| IED ID | IndEnz0002013703 |
| Enzyme Type ID | protease013703 |
| Protein Name |
Aspartic proteinase 3 EC 3.4.23.41 Proprotein convertase Yapsin-1 Cleaved into: Aspartic proteinase 3 subunit alpha; Aspartic proteinase 3 subunit beta |
| Gene Name | YPS1 YAP3 YLR120C L2961 L9233.9 |
| 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 | MKLKTVRSAVLSSLFASQVLGKIIPAANKRDDDSNSKFVKLPFHKLYGDSLENVGSDKKPEVRLLKRADGYEEIIITNQQSFYSVDLEVGTPPQNVTVLVDTGSSDLWIMGSDNPYCSSNSMGSSRRRVIDKRDDSSSGGSLINDINPFGWLTGTGSAIGPTATGLGGGSGTATQSVPASEATMDCQQYGTFSTSGSSTFRSNNTYFSISYGDGTFASGTFGTDVLDLSDLNVTGLSFAVANETNSTMGVLGIGLPELEVTYSGSTASHSGKAYKYDNFPIVLKNSGAIKSNTYSLYLNDSDAMHGTILFGAVDHSKYTGTLYTIPIVNTLSASGFSSPIQFDVTINGIGISDSGSSNKTLTTTKIPALLDSGTTLTYLPQTVVSMIATELGAQYSSRIGYYVLDCPSDDSMEIVFDFGGFHINAPLSSFILSTGTTCLLGIIPTSDDTGTILGDSFLTNAYVVYDLENLEISMAQARYNTTSENIEIITSSVPSAVKAPGYTNTWSTSASIVTGGNIFTVNSSQTASFSGNLTTSTASATSTSSKRNVGDHIVPSLPLTLISLLFAFI |
| Enzyme Length | 569 |
| Uniprot Accession Number | P32329 |
| Absorption | |
| Active Site | ACT_SITE 101; /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=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 mono- and paired-basic residues. Involved in the shedding of a subset of GPI-anchored plasma membrane proteins from the cell surface, including itself, GAS1 and MSB2. May also play a role in the maturation of GPI-mannoproteins associated with the cell wall. Can process the alpha-mating factor precursor. Required for cell wall integrity. {ECO:0000269|PubMed:16087741, ECO:0000269|PubMed:18573178, ECO:0000269|PubMed:18591427, ECO:0000269|PubMed:9417119}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.0. {ECO:0000269|PubMed:9417119}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (3); Domain (1); Glycosylation (10); Lipidation (1); Mutagenesis (1); Propeptide (2); Sequence conflict (1); Signal peptide (1); Site (2) |
| Keywords | Aspartyl protease;Autocatalytic cleavage;Cell membrane;Cleavage on pair of basic residues;Direct protein sequencing;Disulfide bond;GPI-anchor;Glycoprotein;Hydrolase;Lipoprotein;Membrane;Protease;Reference proteome;Signal;Zymogen |
| Interact With | |
| Induction | INDUCTION: Positively regulated by cell integrity signaling through MPK1 in response to cell wall perturbation. {ECO:0000269|PubMed:16087741}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11737827, ECO:0000269|PubMed:14617149, ECO:0000269|PubMed:7657670, ECO:0000269|PubMed:9417119}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:11737827, ECO:0000269|PubMed:14617149, ECO:0000269|PubMed:7657670, ECO:0000269|PubMed:9417119}. Note=GPI-anchored plasma membrane protein (GPI-PMP), peripherally distributed over the entire cell surface. |
| Modified Residue | |
| Post Translational Modification | PTM: The zymogen is transported to the periplasm, where the propeptide is removed and the enzyme is further subjected to an internal, autocatalytic cleavage to generate an alpha/beta two-subunit endopeptidase. The proteolytic processing at the cell surface is regulated by the environmental pH. {ECO:0000269|PubMed:18573178, ECO:0000269|PubMed:9417119}.; PTM: Extensively N-glycosylated. {ECO:0000269|PubMed:7657670, ECO:0000269|PubMed:9417119}. |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10383953; 10564469; 10700387; 10855718; 10862872; 10900456; 11087688; 12827498; 17042746; 18975972; 2022624; 20333241; 20599573; 20833895; 21632904; 22162039; 22219507; 22388689; 22660740; 23029052; 23135325; 23419716; 25886139; 27965112; 7479877; 7750551; 7819327; 8104828; 8540374; 8612794; 8621069; 8626758; 8895388; 9218793; 9409808; 9427388; 9483804; 9494104; 9756943; 9822624; |
| Motif | |
| Gene Encoded By | |
| Mass | 60,010 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.23.41; |