ID   APAF_CANLF              Reviewed;          50 AA.
AC   Q9GL23;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Apoptotic protease-activating factor 1;
DE            Short=APAF-1;
DE   Flags: Fragment;
GN   Name=APAF1;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11419353; DOI=10.1046/j.1365-2052.2001.0647j.x;
RA   Debenham S., Ricketts P., Holmes N.G., Thomas R., Breen M., Binns M.;
RT   "Physical and linkage mapping of the canine phosphate carrier (SLC25A3) and
RT   apoptotic activating factor 1 (APAF1) genes to canine chromosome 15.";
RL   Anim. Genet. 32:50-51(2001).
CC   -!- FUNCTION: Oligomeric Apaf-1 mediates the cytochrome c-dependent
CC       autocatalytic activation of pro-caspase 9 (Apaf-3), leading to the
CC       activation of caspase-3 and apoptosis. This activation requires ATP (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. Oligomerizes to a heptameric ring, known as the
CC       apoptosome, upon binding of cytochrome c and dATP. Oligomeric Apaf-1
CC       and pro-caspase-9 bind to each other via their respective NH2-terminal
CC       CARD domains and consecutively mature caspase-9 is released from the
CC       complex. Interacts with APIP (By similarity). Interacts (via CARD and
CC       NACHT domains) with NAIP/BIRC1 (via NACHT domain) (By similarity).
CC       Interacts with CIAO2A (By similarity). {ECO:0000250|UniProtKB:O14727}.
CC   -!- DOMAIN: The CARD domain mediates interaction with APIP.
CC   -!- DOMAIN: The monomeric form is autoinhibited in a closed conformation
CC       through a bound ADP at the nucleotide binding site. Exchange of ADP for
CC       ATP and binding of cytochrome c trigger a large conformational change
CC       where the first WD repeat region swings out, allowing the NB-ARC domain
CC       to rotate and expose the contact areas for oligomerization (By
CC       similarity). {ECO:0000250}.
CC   -!- MISCELLANEOUS: Physiological concentrations of calcium ions negatively
CC       affect the assembly of apoptosome by inhibiting nucleotide exchange in
CC       the monomeric form. {ECO:0000250}.
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DR   EMBL; AJ299439; CAC17122.1; ALT_TERM; Genomic_DNA.
DR   AlphaFoldDB; Q9GL23; -.
DR   SMR; Q9GL23; -.
DR   STRING; 9615.ENSCAFP00000036296; -.
DR   PaxDb; Q9GL23; -.
DR   eggNOG; KOG4155; Eukaryota.
DR   eggNOG; KOG4658; Eukaryota.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Apoptosis; ATP-binding; Calcium; Nucleotide-binding; Reference proteome.
FT   CHAIN           <1..>50
FT                   /note="Apoptotic protease-activating factor 1"
FT                   /id="PRO_0000050843"
FT   DOMAIN          <1..31
FT                   /note="CARD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00046"
FT   DOMAIN          46..>50
FT                   /note="NB-ARC"
FT   NON_TER         1
FT   NON_TER         50
SQ   SEQUENCE   50 AA;  5315 MW;  04352522C41CE342 CRC64;
     ILKKDNYSYI SFYNALIHEG YKDLAALLHS GIPVISSSNG GKDSVGGITS