| IED ID | IndEnz0002019022 |
| Enzyme Type ID | protease019022 |
| Protein Name |
Dipeptidyl peptidase 2 EC 3.4.14.2 Dipeptidyl aminopeptidase II Dipeptidyl peptidase 7 Dipeptidyl peptidase II DPP II Quiescent cell proline dipeptidase |
| Gene Name | DPP7 DPP2 QPP |
| 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 | MGSAPWAPVLLLALGLRGLQAGARRAPDPGFQERFFQQRLDHFNFERFGNKTFPQRFLVSDRFWVRGEGPIFFYTGNEGDVWAFANNSAFVAELAAERGALLVFAEHRYYGKSLPFGAQSTQRGHTELLTVEQALADFAELLRALRRDLGAQDAPAIAFGGSYGGMLSAYLRMKYPHLVAGALAASAPVLAVAGLGDSNQFFRDVTADFEGQSPKCTQGVREAFRQIKDLFLQGAYDTVRWEFGTCQPLSDEKDLTQLFMFARNAFTVLAMMDYPYPTDFLGPLPANPVKVGCDRLLSEAQRITGLRALAGLVYNASGSEHCYDIYRLYHSCADPTGCGTGPDARAWDYQACTEINLTFASNNVTDMFPDLPFTDELRQRYCLDTWGVWPRPDWLLTSFWGGDLRAASNIIFSNGNLDPWAGGGIRRNLSASVIAVTIQGGAHHLDLRASHPEDPASVVEARKLEATIIGEWVKAARREQQPALRGGPRLSL |
| Enzyme Length | 492 |
| Uniprot Accession Number | Q9UHL4 |
| Absorption | |
| Active Site | ACT_SITE 162; /note=Charge relay system; /evidence=ECO:0000255; ACT_SITE 418; /note=Charge relay system; /evidence=ECO:0000255; ACT_SITE 443; /note=Charge relay system; /evidence=ECO:0000255 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal dipeptide, Xaa-Yaa-|-, preferentially when Yaa is Ala or Pro. Substrates are oligopeptides, preferentially tripeptides.; EC=3.4.14.2; Evidence={ECO:0000269|PubMed:15487984}; |
| DNA Binding | |
| EC Number | 3.4.14.2 |
| Enzyme Function | FUNCTION: Plays an important role in the degradation of some oligopeptides. {ECO:0000269|PubMed:15487984}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5. Has low activity at pH 7 and is inactive at pH 8.; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (13); Chain (1); Glycosylation (6); Helix (19); Natural variant (1); Propeptide (1); Sequence conflict (1); Signal peptide (1); Turn (4) |
| Keywords | 3D-structure;Aminopeptidase;Cleavage on pair of basic residues;Cytoplasmic vesicle;Direct protein sequencing;Glycoprotein;Hydrolase;Lysosome;Protease;Reference proteome;Secreted;Serine protease;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:15487984}. Cytoplasmic vesicle {ECO:0000269|PubMed:15487984}. Secreted {ECO:0000269|PubMed:15487984}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. {ECO:0000269|PubMed:15487984, ECO:0000269|PubMed:19159218}. |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 3JYH; 3N0T; 4EBB; |
| Mapped Pubmed ID | 12529175; 15231747; 18823758; 18985028; 19556882; 20217867; 20534982; 20711500; 22952628; 24835590; 8692836; |
| Motif | |
| Gene Encoded By | |
| Mass | 54,341 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.14.2; |