Catalytic activity:Strict requirement for an Asp residue at position P1 and with a marked preference for His at position P2. It has a preferred cleavage sequence of Leu-Gly-His-Asp-|-Xaa. ,Function:Involved in the activation cascade of caspases responsible for apoptosis execution. Binding of caspase-9 to Apaf-1 leads to activation of the protease which then cleaves and activates caspase-3. Proteolytically cleaves poly (ADP-ribose) polymerase (PARP) . ,Function:Isoform 2 lacks activity is an dominant-negative inhibitor of caspase-9. ,online information:Caspase-9 entry ,PTM:Cleavages at Asp-315 by granzyme B and at Asp-330 by caspase-3 generate the two active subunits. Caspase-8 and -10 can also be involved in these processing events. ,similarity:Belongs to the peptidase C14A family. ,similarity:Contains 1 CARD domain. ,subunit:Heterotetramer that consists of two anti-parallel arranged heterodimers , each one formed by a 35 kDa (p35) and a 10 kDa (p10) subunit. Caspase-9 and APAF1 bind to each other via their respective NH2-terminal CED-3 homologous domains in the presence of cytochrome C and ATP. Interacts with the inhibitors BIRC2 , BIRC4 , BIRC5 and BIRC7. ,tissue specificity:Ubiquitous , with highest expression in the heart , moderate expression in liver , skeletal muscle , and pancreas. Low levels in all other tissues. ,
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