| 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 DPP9, suggesting the existence of substrate(s) required for NLRP1 and CARD8 inhibition. |
| Protein Name | Dipeptidyl Peptidase 9Dp9Dipeptidyl Peptidase Iv-Related Protein 2Dprp-2Dipeptidyl Peptidase IxDpp IxDipeptidyl Peptidase-Like Protein 9Dplp9 |
| Cellular Localisation | Isoform 1: CytoplasmCytosolIsoform 2: Nucleus |
| Alternative Protein Names | Dipeptidyl Peptidase 9 proteinDp9 proteinDipeptidyl Peptidase Iv-Related Protein 2 proteinDprp-2 proteinDipeptidyl Peptidase Ix proteinDpp Ix proteinDipeptidyl Peptidase-Like Protein 9 proteinDplp9 proteinDPP9 proteinDPRP2 protein |
Information sourced from Uniprot.org
