CATH Classification

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 (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.