| Function | Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. Acts as a key inhibitor of caspase-1-dependent monocyte and macrophage pyroptosis in resting cells by preventing activation of NLRP1 and CARD8. 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. 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. |
| Protein Name | Dipeptidyl Peptidase 8Dp8Dipeptidyl Peptidase Iv-Related Protein 1Dprp-1Dipeptidyl Peptidase ViiiDpp ViiiProlyl Dipeptidase Dpp8 |
| Cellular Localisation | Cytoplasm |
| Alternative Protein Names | Dipeptidyl Peptidase 8 proteinDp8 proteinDipeptidyl Peptidase Iv-Related Protein 1 proteinDprp-1 proteinDipeptidyl Peptidase Viii proteinDpp Viii proteinProlyl Dipeptidase Dpp8 proteinDPP8 proteinDPRP1 proteinMSTP097 proteinMSTP135 proteinMSTP141 protein |
Information sourced from Uniprot.org
