Detail Information for IndEnz0002013271
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