The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_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.
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FunFam 7: Transmembrane serine protease 7

There are 3 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.
6 P56677 P56677 Q0IIH7 Q543E3 Q543E3 Q9Y5Y6
Enteropeptidase. [EC: 3.4.21.9]
Activation of trypsinogen by selective cleavage of 6-Lys-|-Ile-7 bond.
  • Activates trypsinogen.
  • Not inhibited by protein inhibitors of trypsin.
  • Belongs to peptidase family S1.
  • Formerly EC 3.4.4.8.
4 P97435 P98072 P98073 P98074
Acrosin. [EC: 3.4.21.10]
Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
  • Inhibited by naturally occurring trypsin inhibitors.
  • Occurs in spermatozoa.
  • Belongs to peptidase family S1.
1 Q2UVH8