IED ID | IndEnz0002018403 |
Enzyme Type ID | protease018403 |
Protein Name |
CLIP domain-containing serine protease B8 EC 3.4.21.- |
Gene Name | CLIPB8 1273740 ser6 AgaP_AGAP003057 |
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 | MSSAVLLLLVCGCALAVLSPVAYGAPMDTDDRPVWDSIRLCDIPNEPNPGQCMLPAECVAYGKINDVSSLSSIERFSFIKQIQCNGSDTVPYVCCPRDSDAYREPYVNETMVPKNRVASRIAFDADSCGIQSYVAKIRGGQLAEIDEFPWMAMLLYERDNNALTQGCGGALISRTYVITAAHCVTGKNFQQTKGRLKFVRLREYNIHTNPDCVYENDLKDCSDDMIDLVPQAVIPHPEYDSESSNQQHDIALIRIEQTPPFTDFLRSICLPEQNFESSATPGKKLSVSGWGRTDIFKDNLGPDVLSPIKLKLSLPYVEREKCSKTFRPWSFALGPGQMCAGGERAKDTCAGDSGSPLMSYDMKRAIWYITGIVSLGVRGCGVEGLPGVYTNVHHYLPWIKMYTGA |
Enzyme Length | 405 |
Uniprot Accession Number | Q8MZM7 |
Absorption | |
Active Site | ACT_SITE 182; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274; ACT_SITE 249; /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 | |
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:16935219, PubMed:26926112). Preferentially, cleaves substrates with an arginine at the P1 site (PubMed:26926112). May be involved in the activation of the prophenoloxidase cascade upstream of CLIPB9; does not cleave prophenoloxidase (PubMed:26926112). {ECO:0000269|PubMed:16935219, ECO:0000269|PubMed:26926112}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Chain (1); Disulfide bond (3); Domain (2); Glycosylation (2); 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:0000305}. |
Modified Residue | |
Post Translational Modification | PTM: Proteolytic cleavage is necessary for activation. {ECO:0000269|PubMed:26926112}. |
Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 44,763 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |