ARBH_CNPV
ID ARBH_CNPV Reviewed; 175 AA.
AC Q6VZT9;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=Apoptosis regulator Bcl-2 homolog;
DE Short=vBcl-2;
GN Name=CNPV058;
OS Canarypox virus (CNPV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Avipoxvirus.
OX NCBI_TaxID=44088;
OH NCBI_TaxID=9134; Serinus.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14671117; DOI=10.1128/jvi.78.1.353-366.2004;
RA Tulman E.R., Afonso C.L., Lu Z., Zsak L., Kutish G.F., Rock D.L.;
RT "The genome of canarypox virus.";
RL J. Virol. 78:353-366(2004).
RN [2]
RP FUNCTION, AND INTERACTION WITH HOST BAK1 AND BAX.
RX PubMed=29053589; DOI=10.3390/v9100305;
RA Anasir M.I., Baxter A.A., Poon I.K.H., Hulett M.D., Kvansakul M.;
RT "Structural and functional insight into canarypox virus CNP058 mediated
RT regulation of apoptosis.";
RL Viruses 9:0-0(2017).
CC -!- FUNCTION: Plays a role in the inhibition of host apoptosis. Interacts
CC with host proapoptotic factors BAK1 and BAX to supposedly prevent their
CC activation. {ECO:0000269|PubMed:29053589}.
CC -!- SUBUNIT: Interacts with host BAK1 and BAX as well as other BH3-
CC containing proteins including BIM, BID or PUMA.
CC {ECO:0000269|PubMed:29053589}.
CC -!- SUBCELLULAR LOCATION: Host membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
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DR EMBL; AY318871; AAR83404.1; -; Genomic_DNA.
DR RefSeq; NP_955081.1; NC_005309.1.
DR PDB; 5WOS; X-ray; 2.45 A; A=1-143.
DR PDBsum; 5WOS; -.
DR SMR; Q6VZT9; -.
DR GeneID; 2700183; -.
DR KEGG; vg:2700183; -.
DR Proteomes; UP000168164; Genome.
DR GO; GO:0033644; C:host cell membrane; 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; IPR013281; Apop_reg_Mc1.
DR InterPro; IPR036834; Bcl-2-like_sf.
DR InterPro; IPR046371; Bcl-2_BH1-3.
DR InterPro; IPR026298; Bcl-2_fam.
DR InterPro; IPR002475; Bcl2-like.
DR PANTHER; PTHR11256; PTHR11256; 1.
DR PANTHER; PTHR11256:SF46; PTHR11256:SF46; 1.
DR Pfam; PF00452; Bcl-2; 1.
DR SUPFAM; SSF56854; SSF56854; 1.
DR PROSITE; PS50062; BCL2_FAMILY; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Host membrane; 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..175
FT /note="Apoptosis regulator Bcl-2 homolog"
FT /id="PRO_0000443228"
FT TRANSMEM 152..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT HELIX 9..27
FT /evidence="ECO:0007829|PDB:5WOS"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:5WOS"
FT HELIX 38..64
FT /evidence="ECO:0007829|PDB:5WOS"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:5WOS"
FT HELIX 73..81
FT /evidence="ECO:0007829|PDB:5WOS"
FT HELIX 87..107
FT /evidence="ECO:0007829|PDB:5WOS"
FT TURN 110..115
FT /evidence="ECO:0007829|PDB:5WOS"
FT HELIX 116..133
FT /evidence="ECO:0007829|PDB:5WOS"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:5WOS"
FT HELIX 137..141
FT /evidence="ECO:0007829|PDB:5WOS"
SQ SEQUENCE 175 AA; 20745 MW; 486BED45D42C90C4 CRC64;
MDPSVKKDEI YYTILNIIQN YFIEYCTGKN RNFHVEDENT YIIVKNMCDI ILRDNIVEFR
KDIDRCSDIE NEIPEIVYDT IHDKITWGRV ISIIAFGAYV TKVFKEKGRD NVVDLMPDII
TESLLSRCRS WLSDQNCWDG LKAYVYNNKK FYYVTRYFRV AAFIITSLAV INLFL