ID   IAP_ASFB7               Reviewed;         224 AA.
AC   P69180; O12627; O12628; O12629; O12630; O12631; O12904; O12905; O12906;
AC   O12907; O12908; Q65138;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Inhibitor of apoptosis protein;
DE            Short=IAP;
GN   OrderedLocusNames=BA71V-032; ORFNames=4CL, A224L;
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   INDUCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=8553574; DOI=10.1006/viro.1995.0083;
RA   Chacon M.R., Almazan F., Nogal M.L., Vinuela E., Rodriguez J.F.;
RT   "The African swine fever virus IAP homolog is a late structural
RT   polypeptide.";
RL   Virology 214:670-674(1995).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH HOST CASP3.
RX   PubMed=11222676; DOI=10.1128/jvi.75.6.2535-2543.2001;
RA   Nogal M.L., Gonzalez de Buitrago G., Rodriguez C., Cubelos B.,
RA   Carrascosa A.L., Salas M.L., Revilla Y.;
RT   "African swine fever virus IAP homologue inhibits caspase activation and
RT   promotes cell survival in mammalian cells.";
RL   J. Virol. 75:2535-2543(2001).
RN   [4]
RP   FUNCTION.
RX   PubMed=11907233; DOI=10.1128/jvi.76.8.3936-3942.2002;
RA   Rodriguez C.I., Nogal M.L., Carrascosa A.L., Salas M.L., Fresno M.,
RA   Revilla Y.;
RT   "African swine fever virus IAP-like protein induces the activation of
RT   nuclear factor kappa B.";
RL   J. Virol. 76:3936-3942(2002).
RN   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=30185597; DOI=10.1128/jvi.01293-18;
RA   Alejo A., Matamoros T., Guerra M., Andres G.;
RT   "A Proteomic Atlas of the African Swine Fever Virus Particle.";
RL   J. Virol. 92:0-0(2018).
CC   -!- FUNCTION: Prevent apoptosis of host cell by inhibiting caspase-3/CASP3
CC       activation to promote the viral replication. Induces also the
CC       activation of host NF-kappaB. {ECO:0000269|PubMed:11222676,
CC       ECO:0000269|PubMed:11907233}.
CC   -!- SUBUNIT: Interacts with subunit p17 of host CASP3.
CC       {ECO:0000269|PubMed:11222676}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:8553574}.
CC       Virion {ECO:0000269|PubMed:30185597}. Note=Probably accumulates in the
CC       perinuclear cytoplasmic viral factories. Found in association with
CC       viral nucleoid (PubMed:30185597). {ECO:0000269|PubMed:30185597}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC       {ECO:0000269|PubMed:8553574}.
CC   -!- SIMILARITY: Belongs to the asfivirus IAP family. {ECO:0000305}.
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DR   EMBL; U18466; AAA65263.1; -; Genomic_DNA.
DR   RefSeq; NP_042727.1; NC_001659.2.
DR   SMR; P69180; -.
DR   GeneID; 22220415; -.
DR   KEGG; vg:22220415; -.
DR   Proteomes; UP000000624; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0039652; P:induction by virus of host NF-kappaB cascade; IEA:UniProtKB-KW.
DR   GO; GO:0039650; P:suppression by virus of host cysteine-type endopeptidase activity involved in apoptotic process; IDA:CACAO.
DR   CDD; cd00022; BIR; 1.
DR   InterPro; IPR010549; ASFV_p27_C.
DR   InterPro; IPR001370; BIR_rpt.
DR   Pfam; PF06556; ASFV_p27; 1.
DR   Pfam; PF00653; BIR; 1.
DR   SMART; SM00238; BIR; 1.
DR   PROSITE; PS01282; BIR_REPEAT_1; 1.
DR   PROSITE; PS50143; BIR_REPEAT_2; 1.
PE   1: Evidence at protein level;
KW   Activation of host NF-kappa-B by virus; Host cytoplasm;
KW   Host-virus interaction; Inhibition of host caspases by virus; Late protein;
KW   Metal-binding; Modulation of host cell apoptosis by virus;
KW   Reference proteome; Virion; Zinc; Zinc-finger.
FT   CHAIN           1..224
FT                   /note="Inhibitor of apoptosis protein"
FT                   /id="PRO_0000122373"
FT   REPEAT          29..92
FT                   /note="BIR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT   ZN_FING         189..207
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255"
FT   BINDING         62
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT   BINDING         65
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT   BINDING         82
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT   BINDING         89
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
SQ   SEQUENCE   224 AA;  26618 MW;  49E81A325EDA00C9 CRC64;
     MFPKINTIDP YISLRLFEVK PKYVGYSSID ARNQSFAIHG IKNYEKFSNA GFFYTSPTEI
     TCYCCGMKFC NWLYEKHPLQ VHGFWSRNCG FMRATLGIIG LKKMIDSYND YYNNEVFVKH
     KNRVYTHKRL EDMGFSKPFM RFILANAFIP PYRKYIHKII LNERYFTFKF AAHLLSFHKV
     NLDNQTTYCM TCGIEPIKKD ENFCNACKTL NYKHYKTLNF SVKL