| IED ID | IndEnz0002015918 |
| Enzyme Type ID | protease015918 |
| Protein Name |
CLIP domain-containing serine protease HP8 EC 3.4.21.- BzArgOEtase BAEEase Hemolymph proteinase 8 HP8 Cleaved into: CLIP domain-containing serine protease HP8 light chain; CLIP domain-containing serine protease HP8 heavy chain |
| Gene Name | |
| Organism | Bombyx mori (Silk moth) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Amphiesmenoptera Lepidoptera (butterflies and moths) Glossata Neolepidoptera Heteroneura Ditrysia Obtectomera Bombycoidea (hawk-moths) Bombycidae (silkworm moths) Bombycinae Bombyx Bombyx mori (Silk moth) |
| Enzyme Sequence | MKTPFEKIRIISCILVIVSTNVVGQKCNGGANCIPLEECTDLFQQLKQGNSPQLTRLLRGLHCGFEDLNSPKICCPPEFLARRSAFSSAGTNSNPTSILPNEKVCGIQNNDRIFGGIQTEIDEHPWMALLRYDKPLGWGFYCGGVLIAPMYVLTAAHCVKGSDLPSSWQLSQVRLGEWNTSTETDCVEGDCSGPVQDIPVQQIIAHENYDPNDKDQQNDIALLRLSRNAQFNDFVSPICLPTSNELRQNEFESDYMEVAGWGKTETRSESDVKLKVRVPIVNREECANVYSNVDRRVTNKQICAGGLAGRDSCRGDSGGALMGQSPKANNWYVFGVVSYGPSPCGTEGWPGVYTRVGSFMDWILSKLEQ |
| Enzyme Length | 369 |
| Uniprot Accession Number | Q2VG86 |
| Absorption | |
| Active Site | ACT_SITE 157; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274; ACT_SITE 219; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274; ACT_SITE 317; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by (p-amidinophenyl) methanesulfonyl fluoride, p-nitrophenyl-p'-guanidinobenzoate, D-phenylalanyl-L-prolyl-L-arginyl chloromethane, leupeptin, antipain and to a lesser extent by antithrombin III. {ECO:0000269|PubMed:7737188}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Endopeptidase with selective post-Arg cleavage site (PubMed:16399077, PubMed:7737188). Functions in the innate immune response to fungal and Gram-positive bacterial infections (PubMed:16399077, PubMed:26707571, PubMed:34022191). Upon pathogen infection promotes nodulation; a cellular defense response in which hemocytes surround and isolate invading pathogens forming aggregates called nodules (PubMed:26707571, PubMed:34022191). Involved in activating nodule formation in response to infection with M.luteus, E. coli or S.cerevisiae (PubMed:34022191). Able to bind the microbes M.luteus, E. coli or S.cerevisiae (PubMed:34022191). According to another report, does not bind microorganisms (PubMed:26707571). {ECO:0000269|PubMed:16399077, ECO:0000269|PubMed:26707571, ECO:0000269|PubMed:34022191, ECO:0000269|PubMed:7737188}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (2); Disulfide bond (8); Domain (2); Erroneous gene model prediction (1); Frameshift (1); Glycosylation (1); Metal binding (4); Propeptide (1); Signal peptide (1); Site (2) |
| Keywords | Calcium;Cleavage on pair of basic residues;Cytoplasm;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Metal-binding;Protease;Reference proteome;Secreted;Serine protease;Signal;Zymogen |
| Interact With | |
| Induction | INDUCTION: Up-regulated in plasma in response to infection with S.cerevisiae and M.luteus. {ECO:0000269|PubMed:26707571}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16399077, ECO:0000269|PubMed:26707571, ECO:0000269|PubMed:7737188}. Cytoplasm {ECO:0000269|PubMed:26707571}. Note=In larvae, secreted in the hemolymph (PubMed:16399077, PubMed:7737188, PubMed:26707571). Only the uncleaved form is detected in hemolymph (PubMed:26707571). Uncleaved (42 kDa) and cleaved (29 kDa) forms, are weakly expressed in hemocytes (PubMed:26707571). Detected in the cytoplasm of various hemocytes including plasmatocytes, oenocytoids, granulocytes and prohemocytes (PubMed:26707571). Cleaved and uncleaved forms also localize to immune defense nodules that have been induced by injection with E.coli, M.luteus or S.cerevisiae cells (PubMed:26707571). {ECO:0000269|PubMed:16399077, ECO:0000269|PubMed:26707571, ECO:0000269|PubMed:7737188}. |
| Modified Residue | |
| Post Translational Modification | PTM: Proteolytically cleaved for activation (PubMed:16399077). Cleavage produces a light chain and a catalytic heavy chain which remains covalently associated probably through an interchain disulfide bond (Probable). {ECO:0000269|PubMed:16399077, ECO:0000305|PubMed:16399077}. |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000269|PubMed:16399077 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 40,744 |
| Kinetics | |
| Metal Binding | METAL 177; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q9VB68; METAL 179; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:O97366; METAL 182; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q9VB68; METAL 185; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q9VB68 |
| Rhea ID | |
| Cross Reference Brenda |