| IED ID | IndEnz0002016588 |
| Enzyme Type ID | protease016588 |
| 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 CPPI |
| Organism | Homo sapiens (Human) |
| 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 Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MGAGPSLLLAALLLLLSGDGAVRCDTPANCTYLDLLGTWVFQVGSSGSQRDVNCSVMGPQEKKVVVYLQKLDTAYDDLGNSGHFTIIYNQGFEIVLNDYKWFAFFKYKEEGSKVTTYCNETMTGWVHDVLGRNWACFTGKKVGTASENVYVNIAHLKNSQEKYSNRLYKYDHNFVKAINAIQKSWTATTYMEYETLTLGDMIRRSGGHSRKIPRPKPAPLTAEIQQKILHLPTSWDWRNVHGINFVSPVRNQASCGSCYSFASMGMLEARIRILTNNSQTPILSPQEVVSCSQYAQGCEGGFPYLIAGKYAQDFGLVEEACFPYTGTDSPCKMKEDCFRYYSSEYHYVGGFYGGCNEALMKLELVHHGPMAVAFEVYDDFLHYKKGIYHHTGLRDPFNPFELTNHAVLLVGYGTDSASGMDYWIVKNSWGTGWGENGYFRIRRGTDECAIESIAVAATPIPKL |
| Enzyme Length | 463 |
| Uniprot Accession Number | P53634 |
| Absorption | |
| Active Site | ACT_SITE 258; /evidence=ECO:0000255|PROSITE-ProRule:PRU10088; ACT_SITE 405; /evidence=ECO:0000255|PROSITE-ProRule:PRU10089; ACT_SITE 427; /evidence=ECO:0000255|PROSITE-ProRule:PRU10090 |
| Activity Regulation | ACTIVITY REGULATION: Strongly inhibited by the cysteine peptidase inhibitors mersalyl acid, iodoacetic acid and cystatin. Inhibited by N-ethylmaleimide, Gly-Phe-diazomethane, TLCK, TPCK and, at low pH, by dithiodipyridine. Not inhibited by the serine peptidase inhibitor PMSF, the aminopeptidase inhibitor bestatin, or metal ion chelators. {ECO:0000269|PubMed:1586157}. |
| Binding Site | BINDING 302; /note="Chloride"; /evidence="ECO:0000269|PubMed:11726493, ECO:0007744|PDB:1K3B"; BINDING 304; /note="Chloride; via amide nitrogen"; /evidence="ECO:0000269|PubMed:11726493, ECO:0007744|PDB:1K3B"; BINDING 347; /note="Chloride"; /evidence="ECO:0000269|PubMed:11726493, ECO:0007744|PDB:1K3B" |
| 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. 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. Can also activate neuraminidase and factor XIII. {ECO:0000269|PubMed:1586157}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: High activity at pH 4.5-6.8. {ECO:0000269|PubMed:1586157}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (4); Beta strand (18); Binding site (3); Chain (3); Disulfide bond (5); Erroneous initiation (1); Glycosylation (4); Helix (11); Natural variant (31); Propeptide (1); Sequence conflict (6); Signal peptide (1); Turn (6) |
| Keywords | 3D-structure;Alternative splicing;Chloride;Direct protein sequencing;Disease variant;Disulfide bond;Glycoprotein;Hydrolase;Lysosome;Palmoplantar keratoderma;Protease;Reference proteome;Signal;Thiol protease;Zymogen |
| Interact With | O76096; G5E9A7; Q7Z699 |
| Induction | INDUCTION: Up-regulated in lymphocytes by IL2/interleukin-2. {ECO:0000269|PubMed:9092576}. |
| Subcellular Location | SUBCELLULAR LOCATION: Lysosome. |
| Modified Residue | |
| Post Translational Modification | PTM: 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. {ECO:0000269|PubMed:11726493, ECO:0000269|PubMed:1586157, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19167329, ECO:0000269|PubMed:9507095}.; PTM: 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. |
| Signal Peptide | SIGNAL 1..24; /evidence="ECO:0000269|PubMed:11015218, ECO:0000269|PubMed:7665576, ECO:0000269|PubMed:9507095" |
| Structure 3D | X-ray crystallography (10) |
| Cross Reference PDB | 1K3B; 2DJF; 2DJG; 3PDF; 4CDC; 4CDD; 4CDE; 4CDF; 4OEL; 4OEM; |
| Mapped Pubmed ID | 10072072; 10559958; 10631941; 10652252; 10679020; 10747087; 10748235; 10809954; 10825291; 10903204; 10982397; 11035026; 11285137; 11306556; 11684289; 11813165; 11853874; 11914041; 11927603; 12078484; 12080079; 12083812; 12235121; 12742663; 12748383; 12857359; 15111626; 15585850; 15985311; 16129679; 16181339; 16303754; 16624868; 17005010; 17020538; 17038314; 17192411; 17287728; 17316621; 17353931; 17446270; 17535802; 17652201; 17943190; 18025080; 18256700; 18283111; 18294227; 18307834; 18809751; 18841559; 18843296; 19164740; 19638414; 19656848; 19816003; 20236208; 20359428; 20477988; 20533886; 20545907; 20679433; 20711500; 20797317; 20966969; 21393975; 21478858; 21532587; 21742978; 22013193; 22157747; 22675024; 22928782; 23108224; 23311634; 23378591; 23397598; 23479643; 23556547; 23698585; 24119662; 24374475; 24592859; 24894642; 24917561; 24949444; 25395616; 25406594; 25586378; 25619252; 26205983; 26385525; 26496610; 26631737; 26884336; 27060303; 27062382; 27746119; 28878298; 29501728; 30703555; 30854815; 31068678; 31846207; 31925812; 34737793; 8663406; 8687433; 8692836; 9094723; 9150144; 9307973; 9395526; 9539769; 9545226; 9647643; |
| Motif | |
| Gene Encoded By | |
| Mass | 51,854 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.14.1; |