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:

"
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 22973: Pepsin B

There are 3 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
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.
16 B9A851 G3I107 P03955 P04073 P20142 P81498 Q64411 Q689Z7 Q6HA02 Q9D7R7
(6 more...)
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.
1 A0A172Q3Y6
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