| IED ID | IndEnz0002005912 |
| Enzyme Type ID | protease005912 |
| Protein Name |
Candidapepsin-9 EC 3.4.23.24 ACP 9 Aspartate protease 9 Secreted aspartic protease 9 |
| Gene Name | SAP9 YPS1 CAALFM_C303870CA CaO19.14190 CaO19.6928 |
| 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 | MRLNSVALLSLVATALAAKAPFKIDFEVRRGESKDDLSPEDDSNPRFVKRDGSLDMTLTNKQTFYMATLKIGSNEDENRVLVDTGSSDLWVMSHDLKCVSAPNSKRNERSFGHGTGVKLNERELMQKRKNLYQPSRTIETDEEKEASEKIHNKLFGFGSIYSTVYITEGPGAYSTFSPFVGTEGGSGGSGGSNTCTSYGSFNTENSDTFKKNNTNDFEIQYADDTSAIGIWGYDDVTISNVTVKDLSFAIANETSSDVGVLGIGLPGLEVTTQYGYTYQNLPLKLKADGIIAKSLYSLYLNTADAKAGSILFGAIDHAKYQGDLVTVKMMRTYSQISYPVRIQVPVSKIDVESSSGSTTNILSSTTGVVLDTGSTLSYVFSDTLQSLGKALNGQYSNSVGAYVVNCNLADSSRTVDIEFGGNKTIKVPISDLVLQASKSTCILGVMQQSSSSSYMLFGDNILRSAYIVYDLDDYEVSLAQVSYTNKESIEVIGASGITNSSGSGTTSSSGTSTSTSTRHSAGSIISKPVYGLLLSLLISCYVLV |
| Enzyme Length | 544 |
| Uniprot Accession Number | Q59SU1 |
| Absorption | |
| Active Site | ACT_SITE 83; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094; ACT_SITE 371; /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. Involved in triggering host polymorphonuclear neutrophils chemotaxis toward germ tubes. Moreover, acts toward human hemoglobin though limited proteolysis to generate a variety of antimicrobial hemocidins, enabling to compete with the other microorganisms of the same physiological niche using the microbicidal peptides generated from the host protein. Required for cell surface integrity and cell separation during budding. {ECO:0000269|PubMed:15820985, ECO:0000269|PubMed:16269404, ECO:0000269|PubMed:19805528, ECO:0000269|PubMed:23927842}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5. {ECO:0000269|PubMed:21646240}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Compositional bias (1); Disulfide bond (1); Domain (1); Glycosylation (5); Lipidation (1); Propeptide (1); Region (2); Signal peptide (1); Transmembrane (1) |
| Keywords | Aspartyl protease;Cell membrane;Cell wall;Cleavage on pair of basic residues;Disulfide bond;GPI-anchor;Glycoprotein;Hydrolase;Lipoprotein;Membrane;Protease;Reference proteome;Repeat;Secreted;Signal;Transmembrane;Transmembrane helix;Virulence;Zymogen |
| Interact With | |
| Induction | INDUCTION: Induced by fluconazole. Expression is regulated by growth phase, temperature, and white-opaque switch. {ECO:0000269|PubMed:15820985, ECO:0000269|PubMed:21622905, ECO:0000269|PubMed:9802014}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}. Secreted, cell wall {ECO:0000269|PubMed:16269404, ECO:0000269|PubMed:21622905}. |
| Modified Residue | |
| Post Translational Modification | PTM: O-glycosylated. {ECO:0000250}.; PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer. |
| Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 58,483 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.23.24; |