| IED ID | IndEnz0002005185 |
| Enzyme Type ID | protease005185 |
| Protein Name |
Candidapepsin-10 EC 3.4.23.24 ACP 10 Aspartate protease 10 Secreted aspartic protease 10 |
| Gene Name | SAP10 YPS3 CAALFM_C404470WA CaO19.11320 CaO19.3839 |
| Organism | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Debaryomycetaceae Candida/Lodderomyces clade Candida Candida albicans (Yeast) Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
| Enzyme Sequence | MDLVIMNFVFLLYLTSVVKCSIKLDFNKVSTPSKYTKRDALPMPLINDKILYTTELEIGSNKDKVSVSIDTGSYDLWVMSNDAVCYKVSEFQTEGAPQLPDIFNDIDQDYSCTFNGTYNSKSSKTFKNTSEDFSIGYVDGSAAQGVWGYDSVQFGQYGVTGLKIGIANRSSVSDGILGIGIANGYDNFPVLLQKQGLINKIAYSVYLNSSNSTTGTILFGAIDHAKYKGALSTVPVDSKSQLSVNVTNLKTKNGNVASGGHSILLDTGSTFSIFPDEWIDALGHSLNATYDEDESVYEIECDGYDEHFFGFSIGDSDFSVPIQDLKTEKDGQCYLAIMSNSVIGGGGILFGDDILRQIYLVYDLQDMTISVAPVVYTEDEDIEEILNPNEDQNEVPTSTSFTQSASSSGSQPSSTISGENMDKNTTSSSSGNCQTRSWIAILSALFLVYIHII |
| Enzyme Length | 453 |
| Uniprot Accession Number | Q5A651 |
| Absorption | |
| Active Site | ACT_SITE 70; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094; ACT_SITE 266; /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; Evidence={ECO:0000269|PubMed:21646240}; |
| DNA Binding | |
| EC Number | 3.4.23.24 |
| Enzyme Function | FUNCTION: Secreted aspartic peptidases (SAPs) are a group of ten acidic hydrolases considered as key virulence factors. These enzymes supply the fungus with nutrient amino acids as well as are able to degrade the selected host's proteins involved in the immune defense. Required for cell surface integrity and cell separation during budding. {ECO:0000269|PubMed:16269404}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0. {ECO:0000269|PubMed:21646240}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Compositional bias (1); Disulfide bond (2); Domain (1); Glycosylation (8); Lipidation (1); Propeptide (1); Region (4); Signal peptide (1) |
| Keywords | Aspartyl protease;Cell membrane;Cleavage on pair of basic residues;Disulfide bond;GPI-anchor;Glycoprotein;Hydrolase;Lipoprotein;Membrane;Protease;Reference proteome;Repeat;Secreted;Signal;Virulence;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16269404}. Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | PTM: O-glycosylated. {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 21097664; |
| Motif | |
| Gene Encoded By | |
| Mass | 49,333 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |