| Activity |
|---|
| Catalytic type | Serine |
| Peplist | Included in the Peplist with identifier PL00312 |
| NC-IUBMB | Subclass 3.4 (Peptidases) >> Sub-subclass 3.4.21 (Serine endopeptidases) >> Peptidase 3.4.21.69
|
| Enzymology | BRENDA database |
| Proteolytic events | CutDB database (9 cleavages) |
| Activity status | human: active (Shen & Dahlback, 2004)
mouse: active (by similarity) (Tada et al., 1992)
|
| Physiology | Human activated protein C (APC) is an antithrombotic, antiinflammatory serine protease. It proteolytically destroys active coagulation factors Va and VIIIa, thus interfering in thrombin activation. |
| Knockout | Human mutations lead to hyper-coagulability disorders (Lind et al., 2002). See also OMIM. |
| Pharmaceutical relevance | Success in altering the substrate specificity and in vivo activity of activated protein C by mutagenesis suggests that there may be therapeutic opportunities for the use of protein C derivatives in disease states with elevated serine protease inhibitor levels (Berg et al., 2003). Recombinant activated protein C (as drotrecogin alfa) is distributed for therapeutic use (McLeay, 2004). |
| Pathways |
KEGG | Complement and coagulation cascades |
|
Other databases
| WIKIPEDIA | http://en.wikipedia.org/wiki/Protein_C |
| Cleavage site specificity |
Explanations of how to interpret the
following cleavage site sequence logo and specificity matrix can be found here. |
|---|
| Cleavage pattern | -/d/pt/R sgm/-/-/- (based on 15 cleavages) |
