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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_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.
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FunFam 46285: Protease serine 2 preproprotein

There are 12 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
Trypsin. [EC: 3.4.21.4]
Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
  • Belongs to peptidase family S1.
  • Formerly EC 3.4.4.4.
 198 A0A061IH12 A0A061IH12 A0A061ILH1 A0A061ILH1 A0A061IMN7 A0A061IMN7 A0A0B4LF52 A0A0B4LF52 A0A0K2B0R9 A0A0K2B0R9
(188 more...)
Tissue kallikrein. [EC: 3.4.21.35]
Preferential cleavage of Arg-|-Xaa bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-|-Xaa or Leu-|-Xaa.
  • Formed from tissue prokallikrein by activation with trypsin.
  • A large number of tissue kallikrein-related sequences have been reported for rats and mice, though fewer seem to exist in other mammals.
  • The few that have been isolated and tested on substrates include mouse EC 3.4.21.54, submandibular proteinase a, epidermal growth- factor-binding protein, nerve growth factor gamma-subunit, rat tonin, submaxillary proteinases A and B, T-kininogenase, kallikreins K7 and K8.
  • The rat enzyme is unusual in liberating bradykinin directly from autologous kininogens by cleavage at two Arg-|-Xaa bonds.
  • Belongs to peptidase family S1.
  • Formerly EC 3.4.21.8.
 68 A0A024R4J4 A0A024R4J4 A0A0B6VSQ6 A0A0B6VSQ6 P00752 P00752 P00755 P00755 P00756 P00756
(58 more...)
Venombin A. [EC: 3.4.21.74]
Selective cleavage of Arg-|-Xaa bond in fibrinogen, to form fibrin, and release fibrinopeptide A. The specificity of further degradation of fibrinogen varies with species origin of the enzyme.
  • A somewhat thrombin-like enzyme from venoms of snakes of the viper/rattlesnake group.
  • Species variants of the enzyme include ancrod from Agkistrodon rhodostoma (Malayan pit viper), batroxobin from Bothrops atrox (South American pit viper) and crotalase from Crotalus adamanteus (Eastern diamondback rattlesnake).
  • Does not require activation by calcium.
  • Belongs to peptidase family S1.
  • Formerly EC 3.4.21.28, EC 3.4.21.29 and EC 3.4.21.30.
 22 A0A0F7Z2N9 A0A0F7Z2N9 F8S114 F8S114 J3S3W5 J3S3W5 P04971 P04971 P05620 P05620
(12 more...)
Semenogelase. [EC: 3.4.21.77]
Preferential cleavage: -Tyr-|-Xaa-.
  • Slowly inhibited by alpha-1-antichymotrypsin.
  • Belongs to peptidase family S1.
 10 G7NMC9 G7NMC9 P07288 P07288 P33619 P33619 Q546G3 Q546G3 Q6DT45 Q6DT45
Kallikrein 8. [EC: 3.4.21.118]
Cleavage of amide substrates following the basic amino acids Arg or Lys at the P1 position, with a preference for Arg over Lys.
  • Activated by removal of an N-terminal prepropeptide.
  • The highest amidolytic activity is observed using Boc-Val-Pro- Arg-|-7-amido-4-methylcoumarin, which is a substrate of alpha- thrombin.
  • Substrates lacking basic amino acids in the P1 position are not cleaved.
  • Degrades casein, fibronectin, gelatin, collagen type IV, fibrinogen, and high-molecular-mass kininogen and is associated with diseases such as ovarian cancer and Alzheimer's disease.
  • Belongs to peptidase family S1A.
 8 A0A0B6VRH9 A0A0B6VRH9 O60259 O60259 O88780 O88780 Q61955 Q61955
Stratum corneum chymotryptic enzyme. [EC: 3.4.21.117]
Cleavage of proteins with aromatic side chains in the P1 position.
  • This enzyme has wide substrate specificity, being able to degrade heat-denatured bovine casein and the alpha-chain of native human fibrinogen.
  • It cleaves the B chain of bovine insulin at 6-Leu-|-Cya-7 (cysteic acid), 16-Tyr-|-Leu-17, 25-Phe-|-Tyr-26 and 26-Tyr-|-Thr-27.
  • It is thought to play a role in the desquamation (skin-shedding) of the outer layer of skin, the stratum corneum, by degrading intercellular cohesive structures.
  • Belongs to peptidase family S1A.
 8 A0A024R4H6 A0A024R4H6 A0A0B6VPC4 A0A0B6VPC4 P49862 P49862 Q91VE3 Q91VE3
Snake venom factor V activator. [EC: 3.4.21.95]
Fully activates human clotting factor V by a single cleavage at the 1545- Trp-Tyr-Leu-Arg-|-Ser-Asn-Asn-Gly-1552 bond. Cattle, but not rabbit, factor V is cleaved, and no other proteins of the clotting system are attacked. Esterase activity is observed on Bz-Arg-OEt and Tos-Arg-OMe, and amidase activity on Phe-pipecolyl-Arg-NHPhNO(2).
  • Inhibited by diisopropyl fluorophosphate.
  • Belongs to peptidase family S1.
 6 P18964 P18964 P18965 P18965 Q9PT41 Q9PT41
Chymotrypsin. [EC: 3.4.21.1]
Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.
  • Belongs to peptidase family S1.
  • Formerly EC 3.4.4.5 and EC 3.4.4.6.
 4 B7QID0 B7QID0 C7DY49 C7DY49
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.
 4 A0A031H1I6 A0A031H1I6 B8L3K5 B8L3K5
Pancreatic elastase II. [EC: 3.4.21.71]
Preferential cleavage: Leu-|-Xaa, Met-|-Xaa and Phe-|-Xaa. Hydrolyzes elastin.
  • Formed by activation of proelastase II from mammalian pancreas by trypsin.
  • Usually, only one of the pancreatic elastases (see also EC 3.4.21.36) is expressed in a given species; human pancreatic elastase is of type II.
  • Belongs to peptidase family S1.
 2 B7QNU3 B7QNU3
Gamma-renin. [EC: 3.4.21.54]
Cleavage of the Leu-|-Leu bond in synthetic tetradecapeptide renin substrate, to produce angiotensin I, but not active on natural angiotensinogen. Also hydrolyzes Bz-Arg-p-nitroanilide.
  • Unlike EC 3.4.23.15, does not act on natural angiotensinogen.
  • A member of the tissue kallikrein family, from submandibular glands of male mice.
  • Belongs to peptidase family S1.
 2 P04071 P04071
Kallikrein 13. [EC: 3.4.21.119]
Hydrolyzes mouse Ren2 protein (a species of prorenin present in the submandibular gland) on the carboxy side of the arginine residue at the Lys-Arg-|- pair in the N-terminus, to yield mature renin.
  • Specific for prorenin from the mouse submandibular gland, as prorenin from the mouse kidney (Ren1) and human prorenin are not substrates.
  • Site-directed mutagenesis studies have shown that the enzyme will also cleave prorenin when Lys-Arg is replaced by Arg-Arg or Gln-Arg but the rate of reaction is much slower when Lys-Lys is used.
  • Also able to process pro-interleukin-1-beta (pro-IL-1-beta) in mouse submandibular gland to form IL-1-beta.
  • Belongs to peptidase family S1A.
 2 P36368 P36368