| Signal peptide(a) |
Y |
Secretome P(b) |
0.505 |
| Function |
Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase. |
| GO - Molecular function |
- brain-derived neurotrophic factor binding : IDA:RGD
- endopeptidase inhibitor activity : IDA:RGD
- nerve growth factor binding : IDA:RGD
- protein homodimerization activity : IDA:RGD
- serine-type endopeptidase inhibitor activity : IEA:UniProtKB-KW
|
| GO - Biological process |
- acute inflammatory response to antigenic stimulus : IEP:RGD
- acute-phase response : IEP:RGD
- embryonic liver development : IEP:RGD
- luteinization : IEP:RGD
- negative regulation of endopeptidase activity : IDA:RGD
- protein homotetramerization : IDA:RGD
- response to carbon dioxide : IEP:RGD
- response to glucocorticoid : IEP:RGD
- response to nutrient : IEP:RGD
- response to prostaglandin E : IEP:RGD
- response to wounding : TAS:RGD
|