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CATH Superfamily 2.40.70.10

Acid 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:

"
Acid 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 4: Pepsin A

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
Pepsin A. [EC: 3.4.23.1]
Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1' positions. Cleaves 1-Phe-|-Val-2, 4-Gln-|-His-5, 13-Glu-|-Ala-14, 14-Ala-|-Leu-15, 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17, 23-Gly-|-Phe-24, 24-Phe-|-Phe-25 and 25-Phe-|-Tyr-26 bonds in the B chain of insulin.
  • The predominant endopeptidase in the gastric juice of vertebrates, formed from pepsinogen A by limited proteolysis.
  • Belongs to peptidase family A1.
  • Formerly EC 3.4.4.1.
 20 A0A1S5UZ02 A0A1S5UZ02 A0A480E6X5 A0A480E6X5 P00791 P00791 P00792 P00793 P03954 P0DJD7
(10 more...)
Cathepsin E. [EC: 3.4.23.34]
Similar to cathepsin D, but slightly broader specificity.
  • Found in stomach, spleen, erythrocyte membrane; not lysosomal.
  • Pro-cathepsin E is an 86 kDa disulfide-linked dimer; activation or reduction produces monomers.
  • Belongs to peptidase family A1.
 17 A0A1L8H7D5 A0A1L8H7D5 B7ZQ61 B7ZQ61 H2R344 H2R344 P14091 P14091 P16228 P25796
(7 more...)
Gastricsin. [EC: 3.4.23.3]
More restricted specificity than pepsin A, but shows preferential cleavage at Tyr-|-Xaa bonds. High activity on hemoglobin.
  • Formed from progastricsin, apparently in the gastric juice of most vertebrates.
  • In addition to the fundus, progastricsin is also secreted in antrum and proximal duodenum.
  • Seminal plasma contains a zymogen that is immunologically identical with progastricsin.
  • Belongs to peptidase family A1.
  • Formerly EC 3.4.4.22.
 7 P03955 P04073 P20142 Q689Z7 Q9D7R7 Q9GMY3 Q9N2D3
Chymosin. [EC: 3.4.23.4]
Broad specificity similar to that of pepsin A. Clots milk by cleavage of a single 104-Ser-Phe-|-Met-Ala-107 bond in kappa-chain of casein.
  • Neonatal gastric enzyme with high milk clotting and weak general proteolytic activity, formed from prochymosin.
  • Found among mammals with postnatal uptake of immunoglobins.
  • Belongs to peptidase family A1.
  • Formerly EC 3.4.4.3.
 6 C0LTP1 C0LTP1 P00794 P00794 P18276 Q9GK11
Pepsin B. [EC: 3.4.23.2]
Degradation of gelatin, little activity on hemoglobin. Specificity on B chain of insulin more restricted than that of pepsin A. Does not cleave 1-Phe-|-Val-2, 4-Gln-|-His-5 or 23-Gly-|-Phe-24.
  • Belongs to peptidase family A1.
  • Formerly EC 3.4.4.2.
 1 Q8SQ41