| IED ID | IndEnz0002008156 |
| Enzyme Type ID | protease008156 |
| Protein Name |
N-V protease EC 3.4.21.- Fragments |
| Gene Name | |
| Organism | Alitta virens (Sandworm) (Nereis virens) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Spiralia Lophotrochozoa Annelida Polychaeta (polychaetes) Errantia Phyllodocida Nereididae (sandworms) Alitta Alitta virens (Sandworm) (Nereis virens) |
| Enzyme Sequence | QAPNYSTASYNVVAVKINLFLSTNNKLYIHDTGVRAVYLAGMKVYLAANPTASSQTFNSDTLVYILDTGINEPNYYINLY |
| Enzyme Length | 80 |
| Uniprot Accession Number | P83433 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by the serine protease inhibitors DFP, PMSF and TLCK. Not inhibited by the serine protease inhibitors aprotinin, elastinal, SBTI and benzamidine, the cysteine protease inhibitors iodoacetate and E64, or the metalloprotease inhibitors EDTA and EGTA. {ECO:0000269|PubMed:16950556}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Serine protease. Hydrolyzes the alpha chains of fibrin and fibrinogen completely, has lower activity on the beta and gamma chains of fibrin and fibrinogen. {ECO:0000269|PubMed:16950556}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius. Active from 30 to 55 degrees Celsius. {ECO:0000269|PubMed:16950556}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.8. Active from pH 4.0 to pH 9.0. {ECO:0000269|PubMed:16950556}; |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Non-adjacent residues (9); Non-terminal residue (2) |
| Keywords | Blood coagulation;Direct protein sequencing;Fibrinolysis;Hemostasis;Hydrolase;Protease;Secreted;Serine protease |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.2}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 8,888 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |