Cloned (Comment) | Organism |
---|---|
gene PROC, location on chromosome 1p13-14 | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
additional information | knockout mice show perinatal lethality, reduced enzyme levels permit birth and growth but lead to thrombosis and inflammation with an early onset | Mus musculus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
active factor Va + H2O | Homo sapiens | proteolytic inactivation | inactive factor V + ? | - |
? | |
active factor VIIIa + H2O | Homo sapiens | proteolytic inactivation | inactive factor VIII + domain B | - |
? | |
additional information | Homo sapiens | the enzyme has anticoagulant, antiapoptotic, and cytoprotective activities, mechanisms, overview, severe homozygous enzyme-deficiency causes massive, usually lethal thrombotic complications that arise in infants, heterozygous adults show a risk for venous thrombosis | ? | - |
? | |
additional information | Mus musculus | the enzyme has anticoagulant, antiapoptotic, and cytoprotective activities, murine injury models, mechanisms, overview | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
gene PROC | - |
Mus musculus | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
glycoprotein | N-glycosylation of residues 97, 248, 313, and 329 | Homo sapiens |
proteolytic modification | proteolytic cleavage and activation by thrombin at Arg169 removing the activation peptide, thrombomodulin and endothelial cell protein C receptor PAR-1 are required for efficient enzyme activation | Homo sapiens |
proteolytic modification | proteolytic cleavage and activation by thrombin removing the activation peptide, thrombomodulin and endothelial cell protein C receptor PAR-1 are required for efficient enzyme activation | Mus musculus |
side-chain modification | beta-hydroxylation of Asp71, and carboxylation of nine glutamic acid residues in the N-terminus | Homo sapiens |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
degradation of blood coagulation factors Va and VIIIa | the catalytic triad is formed by His211, Asp257, and Ser360 | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
active factor Va + H2O | proteolytic inactivation | Homo sapiens | inactive factor V + ? | - |
? | |
active factor VIIIa + H2O | proteolytic inactivation | Homo sapiens | inactive factor VIII + domain B | - |
? | |
additional information | the enzyme has anticoagulant, antiapoptotic, and cytoprotective activities, mechanisms, overview, severe homozygous enzyme-deficiency causes massive, usually lethal thrombotic complications that arise in infants, heterozygous adults show a risk for venous thrombosis | Homo sapiens | ? | - |
? | |
additional information | the enzyme has anticoagulant, antiapoptotic, and cytoprotective activities, murine injury models, mechanisms, overview | Mus musculus | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | the enzyme contains the N-terminal Gladomain, residues 1-37, two epidermal growth factor-like regions, residues 46-92 and 93-136, an activation peptide, residues 158-169, and the serine protease domain, residue 170-419 | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
Activated protein C | - |
Mus musculus |
Activated protein C | - |
Homo sapiens |
APC | - |
Mus musculus |
APC | - |
Homo sapiens |