000443231"
FT TRANSMEM 148..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT HELIX 8..29
FT /evidence="ECO:0007829|PDB:4UF1"
FT HELIX 33..52
FT /evidence="ECO:0007829|PDB:4UF1"
FT HELIX 54..64
FT /evidence="ECO:0007829|PDB:4UF1"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:4UF1"
FT HELIX 71..84
FT /evidence="ECO:0007829|PDB:4UF1"
FT HELIX 88..104
FT /evidence="ECO:0007829|PDB:4UF1"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:4UF3"
FT HELIX 111..117
FT /evidence="ECO:0007829|PDB:4UF1"
FT HELIX 120..126
FT /evidence="ECO:0007829|PDB:4UF1"
FT HELIX 129..136
FT /evidence="ECO:0007829|PDB:4UF1"
SQ SEQUENCE 179 AA; 20874 MW; 70C945A76AF3907F CRC64;
MEAAIEFDEI VKKLLNIYIN DICTMGEKRL LNNYEKSILD RIYKSCEYIK KNYELDFNSM
YNQININDIT TSDIKSKIIE SLLIDSRPSV KLATLSFISL IAEKWGEKNR TKIMEILSNE
IVEKISNNGK DFIDFIDRDD DDIVDDYVLI TNYLKITIFG AILGITAYYI CKYLLKSIF