| IED ID | IndEnz0002004741 |
| Enzyme Type ID | protease004741 |
| Protein Name |
Candidapepsin-3 EC 3.4.23.24 ACP 3 Aspartate protease 3 Secreted aspartic protease 3 |
| Gene Name | SAP3 |
| Organism | Candida albicans (Yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Debaryomycetaceae Candida/Lodderomyces clade Candida Candida albicans (Yeast) |
| Enzyme Sequence | MFLKNIFIALAIALLADATPTTFNNSPGFVALNFDVIKTHKNVTGPQGEINTNVNVKRQTVPVKLINEQVSYASDITVGSNKQKLTVVIDTGSSDLWVPDSQVSCQAGQGQDPNFCKNEGTYSPSSSSSSQNLNSPFSIEYGDGTTSQGTWYKDTIGFGGISITKQQFADVTSTSVDQGILGIGYKTHEAEGNYDNVPVTLKNQGIISKNAYSLYLNSRQATSGQIIFGGVDNAKYSGTLIALPVTSDNELRIHLNTVKVAGQSINADVDVLLDSGTTITYLQQGVADQVISAFNGQETYDANGNLFYLVDCNLSGSVDFAFDKNAKISVPASEFTAPLYTEDGQVYDQCQLLFGTSDYNILGDNFLRSAYIVYDLDDNEISLAQVKYTTASNIAALT |
| Enzyme Length | 398 |
| Uniprot Accession Number | P0CY28 |
| Absorption | |
| Active Site | ACT_SITE 90; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094; ACT_SITE 274; /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); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (2); Propeptide (1); Region (4); Signal peptide (1) |
| Keywords | Aspartyl protease;Cleavage on pair of basic residues;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:0000250}. |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 42,806 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |