| IED ID | IndEnz0002018406 |
| Enzyme Type ID | protease018406 |
| Protein Name |
CLIP domain-containing serine protease B9 EC 3.4.21.- Phenoloxidase-activating enzyme B9 |
| Gene Name | CLIPB9 11175774 AgaP_AGAP013442 |
| Organism | Anopheles gambiae (African malaria mosquito) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Diptera Nematocera Culicomorpha Culicoidea Culicidae (mosquitos) Anophelinae Anopheles Cellia Pyretophorus gambiae species complex Anopheles gambiae (African malaria mosquito) |
| Enzyme Sequence | MTSYNRSVAWLTVCVLLALHIGGSHQQQQQCTTPTRLRGRCISIYECDSILDYFKQRILTWEEREFLRKSQCTGATSGRQPFVCCPGNGSKPVVAPATTVPAGTASTTPAGPAATAPSGDAALADQLVGGLLPNPKKNECGVSIGMRIYGGQNADIDEFPWLALLQYENRKGERKYSCGGSLINRRYVLTAAHCVIGEVERKEGKLVSVRLGEYNTKTEIDCVTEEQEEICADPPIDAGIESVIVHPGYQDMAHADDIALLRLAQSIEYTSFVQPVCLPLTDFRASKTGEVNFVTGFGRTLQESRSAVKQKLGIKVYDHARCQEKYATKNSSITTNQLCAGGEYAKDSCHGDSGGPLMKLQKVWYLEGIVSYGNRCGLEDWPGVYTHVPAYMAWVRSNIKE |
| Enzyme Length | 401 |
| Uniprot Accession Number | F5HKX0 |
| Absorption | |
| Active Site | ACT_SITE 193; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274; ACT_SITE 257; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274; ACT_SITE 353; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by serpin SRPN2. {ECO:0000269|PubMed:20953892, ECO:0000269|PubMed:25525260}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Serine peptidase that functions in the melanization-mediated immune response (PubMed:20953892, PubMed:25525260, PubMed:26926112). Cleaves and activates prophenoloxidase (PPO), which is required for the activation of the prophenoloxidase cascade probably following the recognition of pathogen-derived products (PubMed:20953892, PubMed:26926112). {ECO:0000269|PubMed:20953892, ECO:0000269|PubMed:25525260, ECO:0000269|PubMed:26926112}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (6); Domain (2); Glycosylation (2); Sequence conflict (1); Signal peptide (1) |
| Keywords | Disulfide bond;Glycoprotein;Hydrolase;Immunity;Protease;Reference proteome;Secreted;Serine protease;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000255|RuleBase:RU366078}. |
| Modified Residue | |
| Post Translational Modification | PTM: Proteolytic cleavage is necessary for activation. {ECO:0000269|PubMed:20953892, ECO:0000269|PubMed:25525260, ECO:0000269|PubMed:26926112}. |
| Signal Peptide | SIGNAL 1..26; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 43,934 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |