Caspase-10

Definition:

EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.22 Cysteine endopeptidases > 3.4.22.63 caspase-10
Caspase-10 is an initiator caspase, together with caspase-2 (EC 3.4.22.55), caspase-8 (EC 3.4.22.61) and caspase-9 (EC 3.4.22.62). Like caspase-8, it contains two tandem death-effector domains (DEDs) in its N-terminal prodomain for procaspase activation. It shares many substrates with caspase-8, such as RIP, whose cleavage impairs NF-kappaB signaling. It has a strict requirement for Asp at P1 and a preferred cleavage sequence Leu-Gln-Thr-Asp-/-Gly. In cells it participates in death-receptor and extrinsic apoptosis signaling. It features DED domains fused to a p23/p12 catalytic heterodimer.

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