IED ID | IndEnz0002002016 |
Enzyme Type ID | protease002016 |
Protein Name |
Hirudin-3A' Hirudin IIIA' |
Gene Name | |
Organism | Hirudo medicinalis (Medicinal leech) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Spiralia Lophotrochozoa Annelida Clitellata Hirudinea (leeches) Hirudinida Hirudiniformes Hirudinidae Hirudo Hirudo medicinalis (Medicinal leech) |
Enzyme Sequence | VVYTDCTESGEDLCLCEGSNVCGEGNKCILGSDGEKNECVTGEGTPKPQSHNDGDFEEIPEEYLQ |
Enzyme Length | 65 |
Uniprot Accession Number | P28508 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | FUNCTION: Hirudin is a potent thrombin-specific protease inhibitor. It forms a stable non-covalent complex with alpha-thrombin, thereby abolishing its ability to cleave fibrinogen. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Disulfide bond (3); Glycosylation (1); Helix (1); Modified residue (1); Region (3) |
Keywords | 3D-structure;Direct protein sequencing;Disulfide bond;Glycoprotein;Protease inhibitor;Secreted;Serine protease inhibitor;Sulfation |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
Modified Residue | MOD_RES 63; /note=Sulfotyrosine; /evidence=ECO:0000250 |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | X-ray crystallography (9) |
Cross Reference PDB | 1DWB; 1DWC; 1DWD; 1DWE; 2CF8; 2CF9; 4AYV; 4AYY; 4AZ2; |
Mapped Pubmed ID | 1304349; 1587268; 16763681; 1939071; 2226434; 2369893; 2374926; 2583108; 7966150; |
Motif | |
Gene Encoded By | |
Mass | 6,973 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |