| Post Translational Modifications | N-glycosylated. While glycosylation at Asn-53, Asn-119 and Asn-276 is mediated by STT3A-containing complexes, glycosylation at Asn-29 is mediated STT3B-containing complexes. In approximately 50% of the complexes the exclusion domain is cleaved at position 58 or 61. The two parts of the exclusion domain are held together by a disulfide bond. |
| Function | Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. |
| Protein Name | Dipeptidyl Peptidase 1Cathepsin CCathepsin JDipeptidyl Peptidase IDpp-IDppiDipeptidyl Transferase Cleaved Into - Dipeptidyl Peptidase 1 Exclusion Domain ChainDipeptidyl Peptidase I Exclusion Domain Chain - Dipeptidyl Peptidase 1 Heavy ChainDipeptidyl Peptidase I Heavy Chain - Dipeptidyl Peptidase 1 Light ChainDipeptidyl Peptidase I Light Chain |
| Database Links | Reactome: R-HSA-204005Reactome: R-HSA-2132295Reactome: R-HSA-5694530Reactome: R-HSA-6798695 |
| Cellular Localisation | Lysosome |
| Alternative Protein Names | Dipeptidyl Peptidase 1 proteinCathepsin C proteinCathepsin J proteinDipeptidyl Peptidase I proteinDpp-I proteinDppi proteinDipeptidyl Transferase Cleaved Into - Dipeptidyl Peptidase 1 Exclusion Domain Chain proteinDipeptidyl Peptidase I Exclusion Domain Chain - Dipeptidyl Peptidase 1 Heavy Chain proteinDipeptidyl Peptidase I Heavy Chain - Dipeptidyl Peptidase 1 Light Chain proteinDipeptidyl Peptidase I Light Chain proteinCTSC proteinCPPI protein |
Information sourced from Uniprot.org
