IED ID | IndEnz0002004191 |
Enzyme Type ID | protease004191 |
Protein Name |
Hirudin-1A Hirudin IA Fragment |
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 | VVYTDCTESGQNLCLCE |
Enzyme Length | 17 |
Uniprot Accession Number | P28502 |
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); Non-terminal residue (1); Region (1) |
Keywords | Direct protein sequencing;Protease inhibitor;Secreted;Serine protease inhibitor;Sulfation |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
Modified Residue | |
Post Translational Modification | PTM: Sulfated. {ECO:0000250}. |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 1,877 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |