IED ID | IndEnz0002013271 |
Enzyme Type ID | protease013271 |
Protein Name |
Aspartic proteinase yapsin-3 EC 3.4.23.- |
Gene Name | YPS3 YLR121C L2964 L9233.10 |
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 | MKLQLAAVATLAVLTSPAFGRVLPDGKYVKIPFTKKKNGDNGELSKRSNGHEKFVLANEQSFYSVELAIGTPSQNLTVLLDTGSADLWVPGKGNPYCGSVMDCDQYGVFDKTKSSTFKANKSSPFYAAYGDGTYAEGAFGQDKLKYNELDLSGLSFAVANESNSTFGVLGIGLSTLEVTYSGKVAIMDKRSYEYDNFPLFLKHSGAIDATAYSLFLNDESQSSGSILFGAVDHSKYEGQLYTIPLVNLYKSQGYQHPVAFDVTLQGLGLQTDKRNITLTTTKLPALLDSGTTLTYLPSQAVALLAKSLNASYSKTLGYYEYTCPSSDNKTSVAFDFGGFRINAPLSDFTMQTSVGTCVLAIIPQAGNATAILGDSFLRNAYVVYDLDNYEISLAQAKYGTGKENVEVIKSTVPSAIRAPSYNNTWSNYASATSGGNIFTTVRTFNGTSTATTTRSTTTKKTNSTTTAKSTHKSKRALQRAATNSASSIRSTLGLLLVPSLLILSVFFS |
Enzyme Length | 508 |
Uniprot Accession Number | Q12303 |
Absorption | |
Active Site | ACT_SITE 81; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094; ACT_SITE 288; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.23.- |
Enzyme Function | FUNCTION: Cleaves proteins C-terminally to mono- and paired-basic residues. Required for cell wall integrity. {ECO:0000269|PubMed:10191273, ECO:0000269|PubMed:16087741}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (1); Domain (1); Glycosylation (11); Lipidation (1); Propeptide (2); Region (1); Signal peptide (1) |
Keywords | Aspartyl protease;Cell membrane;Cleavage on pair of basic residues;Direct protein sequencing;GPI-anchor;Glycoprotein;Hydrolase;Lipoprotein;Membrane;Protease;Reference proteome;Signal;Zymogen |
Interact With | |
Induction | INDUCTION: Positively regulated in response to cell wall perturbation. {ECO:0000269|PubMed:11016834}. |
Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10191273, ECO:0000269|PubMed:11016834}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:10191273, ECO:0000269|PubMed:11016834}. Note=GPI-anchored plasma membrane protein (GPI-PMP). |
Modified Residue | |
Post Translational Modification | PTM: Can also be processed to start at Phe-54. {ECO:0000269|PubMed:10191273}. |
Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 10688190; 11283351; 14561723; 17042746; 19108609; 19536198; 20599573; 22162039; 23029052; 23135325; 27965112; |
Motif | |
Gene Encoded By | |
Mass | 54,570 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |