DPP8
Function
Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2 (PubMed:11012666, PubMed:12534281, PubMed:12662155, PubMed:15039077, PubMed:15664838, PubMed:20536396, PubMed:29382749). Acts as a key inhibitor of caspase-1-dependent monocyte and macrophage pyroptosis in resting cells by preventing activation of NLRP1 and CARD8 (PubMed:27820798, PubMed:29967349, PubMed:32796818). Sequesters the cleaved C-terminal part of NLRP1 and CARD8, which respectively constitute the active part of the NLRP1 and CARD8 inflammasomes, in a ternary complex, thereby preventing their oligomerization and activation (PubMed:33731929, PubMed:33731932, PubMed:34019797). The dipeptidyl peptidase activity is required to suppress NLRP1 and CARD8; however, neither NLRP1 nor CARD8 are bona fide substrates of DPP8, suggesting the existence of substrate(s) required for NLRP1 and CARD8 inhibition (By similarity).
Sequence Similarities
Belongs to the peptidase S9B family. DPPIV subfamily.
Tissue Specificity
Ubiquitously expressed, with highest levels in testis, placenta, prostate, muscle and brain.
Cellular localization
- Cytoplasm
Alternative names
DPRP1, MSTP097, MSTP135, MSTP141, DPP8, Dipeptidyl peptidase 8, DP8, Dipeptidyl peptidase IV-related protein 1, Dipeptidyl peptidase VIII, Prolyl dipeptidase DPP8, DPRP-1, DPP VIII