| IED ID | IndEnz0002009864 |
| Enzyme Type ID | protease009864 |
| Protein Name |
Phenoloxidase-activating factor 1 EC 3.4.21.- Prophenoloxidase-activating factor I Serine protease PPAF-1 Cleaved into: Phenoloxidase-activating factor 1 light chain; Phenoloxidase-activating factor 1 heavy chain |
| Gene Name | PPAF1 PPAF-I |
| 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 | MKQVHFFILWFFVLNLYSIKAQAGCRTPNGENARCVPINNCKILYDSVLTSDPEVIRFLRASQCGYNGQPLVCCGSSASYQPPPTSASIRNRRPELLPNDCGYQVEADKILNGDDTVPEEFPWTAMIGYKNSSNFEQFACGGSLINNRYIVTAAHCVAGRVLRVVGALNKVRLGEWNTATDPDCYGAVRVCVPDKPIDLGIEETIQHPDYVDGSKDRYHDIALIRLNRQVEFTNYIRPVCLPQPNEEVQVGQRLTVVGWGRTETGQYSTIKQKLAVPVVHAEQCAKTFGAAGVRVRSSQLCAGGEKAKDSCGGDSGGPLLAERANQQFFLEGLVSFGATCGTEGWPGIYTKVGKYRDWIEGNIRP |
| Enzyme Length | 365 |
| Uniprot Accession Number | O97366 |
| Absorption | |
| Active Site | ACT_SITE 155; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274; ACT_SITE 220; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274; ACT_SITE 315; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274 |
| Activity Regulation | ACTIVITY REGULATION: Protein stability and endopeptidase activity are calcium dependent (PubMed:17287215). First cleavage on prophenoloxidase PPO1 and PPO2 is not dependent on calcium; however, cleavage of PPO1 and PPO2 to their active forms is dependent on calcium and on the presence of PPAF2 and PPAF3 (PubMed:12185078). Cleavage of PPAF2 is inhibited by calcium (PubMed:11012672, PubMed:12185078). Inhibited by ethylenediaminetetraacetic acid (EDTA), p-nitrophenyl-p'-guanido-benzoate, diisopropylphosphorofluoridate (iPr2PF) and p-(Amidinophenyl)methanesulfonyl fluoride (p-APMSF) (PubMed:9652393, PubMed:17287215). {ECO:0000269|PubMed:11012672, ECO:0000269|PubMed:12185078, ECO:0000269|PubMed:17287215, ECO:0000269|PubMed:9652393}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Serine endopeptidase which, by cleaving prophenoloxidase PPO1 and PPO2, is required for the activation of the prophenoloxidase cascade probably following the recognition of pathogen-derived products. {ECO:0000269|PubMed:12185078, ECO:0000269|PubMed:16362048, ECO:0000269|PubMed:17287215, ECO:0000269|PubMed:9652393, ECO:0000269|PubMed:9839951}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (15); Chain (2); Disulfide bond (8); Domain (2); Glycosylation (1); Helix (7); Metal binding (4); Signal peptide (1); Site (1); Turn (1) |
| Keywords | 3D-structure;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, ECO:0000269|PubMed:9652393, ECO:0000269|PubMed:9839951}. Note=Secreted in the hemolymph. {ECO:0000269|PubMed:12185078, ECO:0000269|PubMed:9652393, ECO:0000269|PubMed:9839951}. |
| Modified Residue | |
| Post Translational Modification | PTM: Cleaved following the recognition of pathogen-derived products, probably by a lysyl endopeptidase. {ECO:0000269|PubMed:11012672, ECO:0000269|PubMed:16362048, ECO:0000269|PubMed:17287215, ECO:0000269|PubMed:9652393, ECO:0000269|PubMed:9839951}. |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 2OLG; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 40,195 |
| Kinetics | |
| Metal Binding | METAL 175; /note="Calcium"; /evidence="ECO:0000269|PubMed:17287215, ECO:0007744|PDB:2OLG"; METAL 177; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:17287215, ECO:0007744|PDB:2OLG"; METAL 180; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:17287215, ECO:0007744|PDB:2OLG"; METAL 183; /note="Calcium"; /evidence="ECO:0000269|PubMed:17287215, ECO:0007744|PDB:2OLG" |
| Rhea ID | |
| Cross Reference Brenda |