CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.40 | Beta Barrel |
|
2.40.10 | Thrombin, subunit H |
|
2.40.10.10 | Trypsin-like serine proteases |
Domain Context
CATH Clusters
| Superfamily | Trypsin-like serine proteases |
| Functional Family |
Enzyme Information
| 3.4.21.109 |
Matriptase.
based on mapping to UniProt Q9Y5Y6
Cleaves various synthetic substrates with Arg or Lys at the P1 position and prefers small side-chain amino acids, such as Ala and Gly, at the P2 position.
-!- This trypsin-like integral-membrane serine peptidase has been implicated in breast cancer invasion and metastasis. -!- Can activate hepatocyte growth factor/scattering factor (HGF/SF) by cleavage of the two-chain form at an Arg residue to give active alpha- and beta-HGF, but it does not activate plasminogen, which shares high homology with HGF. -!- Can also activate urokinase plasminogen activator (uPA), which initiates the matrix-degrading peptidase cascade. -!- Belongs to peptidase family S1A.
|
UniProtKB Entries (1)
| Q9Y5Y6 |
ST14_HUMAN
Homo sapiens
Suppressor of tumorigenicity 14 protein
|
PDB Structure
| PDB | 3NCL |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Peptide length and leaving-group sterics influence potency of Peptide phosphonate protease inhibitors.
Chem.Biol.
|
