Detail Information for IndEnz0002018406
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