| IED ID | IndEnz0002011604 |
| Enzyme Type ID | protease011604 |
| Protein Name |
Phenoloxidase-activating factor 3 EC 3.4.21.- Prophenoloxidase-activating factor III Serine protease-like protein PPAF-3 Cleaved into: Phenoloxidase-activating factor 3 light chain; Phenoloxidase-activating factor 3 heavy chain |
| Gene Name | PPAF3 PPAF-III |
| Organism | Holotrichia diomphalia (Korean black chafer) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Coleoptera Polyphaga Scarabaeiformia Scarabaeoidea Scarabaeidae (scarab beetles) Melolonthinae (May beetles & June bugs) Holotrichia Holotrichia diomphalia (Korean black chafer) |
| Enzyme Sequence | MWLSLVILGVASAIVNVSTQESCTTPNGETATCLPIESCKIFWDYVVTSGADPEINSFLRASLCRQGNYVVCCGSTLKFNSALPDRTECGLQDDFKVLGGEDTDLGEYPWMALLQQTKTSGAKSFGCGGSLISDRYVLTAAHCVVSSSYTVTMVRLGEWDLRATQDCVGSGSYQYCSPPPQDIGIESITSHPNYEKSSRGVFNDIALIRLARPVNRNKYVQPICLPLPTERTPVGENLLVAGWGATETKAQSDKKQKLKLPVTDLPACKTLYAKHNKIINDKMICAGGLKGKDSCKGDSGGPLFGQTGAGNAQFYIEGIVSYGAICGTEGFPAIYTRVSDHLDWIKQNVRV |
| Enzyme Length | 351 |
| Uniprot Accession Number | Q8I6K0 |
| Absorption | |
| Active Site | ACT_SITE 142; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274; ACT_SITE 204; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274; ACT_SITE 299; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274 |
| Activity Regulation | ACTIVITY REGULATION: Cleavage of PPAF2 is Ca(2+)-independent (PubMed:12185078). Inhibited by heparin (PubMed:17287215). {ECO:0000269|PubMed:12185078, ECO:0000269|PubMed:17287215}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Serine endopeptidase which, by cleaving prophenoloxidase activating factor PPAF2, is required for the activation of the prophenoloxidase cascade probably following the recognition of pathogen-derived products. {ECO:0000269|PubMed:12185078, ECO:0000269|PubMed:17287215}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (2); Disulfide bond (8); Domain (2); Glycosylation (1); Metal binding (4); Signal peptide (1); Site (1) |
| Keywords | Calcium;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Immunity;Innate immunity;Metal-binding;Protease;Secreted;Serine protease;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12185078}. Note=Secreted in the hemolymph. {ECO:0000269|PubMed:12185078}. |
| Modified Residue | |
| Post Translational Modification | PTM: Proteolytically cleaved. {ECO:0000269|PubMed:12185078}. |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 37,925 |
| Kinetics | |
| Metal Binding | METAL 158; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q9GRW0; METAL 160; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q9GRW0; METAL 163; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q9GRW0; METAL 166; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q9GRW0 |
| Rhea ID | |
| Cross Reference Brenda |