CATH Domain 3v3kO00
|Functional Family||Caspase 9|
based on mapping to UniProt P55211
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.
-!- Caspase-9 is an initiator caspase, as are caspase-2 (EC 18.104.22.168), caspase-8 (EC 22.214.171.124) and caspase-10 (EC 126.96.36.199). -!- Contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation. -!- An alternatively spliced version of caspase-9 also exists, caspase- 9S, that inhibits apoptosis, similar to the situation found with caspase-2. -!- Phosphorylation of caspase-9 from some species by Akt, a serine- threonine protein kinase, inhibits caspase activity in vitro and caspase activation in vivo. -!- The activity of caspase-9 is increased dramatically upon association with the apoptosome but the enzyme can be activated without proteolytic cleavage. -!- Procaspase-3 is the enzyme's physiological substrate. -!- Belongs to peptidase family C14.
UniProtKB Entries (2)
Escherichia coli O157:H7
Effector protein NleF
Human caspase 9 in complex with bacterial effector protein