| IED ID | IndEnz0002001915 |
| Enzyme Type ID | protease001915 |
| Protein Name |
Phenoloxidase-activating factor 2 45 KDa PPAF Hd-45 Prophenoloxidase-activating factor II Serine protease-like PPAF-2 Cleaved into: Phenoloxidase-activating factor 2 light chain; Phenoloxidase-activating factor 2 heavy chain |
| Gene Name | PPAF2 PPAF-II |
| 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 | MKRLFVITAFFLFGAEAQNSVIDAAVVNIFGNASEYIPPGYEIVTKAPLGALTALPRCGTGADQGKKVCIVYHRCDGVTNTVTPEEVINTTGEGIFDIRENANECESYLDVCCGLPEGGVLPTPSPTPPVVPVLKPSFCGIRNERGLDFKITGQTNEAEYGEFPWMVAVLKANVIPGSGEEQLVCGGSLIAPSVVLTGAHCVNSYQSNLDAIKIRAGEWDTLTEKERLPYQERKIRQVIIHSNFNPKTVVNDVALLLLDRPLVQADNIGTICLPQQSQIFDSTECFASGWGKKEFGSRHRYSNILKKIQLPTVDRDKCQADLRNTRLGLKFVLDQTFVCAGGEQGKDTCTGDGGSPLFCPDPRNPSRYMQMGIVAWGIGCGDENVPGVYANVAHFRNWIDQEMQAKGLSTTPYVE |
| Enzyme Length | 415 |
| Uniprot Accession Number | Q9GRW0 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Binds and activates processed prophenoloxidases PPO1 and PPO2 and thus is involved in the activation of the prophenoloxidase cascade probably following the recognition of pathogen-derived products. {ECO:0000269|PubMed:11012672, ECO:0000269|PubMed:12185078, ECO:0000269|PubMed:16362048, ECO:0000269|PubMed:9652393, ECO:0000303|PubMed:12185078}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (21); Chain (2); Disulfide bond (8); Domain (2); Glycosylation (2); Helix (11); Metal binding (4); Mutagenesis (3); Signal peptide (1); Site (1); Turn (6) |
| Keywords | 3D-structure;Antibiotic;Antimicrobial;Calcium;Direct protein sequencing;Disulfide bond;Glycoprotein;Immunity;Innate immunity;Metal-binding;Secreted;Serine protease homolog;Signal |
| Interact With | |
| Induction | INDUCTION: Up-regulated in response to Gram-negative bacterial infections. {ECO:0000269|PubMed:11012672}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9652393}. Note=Secreted in the hemolymph. {ECO:0000269|PubMed:9652393}. |
| Modified Residue | |
| Post Translational Modification | PTM: The N-terminus is blocked (PubMed:11012672). Proteolytically cleaved by PPAF3 (PubMed:11012672, PubMed:12185078). Cleavage produces a light chain and a heavy chain, which probably remain covalently associated through an interchain disulfide bond (Probable). {ECO:0000269|PubMed:11012672, ECO:0000269|PubMed:12185078, ECO:0000269|PubMed:16362048, ECO:0000305|PubMed:16362048}. |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000303|PubMed:11012672 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 2B9L; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 45,258 |
| Kinetics | |
| Metal Binding | METAL 218; /note="Calcium"; /evidence="ECO:0000269|PubMed:16362048, ECO:0007744|PDB:2B9L"; METAL 220; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:16362048, ECO:0007744|PDB:2B9L"; METAL 223; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:16362048, ECO:0007744|PDB:2B9L"; METAL 226; /note="Calcium"; /evidence="ECO:0000269|PubMed:16362048, ECO:0007744|PDB:2B9L" |
| Rhea ID | |
| Cross Reference Brenda |