ID   3.4.22.63
DE   caspase-10.
AN   apoptotic protease Mch-4.
AN   CASP-10.
AN   FAS-associated death domain protein interleukin-1beta-converting enzyme
AN   2.
AN   FLICE2.
AN   ICE-like apoptotic protease 4.
AN   Mch4.
CA   Strict requirement for Asp at position P1 and has a preferred cleavage
CA   sequence of Leu-Gln-Thr-Asp-|-Gly.
CC   -!- Caspase-10 is an initiator caspase, as are caspase-2 (EC 3.4.22.55),
CC       caspase-8 (EC 3.4.22.61) and caspase-9 (EC 3.4.22.62).
CC   -!- Like caspase-8, it contains two tandem death effector domains (DEDs)
CC       in its N-terminal prodomain, which play a role in procaspase
CC       activation.
CC   -!- Has many overlapping substrates in common with caspase-8, such as RIP
CC       (the cleavage of which impairs NF-kappaB survival signaling and
CC       starts the cell-death process) and PAK2 (associated with some of the
CC       morphological features of apoptosis, such as cell rounding and
CC       apoptotic body formation).
CC   -!- Bid, a Bcl2 protein, can be cleaved by caspase-3 (EC 3.4.22.56),
CC       caspase-8 and caspase-10 at Lys-Gln-Thr-Asp-|- to yield the pro-
CC       apoptotic p15 fragment.
CC   -!- The p15 fragment is N-myristoylated and enhances cytochrome c release
CC       from mitochondria (which initiatiates the intrinsic apoptosis
CC       pathway).
CC   -!- Bid can be further cleaved by caspase-10 and granzyme B but not by
CC       caspase-3 and caspase-8 at Ile-Glu-Thr-Asp-|- to yield a p13 fragment
CC       that is not N-myristoylated.
CC   -!- Belongs to peptidase family C14.
DR   Q92851, CASPA_HUMAN;
//