ID   IAP_ASFM1               Reviewed;         224 AA.
AC   O11452;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Inhibitor of apoptosis protein;
DE            Short=IAP;
GN   Name=p27; ORFNames=4CL;
OS   African swine fever virus (isolate Tick/South Africa/Wildebeeslaagte
OS   M1/1996) (ASFV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Asfuvirales; Asfarviridae; Asfivirus.
OX   NCBI_TaxID=82816;
OH   NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH   NCBI_TaxID=85517; Phacochoerus aethiopicus (Warthog).
OH   NCBI_TaxID=41426; Phacochoerus africanus (Warthog).
OH   NCBI_TaxID=273792; Potamochoerus larvatus (Bushpig).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9143281; DOI=10.1006/viro.1997.8481;
RA   Neilan J.G., Lu Z., Kutish G.F., Zsak L., Burrage T.G., Borca M.V.,
RA   Carrillo C., Rock D.L.;
RT   "A BIR motif containing gene of African swine fever virus, 4CL, is
RT   nonessential for growth in vitro and viral virulence.";
RL   Virology 230:252-264(1997).
CC   -!- FUNCTION: Prevents 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:0000250|UniProtKB:P69180}.
CC   -!- SUBUNIT: Interacts with subunit p17 of host CASP3.
CC       {ECO:0000250|UniProtKB:P69180}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250|UniProtKB:P69180}.
CC       Virion {ECO:0000250|UniProtKB:P69180}. Note=Probably accumulates in the
CC       perinuclear cytoplasmic viral factories. Found in association with
CC       viral nucleoid. {ECO:0000250|UniProtKB:P69180}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the asfivirus IAP family. {ECO:0000305}.
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DR   EMBL; U91737; AAB58392.1; -; Genomic_DNA.
DR   SMR; O11452; -.
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; IEA:UniProtKB-KW.
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   3: Inferred from homology;
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; Virion; Zinc.
FT   CHAIN           1..224
FT                   /note="Inhibitor of apoptosis protein"
FT                   /id="PRO_0000122381"
FT   REPEAT          29..92
FT                   /note="BIR"
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;  26600 MW;  9151DEF472645A3A CRC64;
     MFPKINTIDP YISLRLFEVK PKYVGYSSVD ARNQSFAIHD IKNYEKFSNA GLFYTSPTEI
     TCYCCGMKFC NWLYEKHPLQ VHAFWSRNCG FMRATLGIIG LKKMIDSYND YYNNEVFVKH
     KNRVYTHKRL EDMGFSKPFM QFILANAFIP PYRKYIHKII LNDRYFTFKF AAHLLSFHKV
     NLDNQTTYCM TCGIEPIKKD ENFCNACKTL NYKHYKTLNF SVKL