| IED ID | IndEnz0002002837 |
| Enzyme Type ID | protease002837 |
| Protein Name |
Aspartic proteinase MKC7 EC 3.4.23.41 Yapsin-2 |
| Gene Name | MKC7 YPS2 YDR144C YD2943.03C YD8358.01C |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Enzyme Sequence | MKLSVLTFVVDALLVCSSIVDAGVTDFPSLPSNEVYVKMNFQKKYGSSFENALDDTKGRTRLMTRDDDYELVELTNQNSFYSVELDIGTPPQKVTVLVDTGSSDLWVTGSDNPYCSTKKKDTTGSSFKQVNKDALASVVESVFTEISYDTTIVTSEATATFDSTASTSQLIDCATYGTFNTSKSSTFNSNNTEFSIAYGDTTFASGTWGHDQLSLNDLNITGLSFAVANETNSTVGVLGIGLPGLESTYSGVSLSSVQKSYTYNNFPMVLKNSGVIKSTAYSLFANDSDSKHGTILFGAVDHGKYAGDLYTIPIINTLQHRGYKDPIQFQVTLQGLGTSKGDKEDNLTTLTTTKIPVLLDSGTTISYMPTELVKMLADQVGATYSSAYGYYIMDCIKEMEEESSIIFDFGGFYLSNWLSDFQLVTDSRSNICILGIAPQSDPTIILGDNFLANTYVVYDLDNMEISMAQANFSDDGEYIEIIESAVPSALKAPGYSSTWSTYESIVSGGNMFSTAANSSISYFASTSHSATSSSSSKGQKTQTSTTALSISKSTSSTSSTGMLSPTSSSSTRKENGGHNLNPPFFARFITAIFHHI |
| Enzyme Length | 596 |
| Uniprot Accession Number | P53379 |
| Absorption | |
| Active Site | ACT_SITE 99; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094; ACT_SITE 360; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolyzes various precursor proteins with Arg or Lys in P1, and commonly Arg or Lys also in P2. The P3 amino acid is usually non-polar, but otherwise additional basic amino acids are favorable in both non-prime and prime positions.; EC=3.4.23.41; |
| DNA Binding | |
| EC Number | 3.4.23.41 |
| Enzyme Function | FUNCTION: Cleaves proteins C-terminally to the most C-terminal basic residue. Can process the alpha-mating factor precursor. Required for cell wall integrity. {ECO:0000269|PubMed:10446224, ECO:0000269|PubMed:16087741, ECO:0000269|PubMed:7479877}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4-7. Optimum pH is substrate-dependent. {ECO:0000269|PubMed:10446224}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Compositional bias (1); Domain (1); Glycosylation (9); Lipidation (1); Propeptide (2); Region (1); Sequence conflict (2); Signal peptide (1) |
| Keywords | Aspartyl protease;Cell membrane;Direct protein sequencing;GPI-anchor;Glycoprotein;Hydrolase;Lipoprotein;Membrane;Protease;Reference proteome;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10446224, ECO:0000269|PubMed:7479877}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:10446224, ECO:0000269|PubMed:7479877}. Note=GPI-anchored plasma membrane protein (GPI-PMP). |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10383953; 11283351; 12827498; 17042746; 18467557; 18591427; 20599573; 20833895; 21936845; 22162039; 23135325; 23237624; 26270963; 27965112; 9092503; 9409808; 9417119; 9494104; 9822624; |
| Motif | |
| Gene Encoded By | |
| Mass | 64,269 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |