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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_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 22912: Cathepsin D (Lysosomal aspartyl protease)

There are 10 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
Cathepsin D. [EC: 3.4.23.5]
Specificity similar to, but narrower than, that of pepsin A. Does not cleave the 4-Gln-|-His-5 bond in B chain of insulin.
  • Occurs intracellularly, in lysosomes.
  • Belongs to peptidase family A1.
  • Formerly EC 3.4.4.23.
 52 A0A074T3W0 A0A084G9U0 A0A086K9K0 A0A086KM05 A0A086LAA3 A0A086LZI4 A0A086Q2X1 A0A086QG87 A0A0D2MF35 A0A139XZ46
(42 more...)
Phytepsin. [EC: 3.4.23.40]
Prefers hydrophobic residues Phe, Val, Ile, Leu, and Ala at P1 and P1', but also cleaves -Phe-|-Asp- and -Asp-|-Asp- bonds in 2S albumin from plant seeds.
  • Known particularly fron barley grain, but present in other plants also.
  • Belongs to peptidase family A1.
 34 A0A084G9U0 A0A0B2P2L1 A0A0B2P5X3 A0A0B2PY44 A0A0B2QD39 A0A0B2QDD4 A0A0B2QX92 A0A0B2RKZ4 A0A0B2RVB1 A0A0B2S2B8
(24 more...)
Saccharopepsin. [EC: 3.4.23.25]
Hydrolysis of proteins with broad specificity for peptide bonds. Cleaves -Leu-Leu-|-Val-Tyr- bond in a synthetic substrate. Does not act on esters of Tyr or Arg.
  • Located in the vacuole.
  • Belongs to peptidase family A1.
  • Formerly EC 3.4.4.17, EC 3.4.23.6 and EC 3.4.23.8.
 30 A0A084G9U0 A0A0B7FUH8 A0A0J5PY94 A0A0J6IM61 A0A0J6YGT1 A0A0J8R1L0 A0A0J8UCV1 A0A0L8VFV1 A6ZW99 B0XXK9
(20 more...)
Renin. [EC: 3.4.23.15]
Cleavage of Leu-|-Xaa bond in angiotensinogen to generate angiotensin I.
  • Belongs to peptidase family A1.
  • Formerly EC 3.4.4.15 and EC 3.4.99.19.
 11 P00796 P00797 P06281 P08424 P52115 P60016 Q6DLS0 Q6DLW5 Q6DYE7 Q7M3D2
(1 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.
 9 A0A084G9U0 P81498 Q64411 Q689Z7 Q6HA02 Q9DDV5 Q9DE45 Q9GMY3 Q9GMY4
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.
 8 A0A0F4YSP8 G3Y3K2 Q00070 Q6HA03 Q6HA04 Q6HA05 Q9PUR8 Q9PUR9
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
Sterol 3-beta-glucosyltransferase. [EC: 2.4.1.173]
UDP-glucose + a sterol = UDP + a sterol 3-beta-D-glucoside.
  • Not identical with EC 2.4.1.192 or EC 2.4.1.193.
 1 A0A139IVU9
Candidapepsin. [EC: 3.4.23.24]
Preferential cleavage at the carboxyl of hydrophobic amino acids, but fails to cleave 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17 and 24-Phe-|-Phe-25 of insulin B chain. Activates trypsinogen, and degrades keratin.
  • This endopeptidase from the imperfect yeast Candida albicans is inhibited by pepstatin, but not by methyl 2-diazoacetamido-hexanoate or 1,2-epoxy-3-(p-nitrophenoxy)propane.
  • Belongs to peptidase family A1.
  • Formerly EC 3.4.4.17 and EC 3.4.23.6.
 1 A3LYI5
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.
 1 U6A6W7