| IED ID | IndEnz0002005961 |
| Enzyme Type ID | protease005961 |
| 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 |
| Organism | Rattus norvegicus (Rat) |
| 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 Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MGPWTHSLRAALLLVLLGVCTVSSDTPANCTYPDLLGTWVFQVGPRHPRSHINCSVMEPTEEKVVIHLKKLDTAYDEVGNSGYFTLIYNQGFEIVLNDYKWFAFFKYEVKGSRAISYCHETMTGWVHDVLGRNWACFVGKKMANHSEKVYVNVAHLGGLQEKYSERLYSHNHNFVKAINSVQKSWTATTYEEYEKLSIRDLIRRSGHSGRILRPKPAPITDEIQQQILSLPESWDWRNVRGINFVSPVRNQESCGSCYSFASLGMLEARIRILTNNSQTPILSPQEVVSCSPYAQGCDGGFPYLIAGKYAQDFGVVEENCFPYTATDAPCKPKENCLRYYSSEYYYVGGFYGGCNEALMKLELVKHGPMAVAFEVHDDFLHYHSGIYHHTGLSDPFNPFELTNHAVLLVGYGKDPVTGLDYWIVKNSWGSQWGESGYFRIRRGTDECAIESIAMAAIPIPKL |
| Enzyme Length | 462 |
| Uniprot Accession Number | P80067 |
| Absorption | |
| Active Site | ACT_SITE 257; /evidence=ECO:0000250; ACT_SITE 404; /evidence=ECO:0000250; ACT_SITE 426; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | BINDING 301; /note=Chloride; /evidence=ECO:0000250; BINDING 303; /note=Chloride; via amide nitrogen; /evidence=ECO:0000250; BINDING 346; /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 (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (19); Binding site (3); Chain (3); Disulfide bond (5); Glycosylation (4); Helix (9); Propeptide (1); Sequence conflict (5); Signal peptide (1); Turn (4) |
| Keywords | 3D-structure;Chloride;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Lysosome;Protease;Reference proteome;Signal;Thiol protease;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Lysosome. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. {ECO:0000269|PubMed:11602245}. |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000269|PubMed:1740150 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1JQP; |
| Mapped Pubmed ID | 11367515; 12843783; 148980; 18307834; 3094018; 3705543; 4065148; 657443; 8215389; 843913; |
| Motif | |
| Gene Encoded By | |
| Mass | 52,235 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.14.1; |