| IED ID | IndEnz0002012947 |
| Enzyme Type ID | protease012947 |
| Protein Name |
Phenoloxidase-activating enzyme 1 EC 3.4.21.- Prophenoloxidase-activating enzyme 1 Serine protease PPAE1 Slppae1 |
| Gene Name | PPAE1 |
| Organism | Spodoptera litura (Asian cotton leafworm) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Amphiesmenoptera Lepidoptera (butterflies and moths) Glossata Neolepidoptera Heteroneura Ditrysia Obtectomera Noctuoidea Noctuidae (owlet moths) Amphipyrinae Spodoptera Spodoptera litura (Asian cotton leafworm) |
| Enzyme Sequence | MWKSLVFFVSALIWSFGSSQDCTTPTGSRSNCVSLYQCQPLYNAFEQRPLPTHVVSYLGRSQCGFEGYVPRVCCGPLPEEQEATSARPTQAPTQGSSDVFPEDSSPAPRNQCGIDTTGDRVYGGTITDLDEFPWMALLGYRTKKGTTSYQCGGVLVNHRYILTAAHCITGAIEQAVGTLITVRLGEYDTQQDVDCIDSVCADRPQEIRVASAYPHPGYSDKNKNRQDDIGIVRLATRAAYTYYVQPICLIDNRARLDTGSDVYVAGWGKTLNGRNSPIKLKLNLPIFNKQECDDKHRGEVLSSVQICAGGVFAEDACRGDSGGPLMKKTPNGIWEVVGVVSFGYGCGRDGWPGVYTSVARYIDWIQNTIASSNV |
| Enzyme Length | 374 |
| Uniprot Accession Number | Q49QW1 |
| Absorption | |
| Active Site | ACT_SITE 166; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274; ACT_SITE 228; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274; ACT_SITE 321; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by aprotenin. Not inhibited by EDTA, PMSF or leupeptin. {ECO:0000269|PubMed:19557749}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Serine protease which, by cleaving and activating prophenoloxidase (PPO1) after immune challenge, plays an essential role in the melanization immune response to wounding. {ECO:0000305|PubMed:19557749}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Compositional bias (1); Disulfide bond (6); Domain (2); Metal binding (2); Propeptide (1); Region (1); Signal peptide (1) |
| Keywords | Calcium;Disulfide bond;Hydrolase;Metal-binding;Protease;Secreted;Serine protease;Signal;Zymogen |
| Interact With | |
| Induction | INDUCTION: Upon physical injury. Up-regulated 5-fold after 6 hours and 15-fold after 18 hours of injury. {ECO:0000269|PubMed:19557749}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000255|RuleBase:RU366078, ECO:0000269|PubMed:19557749}. Note=Secreted in the hemolymph. {ECO:0000269|PubMed:19557749}. |
| Modified Residue | |
| Post Translational Modification | PTM: Activated by the removal of the N-terminal inhibitory propeptide. {ECO:0000305|PubMed:19557749}. |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 40,896 |
| Kinetics | |
| Metal Binding | METAL 186; /note=Calcium; /evidence=ECO:0000250|UniProtKB:O97366; METAL 194; /note=Calcium; /evidence=ECO:0000250|UniProtKB:O97366 |
| Rhea ID | |
| Cross Reference Brenda |