| IED ID | IndEnz0002014066 |
| Enzyme Type ID | protease014066 |
| 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 1 Dipeptidyl peptidase I heavy chain 1 ; Dipeptidyl peptidase 1 heavy chain 2 Dipeptidyl peptidase I heavy chain 2 ; Dipeptidyl peptidase 1 heavy chain 3 Dipeptidyl peptidase I heavy chain 3 ; Dipeptidyl peptidase 1 heavy chain 4 Dipeptidyl peptidase I heavy chain 4 ; Dipeptidyl peptidase 1 light chain Dipeptidyl peptidase I light chain Fragment |
| Gene Name | CTSC |
| Organism | Canis lupus familiaris (Dog) (Canis familiaris) |
| 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 Laurasiatheria Carnivora Caniformia Canidae (dog coyote wolf fox) Canis Canis lupus (Gray wolf) Canis lupus familiaris (Dog) (Canis familiaris) |
| Enzyme Sequence | DTPANCTHPELLGTWVFQVGPAGSRSVNCSVMGPPEKKVVVHLEKLDTAYDNFGNTGHFTIIYNQGFEIVLNDYKWFAFFKYKEEGHKVTSYCNETMTGWVHDVLGRNWACFTGTKMGTTSEKAKVNTKHIERLQENNSNRLYKYNYEFVKAINTIQKSWTATRYIEYETLTLRDMMTRVGGRKIPRPKPTPLTAEIHEEISRLPTSWDWRNVRGTNFVSPVRNQASCGSCYAFASTAMLEARIRILTNNTQTPILSPQEIVSCSQYAQGCEGGFPYLIAGKYAQDFGLVEEACFPYAGSDSPCKPNDCFRYYSSEYYYVGGFYGACNEALMKLELVRHGPMAVAFEVYDDFFHYQKGIYYHTGLRDPFNPFELTNHAVLLVGYGTDSASGMDYWIVKNSWGSRWGEDGYFRIRRGTDECAIESIAVAATPIPKL |
| Enzyme Length | 435 |
| Uniprot Accession Number | O97578 |
| Absorption | |
| Active Site | ACT_SITE 231; /evidence=ECO:0000250; ACT_SITE 377; /evidence=ECO:0000250; ACT_SITE 399; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | BINDING 275; /note=Chloride; /evidence=ECO:0000250; BINDING 277; /note=Chloride; via amide nitrogen; /evidence=ECO:0000250; BINDING 319; /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 | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5. Active over a broad pH range.; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Binding site (3); Chain (6); Disulfide bond (5); Glycosylation (4); Non-terminal residue (1); Propeptide (1) |
| Keywords | Chloride;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Lysosome;Protease;Reference proteome;Thiol protease;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Lysosome {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: The N-terminus of the heavy chain is heterogeneously processed to produce four different chains. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 49,412 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |