View in Gene3D

CATH Superfamily 2.40.10.10

Trypsin-like serine proteases

The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:

"
Trypsin-like serine proteases
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
« Back to all FunFams

FunFam 47593: Transmembrane protease serine 7

There are 4 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Matriptase. [EC: 3.4.21.109]
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.
 4 Q63ZQ6 Q63ZQ6 Q9DGR1 Q9DGR1
Trypsin. [EC: 3.4.21.4]
Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
  • Belongs to peptidase family S1.
  • Formerly EC 3.4.4.4.
 4 B7P9J0 B7P9J0 Q1D193 Q1D193
Tryptase. [EC: 3.4.21.59]
Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa, but with more restricted specificity than trypsin.
  • Occurs as a tetrameric molecule with high affinity for heparin, in mast cell granules.
  • Not inhibited by alpha-1-proteinase inhibitor of alpha-2- macroglobulin.
  • Belongs to peptidase family S1.
 2 B7P211 B7P211
Plasmin. [EC: 3.4.21.7]
Preferential cleavage: Lys-|-Xaa > Arg-|-Xaa; higher selectivity than trypsin. Converts fibrin into soluble products.
  • Formed from plasminogen by proteolysis which results in multiple forms of the active plasmin.
  • Belongs to peptidase family S1.
  • Formerly EC 3.4.4.14.
 2 B7PC98 B7PC98