IED ID |
IndEnz0002003218 |
Enzyme Type ID |
protease003218 |
Protein Name |
Hirudin-PA
|
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 |
ITYTDCTESGQNLCLCEGSNVCGKGNKCILGSQGKDNQCVTGEGTPKPQSHNQGDFEPIPEDAYDE |
Enzyme Length |
66 |
Uniprot Accession Number |
P09944 |
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); 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 64; /note=Sulfotyrosine; /evidence=ECO:0000269|PubMed:3768144 |
Post Translational Modification |
|
Signal Peptide |
|
Structure 3D |
X-ray crystallography (1) |
Cross Reference PDB |
1IHT;
|
Mapped Pubmed ID |
8272424;
|
Motif |
|
Gene Encoded By |
|
Mass |
7,026 |
Kinetics |
|
Metal Binding |
|
Rhea ID |
|
Cross Reference Brenda |
|