| IED ID | IndEnz0002016417 |
| Enzyme Type ID | protease016417 |
| Protein Name |
Dipeptidyl aminopeptidase 1 Cathepsin C homolog EC 3.4.14.1 Cleaved into: Dipeptidyl aminopeptidase 1 exclusion domain chain; Dipeptidyl aminopeptidase 1 heavy chain; Dipeptidyl aminopeptidase 1 light chain |
| Gene Name | DPAP1 PF11_0174 PF3D7_1116700 |
| Organism | Plasmodium falciparum (isolate 3D7) |
| Taxonomic Lineage | cellular organisms Eukaryota Sar Alveolata Apicomplexa Aconoidasida Haemosporida (haemosporidians) Plasmodiidae Plasmodium Plasmodium (Laverania) Plasmodium falciparum Plasmodium falciparum (isolate 3D7) |
| Enzyme Sequence | MAKRIFSVSFLLVLLNVLHICIKFSVADLPTHVETKNLLGKWKILRTKTSPNLTTCGSSQPNKNTYNVGITDYKKYLLENNYEFVSELNVILSDDYVLYGDIYNTQDNEHRSKWKVLAVYDENKRVIGTWTTICDEGFEIKIGNETYAALMHYEPNGKCGPVSDEDSLDSNGDTDCYTTSFSKIRYGWLDVENEKNEHLHGCFYAERIFDNVNEIKHLDSFTIDKDSQNVLQTFTYDTKLNNILNSNNMLYKFGNLQKPTFTKRNNTNVQFNSELNWHRMKHHGKKKPLKKSMLDASRQTYACPCNANEVVDNVINKGDSDNPVSPTLIQLNNNLKNTTQTGNKDTNEMDLENYEDTLNSPKRELEINELPKNFTWGDPWNKNTREYEVTNQLLCGSCYIASQLYAFKRRIEVALTKKLDRKYLNNFDDQLSIQTVLSCSFYDQGCNGGFPYLVSKLAKLQGIPLNVYFPYSATEETCPYNISKHPNDMNGSAKLREINAIFNSNNNMSTYNNINNDHHQLGVYANTASSQEQHGISEENRWYAKDFNYVGGCYGCNQCNGEKIMMNEIYRNGPIVSSFEASPDFYDYADGVYFVEDFPHARRCTIEPKNDGVYNITGWDRVNHAIVLLGWGEEEINGKLYKYWIGRNSWGNGWGKEGYFKILRGQNFSGIESQSLFIEPDFSRGAGKILLEKMQKELGN |
| Enzyme Length | 700 |
| Uniprot Accession Number | Q8IIJ9 |
| Absorption | |
| Active Site | ACT_SITE 398; /evidence=ECO:0000255|PROSITE-ProRule:PRU10088; ACT_SITE 624; /evidence=ECO:0000255|PROSITE-ProRule:PRU10089; ACT_SITE 648; /evidence=ECO:0000255|PROSITE-ProRule:PRU10090 |
| Activity Regulation | |
| Binding Site | BINDING 450; /note=Chloride; /evidence=ECO:0000250|UniProtKB:P53634; BINDING 452; /note=Chloride; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P53634; BINDING 549; /note=Chloride; /evidence=ECO:0000250|UniProtKB:P53634 |
| 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; Evidence={ECO:0000269|PubMed:15304495, ECO:0000269|PubMed:20833209}; |
| DNA Binding | |
| EC Number | 3.4.14.1 |
| Enzyme Function | FUNCTION: Thiol protease that cleaves dipeptides from the N-terminus of protein substrates (PubMed:15304495, PubMed:20833209). Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids (PubMed:20833209). Proline cannot occupy the P1 position and arginine or lysine cannot occupy the P2 position of the substrate (PubMed:20833209). Involved in host hemoglobin degradation by generating dipeptides from hemoglobin-derived oligopeptides (PubMed:15304495). {ECO:0000269|PubMed:15304495, ECO:0000269|PubMed:20833209}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6-6.5. {ECO:0000269|PubMed:20833209}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Binding site (3); Chain (3); Disulfide bond (2); Glycosylation (10); Modified residue (1); Propeptide (1); Signal peptide (1) |
| Keywords | Chloride;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Protease;Reference proteome;Signal;Sulfation;Thiol protease;Vacuole;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Vacuole lumen {ECO:0000269|PubMed:15304495}. Parasitophorous vacuole lumen {ECO:0000269|PubMed:15304495}. Note=In schizonts, the immature form localizes to the parasitophorous vacuole (PubMed:15304495). In trophozoites, the mature form localizes to the digestive (or food) vacuole, an acidic vacuole where host hemoglobin is digested (PubMed:15304495). {ECO:0000269|PubMed:15304495}. |
| Modified Residue | MOD_RES 416; /note=Sulfothreonine; /evidence=ECO:0000269|PubMed:14752058 |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..27; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 16267556; |
| Motif | |
| Gene Encoded By | |
| Mass | 80,412 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |