| IED ID | IndEnz0002014583 |
| Enzyme Type ID | protease014583 |
| Protein Name |
Actinia tenebrosa protease inhibitors Carboxypeptidase inhibitor SmCI-like Cleaved into: ATPI-I; ATPI-II |
| Gene Name | |
| Organism | Actinia tenebrosa (Australian red waratah sea anemone) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Cnidaria Anthozoa (anthozoans) Hexacorallia Actiniaria (sea anemones) Actiniidae Actinia Actinia tenebrosa (Australian red waratah sea anemone) |
| Enzyme Sequence | MARTASTILFLLCLVLITGYTMARQEHCNLPLEKGKCGGRFERFYYNSHKGKCESFFYGGCSGNDNNFENEEECDKACGAFMTMADANSFCNLPAVVGRCKGYFPRYFYNTEAGKCQRFIYGGCGGNRNNFETVXDCRATCHPREKRALADMTMADANSFCQLPAVVGRCRGRFPRYYYNTEAGKCQRFIYGGCXGNRNNFETVEDCRATCHPREKRALADMTMADANSFCQLPAVVGKCRGYFPRYYYNTEAGKCQQFIYGGCGGNRNNFETVEDCRATCHSHA |
| Enzyme Length | 285 |
| Uniprot Accession Number | A0A6P8HC43 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: [ATPI-I]: May be involved in regulating functions and processes within the digestive system (Probable). Shows serine protease inhibitory activities (PubMed:31842369). Strongly inhibits trypsin (Ki=0.05 nM), chymotrypsin (Ki=7.4 nM), and kallikreins (KLK5, KLK7 and KLK14) (PubMed:31842369). {ECO:0000269|PubMed:31842369, ECO:0000305|PubMed:31842369}.; FUNCTION: [ATPI-II]: May be involved in regulating functions and processes within the digestive system (Probable). Shows serine protease inhibitory activities (PubMed:31842369). Strongly inhibits trypsin (Ki=0.08 nM), chymotrypsin (Ki=2.9 nM), and kallikreins (KLK5, KLK7 and KLK14) (PubMed:31842369). {ECO:0000269|PubMed:31842369, ECO:0000305|PubMed:31842369}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: [ATPI-I]: Temperature dependence: Is resistant to heat-induced denaturation (95 degrees Celsius). {ECO:0000269|PubMed:31842369}; |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (2); Disulfide bond (12); Domain (4); Propeptide (2); Signal peptide (1) |
| Keywords | Cleavage on pair of basic residues;Direct protein sequencing;Disulfide bond;Ion channel impairing toxin;Nematocyst;Potassium channel impairing toxin;Protease inhibitor;Reference proteome;Repeat;Secreted;Serine protease inhibitor;Signal;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0DMW6}. Nematocyst {ECO:0000250|UniProtKB:P0DMW6}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 32,113 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |