ARBH_ASFB7
ID ARBH_ASFB7 Reviewed; 179 AA.
AC P42485;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Apoptosis regulator Bcl-2 homolog;
GN OrderedLocusNames=Ba71V-041; ORFNames=A179L;
OS African swine fever virus (strain Badajoz 1971 Vero-adapted) (Ba71V)
OS (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=10498;
OH NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11831707; DOI=10.1006/viro.1995.1149;
RA Yanez R.J., Rodriguez J.M., Nogal M.L., Yuste L., Enriquez C.,
RA Rodriguez J.F., Vinuela E.;
RT "Analysis of the complete nucleotide sequence of African swine fever
RT virus.";
RL Virology 208:249-278(1995).
RN [2]
RP FUNCTION, AND MUTAGENESIS OF GLY-85.
RX PubMed=9123849; DOI=10.1006/viro.1996.8395;
RA Revilla Y., Cebrian A., Baixeras E., Martinez C., Vinuela E., Salas M.L.;
RT "Inhibition of apoptosis by the African swine fever virus Bcl-2 homologue:
RT role of the BH1 domain.";
RL Virology 228:400-404(1997).
RN [3]
RP FUNCTION.
RX PubMed=18329683; DOI=10.1016/j.virol.2008.01.050;
RA Galindo I., Hernaez B., Diaz-Gil G., Escribano J.M., Alonso C.;
RT "A179L, a viral Bcl-2 homologue, targets the core Bcl-2 apoptotic machinery
RT and its upstream BH3 activators with selective binding restrictions for Bid
RT and Noxa.";
RL Virology 375:561-572(2008).
RN [4]
RP INTERACTION WITH HOST BECN1, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=23228131; DOI=10.2174/156652413804810736;
RA Hernaez B., Cabezas M., Munoz-Moreno R., Galindo I., Cuesta-Geijo M.A.,
RA Alonso C.;
RT "A179L, a new viral Bcl2 homolog targeting Beclin 1 autophagy related
RT protein.";
RL Curr. Mol. Med. 13:305-316(2013).
RN [5]
RP INDUCTION.
RX PubMed=32075923; DOI=10.1128/jvi.00119-20;
RA Cackett G., Matelska D., Sykora M., Portugal R., Malecki M., Baehler J.,
RA Dixon L., Werner F.;
RT "The African Swine Fever Virus Transcriptome.";
RL J. Virol. 94:0-0(2020).
RN [6] {ECO:0007744|PDB:5UA4, ECO:0007744|PDB:5UA5}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1-148, INTERACTION WITH HOST BID,
RP INTERACTION WITH HOST BAX, AND FUNCTION.
RX PubMed=28053104; DOI=10.1128/jvi.02228-16;
RA Banjara S., Caria S., Dixon L.K., Hinds M.G., Kvansakul M.;
RT "Structural insight into African swine fever virus A179L-mediated
RT inhibition of apoptosis.";
RL J. Virol. 91:0-0(2017).
RN [7] {ECO:0007744|PDB:6TZC}
RP X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) OF 1-148, FUNCTION, INTERACTION WITH
RP HOST BECN1, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=31461953; DOI=10.3390/v11090789;
RA Banjara S., Shimmon G.L., Dixon L.K., Netherton C.L., Hinds M.G.,
RA Kvansakul M.;
RT "Crystal Structure of African Swine Fever Virus A179L with the Autophagy
RT Regulator Beclin.";
RL Viruses 11:0-0(2019).
CC -!- FUNCTION: Suppresses apoptosis in host cell to promote the viral
CC replication (PubMed:18329683, PubMed:9123849). Has the ability to
CC potentially bind to all the members of the proapoptotic Bcl-2 family
CC (PubMed:18329683, PubMed:28053104). Inhibits autophagy by interacting
CC with host Beclin 1 (BECN1) (PubMed:23228131, PubMed:31461953).
CC {ECO:0000269|PubMed:18329683, ECO:0000269|PubMed:23228131,
CC ECO:0000269|PubMed:28053104, ECO:0000269|PubMed:31461953,
CC ECO:0000269|PubMed:9123849}.
CC -!- SUBUNIT: Interacts with host BECN1 (via BH3 homology domain); this
CC interaction allows the virus to inhibit BECN1, and thus autophagy
CC (PubMed:23228131, PubMed:31461953). Interacts with host BID
CC (PubMed:28053104). Interacts with host BAX (PubMed:28053104).
CC {ECO:0000269|PubMed:23228131, ECO:0000269|PubMed:28053104,
CC ECO:0000269|PubMed:31461953}.
CC -!- SUBCELLULAR LOCATION: Host mitochondrion {ECO:0000269|PubMed:23228131}.
CC Host endoplasmic reticulum {ECO:0000269|PubMed:23228131}.
CC -!- INDUCTION: Expressed in the early phase of the viral replicative cycle
CC (PubMed:32075923). Expressed in the late phase of the viral replicative
CC cycle (By similarity). {ECO:0000250|UniProtKB:Q07819,
CC ECO:0000269|PubMed:32075923}.
CC -!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
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DR EMBL; U18466; AAA65271.1; -; Genomic_DNA.
DR RefSeq; NP_042735.1; NC_001659.2.
DR PDB; 5UA4; X-ray; 2.60 A; A=1-148.
DR PDB; 5UA5; X-ray; 2.50 A; A=1-148.
DR PDB; 6TZC; X-ray; 2.41 A; B=1-148.
DR PDBsum; 5UA4; -.
DR PDBsum; 5UA5; -.
DR PDBsum; 6TZC; -.
DR SMR; P42485; -.
DR GeneID; 22220423; -.
DR KEGG; vg:22220423; -.
DR Proteomes; UP000000624; Genome.
DR GO; GO:0044165; C:host cell endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0033650; C:host cell mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0019050; P:suppression by virus of host apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0039521; P:suppression by virus of host autophagy; IEA:UniProtKB-KW.
DR Gene3D; 1.10.437.10; -; 1.
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 InterPro; IPR020717; Bcl2_BH1_motif_CS.
DR InterPro; IPR020726; Bcl2_BH2_motif_CS.
DR PANTHER; PTHR11256; PTHR11256; 1.
DR Pfam; PF00452; Bcl-2; 1.
DR PRINTS; PR01862; BCL2FAMILY.
DR SMART; SM00337; BCL; 1.
DR SUPFAM; SSF56854; SSF56854; 1.
DR PROSITE; PS50062; BCL2_FAMILY; 1.
DR PROSITE; PS01080; BH1; 1.
DR PROSITE; PS01258; BH2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Early protein; Host endoplasmic reticulum;
KW Host mitochondrion; Host-virus interaction;
KW Inhibition of host apoptosis by viral BCL2-like protein;
KW Inhibition of host autophagy by virus; Late protein;
KW Modulation of host cell apoptosis by virus; Reference proteome.
FT CHAIN 1..179
FT /note="Apoptosis regulator Bcl-2 homolog"
FT /id="PRO_0000002811"
FT MOTIF 76..95
FT /note="BH1"
FT /evidence="ECO:0000255"
FT MOTIF 126..141
FT /note="BH2"
FT /evidence="ECO:0000255"
FT MUTAGEN 85
FT /note="G->A: Complete loss of apoptosis suppression."
FT /evidence="ECO:0000269|PubMed:9123849"
FT HELIX 4..15
FT /evidence="ECO:0007829|PDB:6TZC"
FT HELIX 17..23
FT /evidence="ECO:0007829|PDB:6TZC"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:5UA5"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:6TZC"
FT HELIX 34..53
FT /evidence="ECO:0007829|PDB:6TZC"
FT HELIX 63..79
FT /evidence="ECO:0007829|PDB:6TZC"
FT HELIX 84..104
FT /evidence="ECO:0007829|PDB:6TZC"
FT HELIX 109..123
FT /evidence="ECO:0007829|PDB:6TZC"
FT HELIX 125..130
FT /evidence="ECO:0007829|PDB:6TZC"
FT HELIX 133..144
FT /evidence="ECO:0007829|PDB:6TZC"
SQ SEQUENCE 179 AA; 21075 MW; 62CB13D82374BF35 CRC64;
MEGEELIYHN IINEILVGYI KYYINDISEH ELSPYQQQIK KILTYYDECL NKQVTITFSL
TSVQEIKTQF TGVVTELFKD LINWGRICGF IVFSAKMAKY CKDANNHLES TVITTAYNFM
KHNLLPWMIS HGGQEEFLAF SLHSDMYSVI FNIKYFLSKF CNHMFFRSCV QLLRNCNLI
