Function and Biology Details
Reaction catalysed:
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.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Secreted aspartic protease 2 (preferred)
PDBe Complex ID:
PDB-CPX-143548 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Secreted aspartic protease 2
Molecule details ›
Chain: A
Length: 342 amino acids
Theoretical weight: 36.32 KDa
Source organism: Candida albicans
UniProt:
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases
Length: 342 amino acids
Theoretical weight: 36.32 KDa
Source organism: Candida albicans
UniProt:
- Canonical:
P0CS83 (Residues: 57-398; Coverage: 90%)
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases
