| IED ID | IndEnz0002005987 |
| Enzyme Type ID | protease005987 |
| Protein Name |
Candidapepsin-7 EC 3.4.23.24 ACP 7 Aspartate protease 7 Secreted aspartic protease 7 |
| Gene Name | SAP7 CAALFM_C104870WA CaO19.756 CaO19.8376 |
| 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 | MQRVLELLLLSSTALAVIGDGFIALPVHKLQAGEGSAHFPNRLPIFDVVNGVAKSVEDDVNQIIQPIFGNGIFSGGSIQGTHSGNGHSVKYEVSLPSSSSQKGSNGPSSTDNKDTDPSKTGFSLDDLMNSIPTDFWNLIGLNKAPTSSDNGSKDADFTPSAVSQVEQPTSKSVESTAPGPASSASSSSSSEAASSSQPSEDSQPSSSANKKTGAFFLSLDNTQTLYTATLKVGSPAQEVQVMIDTGSSDLWFISSGNSQCKVNGGSIDCDKYGVFDKSKSSTWHDNKTDYSISYYDGDKASGTMGQDNITFADGFSIENANFAVIDNTTSSIGVFGVGYPELEAVKSKYTNLPFAMKEQNLIAKVAYSLYLDSRDAVQGYILFGGIDHAKYTGDLKAFDIVQSNDKYVYSQIPLTSVASSLNNYTNAYGLPAGSNHPKVGAVIYNGTDSFNGGVDLKDTPTLLDTGTTYSYLSKDQVESIVGLYGNVTYNDAGKAYEVPCWVGNPGNYLEFNFKNEQYIKVPTSEFVISVGTYASGAELCVFGILPGTHSILGDNFMRSVYAVFDLEDHVISIAQAAYNDNHAVVPIE |
| Enzyme Length | 588 |
| Uniprot Accession Number | Q59VH7 |
| Absorption | |
| Active Site | ACT_SITE 244; /evidence="ECO:0000255|PROSITE-ProRule:PRU10094, ECO:0000269|PubMed:22384266"; ACT_SITE 464; /evidence="ECO:0000255|PROSITE-ProRule:PRU10094, ECO:0000269|PubMed:22384266" |
| Activity Regulation | ACTIVITY REGULATION: Contrary to other SAPs, SAP7 is insensitive to pepstatin A inhibition, which is due restriction of the accessibility of pepstatin A to the active site by Met-242 and Thr-467. |
| 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, ECO:0000269|PubMed:22384266}; |
| 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. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5. {ECO:0000269|PubMed:21646240}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Domain (1); Glycosylation (7); Mutagenesis (4); Propeptide (1); Region (5); Signal peptide (1) |
| Keywords | Aspartyl protease;Cleavage on pair of basic residues;Glycoprotein;Hydrolase;Protease;Reference proteome;Secreted;Signal;Virulence;Zymogen |
| Interact With | |
| Induction | INDUCTION: Expression is regulated by SSN6 and induced during host infection. {ECO:0000269|PubMed:15814841, ECO:0000269|PubMed:16177393}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. {ECO:0000269|PubMed:22384266}.; PTM: O-glycosylated. {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..16; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 62,526 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.23.24; |