IED ID | IndEnz0002018959 |
Enzyme Type ID | protease018959 |
Protein Name |
Candidapepsin-1 EC 3.4.23.24 ACP 1 Aspartate protease 1 |
Gene Name | SAPP1 ACPR |
Organism | Candida parapsilosis (Yeast) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Debaryomycetaceae Candida/Lodderomyces clade Candida Candida parapsilosis (Yeast) |
Enzyme Sequence | MVAIVTLTRQVLLTIALALFAQGAAIPEEAAKRDDNPGFVALDFDVLRKPLNLTEALLREKRDSISLSLINEGPSYASKVSVGSNKQQQTVIIDTGSSDFWVVDSNAQCGKGVDCKSSGTFTPSSSSSYKNLGAAFTIRYGDGSTSQGTWGKDTVTINGVSITGQQIADVTQTSVDQGILGIGYTSNEAVYDTSGRQTTPNYDNVPVTLKKQGKIRTNAYSLYLNSPSAETGTIIFGGVDNAKYSGKLVAEQVTSSQPLTISLASVNLKGSSFSFGDGALLDSGTTLTYFPSDFAAQLADKAGARLVQVARDQYLYFIDCNTDTSGTTVFNFGNGAKITVPNTEYVYQNGDGTCLWGIQPSDDTILGDNFLRHAYYLLYNLDANTISIAQVKYTTDSSISAV |
Enzyme Length | 402 |
Uniprot Accession Number | P32951 |
Absorption | |
Active Site | ACT_SITE 94; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094; ACT_SITE 282; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=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.; EC=3.4.23.24; |
DNA Binding | |
EC Number | 3.4.23.24 |
Enzyme Function | |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Beta strand (27); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (1); Helix (6); Propeptide (1); Signal peptide (1); Turn (3) |
Keywords | 3D-structure;Aspartyl protease;Cleavage on pair of basic residues;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Protease;Secreted;Signal;Zymogen |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
Modified Residue | |
Post Translational Modification | PTM: O-glycosylated. {ECO:0000305}. |
Signal Peptide | SIGNAL 1..25; /note="Or 18, or 21"; /evidence="ECO:0000255" |
Structure 3D | X-ray crystallography (2) |
Cross Reference PDB | 3FV3; 3TNE; |
Mapped Pubmed ID | 19401235; 22146051; |
Motif | |
Gene Encoded By | |
Mass | 42,833 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.4.23.24; |