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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 90: serine protease hepsin

There are 1 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.
 2 O35453 Q05511
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