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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_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 2: Transmembrane protease serine

There are 5 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
T-plasminogen activator. [EC: 3.4.21.68]
Specific cleavage of Arg-|-Val bond in plasminogen to form plasmin.
  • From a wide variety of mammalian tissues, especially endothelial cells.
  • Secreted as a single chain precursor which is cleaved to a two-chain form by plasmin.
  • Activity is considerably enhanced by fibrin.
  • Belongs to peptidase family S1.
  • Formerly EC 3.4.21.31 and EC 3.4.99.26.
 9 A0A480NSF2 A0A480NSF2 P00750 P11214 P19637 Q28198 Q5R8J0 Q8SQ23 Q8SQ23
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.
 7 P08001 P10323 P23578 P29293 P48038 Q2UVH8 Q9GL10
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
Coagulation factor XIa. [EC: 3.4.21.27]
Selective cleavage of Arg-|-Ala and Arg-|-Val bonds in factor IX to form factor IXa.
  • The proenzyme XI is activated by EC 3.4.21.38.
  • Belongs to peptidase family S1.
 1 P03951