| IED ID | IndEnz0002011382 |
| Enzyme Type ID | protease011382 |
| Protein Name |
PI-stichotoxin-Hmg3d PI-SHTX-Hmg3d IQ-peptide Kunitz-type serine protease inhibitor HMIQ3c1 Fragment |
| Gene Name | |
| Organism | Heteractis magnifica (Magnificent sea anemone) (Radianthus magnifica) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Cnidaria Anthozoa (anthozoans) Hexacorallia Actiniaria (sea anemones) Stichodactylidae Heteractis Heteractis magnifica (Magnificent sea anemone) (Radianthus magnifica) |
| Enzyme Sequence | GFYFRSIQGFYFKRIQGNICSEPKKVGRCRGSFPRFYFDSETGKCTPFIYGGCGGNGNNFETLRRCRAICRA |
| Enzyme Length | 72 |
| Uniprot Accession Number | A0A3G2FQK2 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Serine protease inhibitor that inhibits trypsin (Ki=50 nM). This protease exhibits a pronounced neuroprotective activity on Alzheimer's disease model. It enhances cell viability by 39.4% when neuroblastoma cells are in presence of the toxin component beta-amyloid, but has no effect when these cells are in presence of 6-OHDA. {ECO:0000269|Ref.1}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Disulfide bond (3); Domain (1); Non-terminal residue (1); Signal peptide (1) |
| Keywords | Cleavage on pair of basic residues;Disulfide bond;Nematocyst;Protease inhibitor;Secreted;Serine protease inhibitor;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0DMJ5}. Nematocyst {ECO:0000250|UniProtKB:P0DMJ5}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL <1..14; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 8,238 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |