CATH Classification

Domain Context

CATH Clusters

Superfamily Trypsin-like serine proteases
Functional Family Transmembrane serine protease 7

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 (2)

P00974
BPT1_BOVIN
Bos taurus
Pancreatic trypsin inhibitor
Q9Y5Y6
ST14_HUMAN
Homo sapiens
Suppressor of tumorigenicity 14 protein

PDB Structure

PDB 1EAW
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Catalytic Domain Structures of Mt-Sp1/Matriptase, a Matrix-Degrading Transmembrane Serine Proteinase.
Friedrich, R., Fuentes-Prior, P., Ong, E., Coombs, G., Hunter, M., Oehler, R., Pierson, D., Gonzalez, R., Huber, R., Bode, W., Madison, E.L.
J.Biol.Chem.