| IED ID | IndEnz0002016591 |
| Enzyme Type ID | protease016591 |
| Protein Name |
Dipeptidyl peptidase 1 EC 3.4.14.1 Cathepsin C Cathepsin J Dipeptidyl peptidase I DPP-I DPPI Dipeptidyl transferase Cleaved into: Dipeptidyl peptidase 1 exclusion domain chain Dipeptidyl peptidase I exclusion domain chain ; Dipeptidyl peptidase 1 heavy chain Dipeptidyl peptidase I heavy chain ; Dipeptidyl peptidase 1 light chain Dipeptidyl peptidase I light chain |
| Gene Name | CTSC QnpA-12394 |
| Organism | Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Cercopithecoidea Cercopithecidae (Old World monkeys) Cercopithecinae Macaca (macaques) Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) |
| Enzyme Sequence | MGVGPASLLAALLLLLSGDRAVRCDTPANCTYLDLLGTWVFQVGSSGSLRDVNCSVMGPPEKKVVVHLQKLDTAYDDLGNSGHFTIIYNQGFEIVLNDYKWFAFFKYKEEGIKVTIYCNETMTGWVHDVLGRNWACFTGKKVGTASENVYVNTAHLKNSQEKYSNRLYKYDHNFVKAINAIQKSWTATTYMEYETLTLGDMIKRSGGHSRKIPRPKPTPLTAEIQQKILHLPTSWDWRNVHGINFVSPVRNQASCGSCYSFASVGMLEARIRILTNNSQTPILSSQEVVSCSQYAQGCEGGFPYLTAGKYAQDFGLVEEACFPYTGTDSPCKMKEDCFRYYSSEYHYVGGFYGGCNEALMKLELVYHGPLAVAFEVYDDFLHYQNGIYHHTGLRDPFNPFELTNHAVLLVGYGTDSASGMDYWIVKNSWGTSWGEDGYFRIRRGTDECAIESIAVAATPIPKL |
| Enzyme Length | 463 |
| Uniprot Accession Number | Q60HG6 |
| Absorption | |
| Active Site | ACT_SITE 258; /evidence=ECO:0000250; ACT_SITE 405; /evidence=ECO:0000250; ACT_SITE 427; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | BINDING 302; /note=Chloride; /evidence=ECO:0000250; BINDING 304; /note=Chloride; via amide nitrogen; /evidence=ECO:0000250; BINDING 347; /note=Chloride; /evidence=ECO:0000250 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, except when Xaa is Arg or Lys, or Yaa or Zaa is Pro.; EC=3.4.14.1; |
| DNA Binding | |
| EC Number | 3.4.14.1 |
| Enzyme Function | FUNCTION: Thiol protease. Has dipeptidylpeptidase activity. Can act as both an exopeptidase and endopeptidase. Can degrade glucagon. Plays a role in the generation of cytotoxic lymphocyte effector function (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Binding site (3); Chain (3); Disulfide bond (5); Glycosylation (4); Propeptide (1); Signal peptide (1) |
| Keywords | Chloride;Disulfide bond;Glycoprotein;Hydrolase;Lysosome;Protease;Reference proteome;Signal;Thiol protease;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Lysosome {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000250 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 51,866 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |