| IED ID | IndEnz0002010332 |
| Enzyme Type ID | protease010332 |
| Protein Name |
Dipeptidyl peptidase 3 EC 3.4.14.4 Dipeptidyl aminopeptidase III Dipeptidyl arylamidase III Dipeptidyl peptidase III DPP III |
| Gene Name | DppIII CG7415 |
| Organism | Drosophila melanogaster (Fruit fly) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Diptera Brachycera Muscomorpha Eremoneura Cyclorrhapha Schizophora Acalyptratae Ephydroidea Drosophilidae (pomace flies) Drosophilinae Drosophilini Drosophila (fruit flies) Sophophora melanogaster group melanogaster subgroup Drosophila melanogaster (Fruit fly) |
| Enzyme Sequence | MFWLRGLQRSRQQLNRLCHFRSRLNYGTSPSIRSVQPSISRSLGFCSSLVRYSCSTNLPQPAEMASKTAHFVLPNTQPIADLDCKSAFENLTEKEKLYAHHFSQASWDGGLIALIQSSPEAPLIFSLLHRIFLAEKIPVLRAKALEAGVSADDFTAFLVYACGVFANAGNYKGMGDSKIVPNLSEKQFETIVKASAAYSDEPRVGKIFEKVKNLIYALESRNEILGFAPDGITTYWSDNCTKEDSEIVNAWLTSKRIEPYMCRTFKIVENGQTVYDVKLGSVAESTQDGITLPLEEYNGNKFRVTRGDYQKLLQRVNQHLLQAQKYAANENESKMIEHYVRSFEQGSLDEHKNGSRWWIKDKGPVIETYIGFIETYRDPAGGRAEFEGFVAMVNKESSAKFSELVNRAEKLIEYLPWTEPYEKDSYLKPDFTSLDVLTFAGSGVPAGINIPNYDEIRQDEGFKNVSLGNVLANINRKDPIPFLTEEDQTLMKEYKVKAFEVQVGLHELLGHGSGKLFRIDENGVYNFDKENTKNLVTGEPITKWYLPGETYDTKFGAIGSSYEECRAEAVGLYLSLQRDILEIFGFKDKAEQDNIIYVNWLSLIWNGMGVALEMFNPKSKLWLQAHSRARFVIMKVLLEAGEGLVKVEETEKGKNLLLTVDRSKIDTVGRKALGDFLTKLQVYKSTADIEAASKMYEHYSKVDESGSHPWAKWRDICLAHKKPRMILVQANTAIGQDQKVQLKTYEPTHEGYIQSWVERYPNTDIDDLLESIVEKDKKYFPTAFNN |
| Enzyme Length | 786 |
| Uniprot Accession Number | Q9VHR8 |
| Absorption | |
| Active Site | ACT_SITE 507; /evidence=ECO:0000250|UniProtKB:O55096 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal dipeptide from a peptide comprising four or more residues, with broad specificity. Also acts on dipeptidyl 2-naphthylamides.; EC=3.4.14.4; Evidence={ECO:0000269|PubMed:12846841}; |
| DNA Binding | |
| EC Number | 3.4.14.4 |
| Enzyme Function | FUNCTION: Degrades neuropeptide proctolin (RYLPT) by cleavage between Tyr and Leu residues. {ECO:0000269|PubMed:12846841}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (1); Chain (1); Erroneous initiation (1); Metal binding (3); Topological domain (3); Transmembrane (2) |
| Keywords | Alternative splicing;Aminopeptidase;Cell membrane;Cytoplasm;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Transmembrane;Transmembrane helix;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Isoform 1]: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:12846841}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:12846841}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 15579698; 15899868; 16478478; 18039869; 20220848; 20371351; 21074052; 23071443; 24658702; 25312911; 25414008; 25776889; 26290570; 26362788; 26526100; 26870755; 27582081; 28067623; 31690598; 31722958; |
| Motif | |
| Gene Encoded By | |
| Mass | 89,194 |
| Kinetics | |
| Metal Binding | METAL 506; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:Q9NY33; METAL 511; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:Q9NY33; METAL 564; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:Q9NY33 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.14.4; |