| IED ID | IndEnz0002015860 |
| Enzyme Type ID | protease015860 |
| Protein Name |
CLIP domain-containing serine protease B15 EC 3.4.21.- |
| Gene Name | ser3 CLIPB15 AGAP009844 |
| 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 | MRWLVCLIVSWCSLVPLGATVGQSLNSGDPCQTPSGTAGTCEPVKNCSYVRKILKSPDFSHYDTTYLDTLKCGDLMVPMRKKPIPLLCCPKFSNSPTCGAQQLADRIYFGEETERGAHPWAALLFYNVGRNRTVPKCGGALISERYVITAAHCTVDKPNWKLLYVRFNEFNTSSADNCTTENDEVICREDYAVESIVPHPEYDMHNISRPNDICILRLASDVTFNDYVRPICLPFDPDVQQLPIVDEIFTVTGWGETEDRRPSDTQKHVELPGLEHEACNSVYAVANVTLSDKQLCIGGLNGSDSCRGDSGGPLMREVRGGWFLIGVVSFGARFCGTQNLPGVYTNVAKYLDWMETVMFVERYL |
| Enzyme Length | 364 |
| Uniprot Accession Number | Q9NAS9 |
| Absorption | |
| Active Site | ACT_SITE 152; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274; ACT_SITE 212; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274; ACT_SITE 310; /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 protease (By similarity). Plays a role in innate immunity against infections by parasite P.berghei and by Gram-negative bacteria such as E.coli (PubMed:16188883). In response to P.berghei infection, contributes to the clearing of parasite ookinetes independent of melanization, an innate immune response which consists in the deposition of melanin pigments on invading pathogens and parasites (PubMed:16188883). {ECO:0000250|UniProtKB:A0A126GUP6, ECO:0000269|PubMed:16188883}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (7); Domain (2); Glycosylation (7); Signal peptide (1) |
| Keywords | Disulfide bond;Glycoprotein;Hydrolase;Immunity;Innate immunity;Protease;Reference proteome;Secreted;Serine protease;Signal |
| Interact With | |
| Induction | INDUCTION: Induced by infection with E.coli or S.aureus bacteria. Induced by infection with P.berghei parasite following ookinete invasion of the midgut cells. {ECO:0000269|PubMed:16188883}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16188883}. Note=Secreted in the hemolymph. {ECO:0000269|PubMed:16188883}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. {ECO:0000269|PubMed:16188883}.; PTM: May be proteolytically cleaved. {ECO:0000305|PubMed:16188883}. |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 40,555 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |