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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 3: Transmembrane serine protease 3

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
Hepsin. [EC: 3.4.21.106]
Cleavage after basic amino-acid residues, with Arg strongly preferred to Lys.
  • This type-II membrane-associated serine peptidase has been implicated in cell growth and development.
  • The enzyme has been shown to activate blood coagulation factor VII by cleavage of the 152-Arg-|-Ile-153 peptide bound in BHK cells, thus indicating a possible role in the initiation of blood coagulation.
  • There is no cleavage after aromatic or aliphatic residues.
  • The occupancy of the S2 site is an absolute requirement for catalysis and a basic residue at that site is preferred to an aliphatic residue.
  • The nature of the residue at S3 also affects hydrolysis, with Gln being much more favorable than Ala.
  • Belongs to peptidase family S1A.
 17 A0A140VJK9 A0A140VJK9 A0A140VJK9 A0A140VJK9 A0A2J8QH94 A0A2J8QH94 A0A2J8QH94 A0A2J8QH94 A0A2R9AW56 A0A2R9AW56
(7 more...)
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.
 9 P00747 P06867 P06868 P12545 P20918 P80009 P80010 Q01177 Q5R8X6
Plasma kallikrein. [EC: 3.4.21.34]
Cleaves selectively Arg-|-Xaa and Lys-|-Xaa bonds, including Lys-|-Arg and Arg-|-Ser bonds in (human) kininogen to release bradykinin.
  • Formed from plasma prokallikrein (Fletcher factor) by factor XIIa.
  • Activates coagulation factors XII, VII and plasminogen.
  • Selective for Arg > Lys in P1, in small molecule substrates.
  • Belongs to peptidase family S1.
  • Formerly EC 3.4.4.21 and EC 3.4.21.8.
 7 H9H9R5 H9H9R5 P03952 P14272 P26262 P26262 Q2KJ63
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 Q91Y47
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