Involved in the activation cascade of caspases responsible for apoptosis execution. Recruited to both Fas- and TNFR-1 receptors in a FADD dependent manner. May participate in the granzyme B apoptotic pathways. Cleaves and activates caspase-3, -4, -6, -7, -8, and -9. Hydrolyzes the small- molecule substrates, Tyr-Val-Ala-Asp-|-AMC and Asp-Glu-Val-Asp-|-AMC. Isoform 7 can enhance NF-kappaB activity but promotes only slight apoptosis. Isoform C is proteolytically inactive. Strict requirement for Asp at position P1 and has a preferred cleavage sequence of Leu-Gln-Thr-Asp-|-Gly. Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 23/17 kDa (p23/17) (depending on the splicing events) and a 12 kDa (p12) subunit (By similarity). Self-associates. Interacts with FADD and CASP8. Found in a Fas signaling complex consisting of FAS, FADD, CASP8 and CASP10. Interacts with RFFL and RNF34; negatively regulate CASP10 through proteasomal degradation. Interacts with RIOK3. Detectable in most tissues. Lowest expression is seen in brain, kidney, prostate, testis and colon. Cleavage by granzyme B and autocatalytic activity generate the two active subunits. The disease is caused by variants affecting the gene represented in this entry. The gene represented in this entry is involved in disease pathogenesis. The gene represented in this entry is involved in disease pathogenesis. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. Belongs to the peptidase C14A family. CASP10 mutation db Caspase-10 mutations causing ALPS type II