| IED ID | IndEnz0002009895 |
| Enzyme Type ID | protease009895 |
| Protein Name |
Secapin AcSecapin-1 |
| Gene Name | |
| Organism | Apis cerana (Indian honeybee) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Hymenoptera Apocrita (wasps ants and bees) Aculeata Apoidea (bees) Apidae (bumble bees and honey bees) Apinae (honey bees) Apini Apis Apis cerana (Indian honeybee) |
| Enzyme Sequence | MRFQVYILHLCFFILVVLTYLSQGQSYTTTTTTSTTEQPTFLQKIHETFKKVKENAKIHNLYIFDPPTWIYTTTTEKPVESTENFDITNRQLITVPVRCPPNYDFIKGRCREKIP |
| Enzyme Length | 115 |
| Uniprot Accession Number | A0A0K1YW63 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Serine protease inhibitor which exhibits antifibrinolytic, antielastolytic and antimicrobial activities (PubMed:27208884). Displays antimicrobial activity against bacteria and fungi (PubMed:27208884). Likely functions in the innate immune response to microbial infection and possibly in the venom, as an antifibrinolytic agent (PubMed:27208884). The recombinant form inhibits trypsin (IC(50)=80.02 nM, Ki=127.25 nM), chymotrypsin (IC(50)=393.78 nM, Ki=432.59 nM), the microbial serine proteases subtilisin A (IC(50)=379.20 nM, Ki=492.77 nM) and proteinase K (IC(50)=189.43 nM, Ki=271.76 nM), plasmin (IC(50)=457.98 nM, Ki=502.91 nM), human elastase (IC(50)=347.81 nM, Ki=469.90 nM) and porcine elastase (IC(50)=94.70 nM, Ki=125.62 nM) (PubMed:27208884). Does not inhibit thrombin (PubMed:27208884). Binds to human plasmin and inhibits the plasmin-mediated degradation of fibrin to fibrin degradation products (PubMed:27208884). Also binds to bacterial and fungal surfaces and exhibits antimicrobial activity against the Gram-positive bacteria B.thuringiensis (MIC=4.21 uM) and P.larvae (MIC=11.13 uM), the Gram-negative bacterium E.coli (MIC=6.50 uM), and the fungus B.bassiana (IC(50)=2.57 uM) (PubMed:27208884). The synthetic peptide also exhibits antimicrobial activity against the Gram-positive bacterium P.larvae (MIC=41.12 uM), the Gram-negative bacterium P.aeruginosa (MIC=65.75 uM), and the fungus B.bassiana (IC(50)=44.27 uM) (Ref.2). In vitro it does not induce an inflammatory response and has no cytotoxic activity against mouse embryo cells (Ref.2). {ECO:0000269|PubMed:27208884, ECO:0000269|Ref.2}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Antibacterial activity against P.aeruginosa is retained between 25 and 90 degrees Celsius. {ECO:0000269|Ref.2}; |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Disulfide bond (1); Peptide (1); Propeptide (1); Signal peptide (1) |
| Keywords | Antibiotic;Antimicrobial;Disulfide bond;Fungicide;Immunity;Innate immunity;Protease inhibitor;Secreted;Serine protease inhibitor;Signal |
| Interact With | |
| Induction | INDUCTION: Up-regulated in the fat body after injection with bacteria (B.thuringiensis, P.larvae or E.coli) or the fungus B.bassiana. {ECO:0000269|PubMed:27208884}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:27208884}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 13,570 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |