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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
 
 
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