Detail Information for IndEnz0002012467
IED ID IndEnz0002012467
Enzyme Type ID protease012467
Protein Name Aspartic proteinase yapsin-6
EC 3.4.23.-
Gene Name YPS6 YIR039C
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 MQLISILSLLSSLMCSLTVLGSSASSYVKFPVQKLADIINICTQDVSTVFKRNEVLNTTVINGIGVYVVKMEIGTPPQTLYLQLDTGSSDMIVNNADIAYCKSMSDGSDYASTDNYELTATFNGLPSTTISSEAYNTLCSYWGTFDASNSSTFENNATFFNNTYGDGTYYAGTYGTDVVSFENITLNDFTFGVSNDTIGNPSGILGISLPIAEFTDGIEYALALNRTPFIYDNFPMELKNQGKINKIAYSLFLNGPDAHFGSILFGAVDKSKYTGQLYTLPMLQAFNTLGSNPGMIITAQSVAILDSESGNKTVSDIQFPVMLDSGTTFSYLPTEIAEAIGKSFDGEYSSDDQGYIFDCSKVNDTLLSVDFGGFNISANISNFVTSAKDRCVLNVKQSESTYMLGDAFLVDAYVVYDLENYEISIAQASFNNQEEDIEVISDTVPGATPAPGYFSTWVYKPGSPIGTGDFINVSWTSYSEFSQYKSLLATAAQSDDASSFSSSGGSSESTTKKQNAGYKYRSSFSFSLLSFISYFLL
Enzyme Length 537
Uniprot Accession Number P40583
Absorption
Active Site ACT_SITE 85; /evidence=ECO:0000255|PROSITE-ProRule:PRU01103; ACT_SITE 324; /evidence=ECO:0000255|PROSITE-ProRule:PRU01103
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 (By similarity). Required for cell wall integrity. {ECO:0000250, 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); Signal peptide (1)
Keywords Aspartyl protease;Cell membrane;Cleavage on pair of basic residues;GPI-anchor;Glycoprotein;Hydrolase;Lipoprotein;Membrane;Protease;Reference proteome;Signal;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:10383953}; Lipid-anchor, GPI-anchor {ECO:0000305|PubMed:10383953}.
Modified Residue
Post Translational Modification PTM: N-glycosylated. {ECO:0000269|PubMed:19756047}.
Signal Peptide SIGNAL 1..24; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10191273; 10688190; 11283351; 17042746; 19536198; 20599573; 21072241; 21918511; 23135325; 27965112;
Motif
Gene Encoded By
Mass 58,214
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda