| IED ID | IndEnz0002018970 |
| Enzyme Type ID | protease018970 |
| Protein Name |
Saccharopepsin EC 3.4.23.25 Aspartate protease PrA Proteinase A Carboxypeptidase Y-deficient protein 4 Proteinase YSCA |
| Gene Name | PEP4 PHO9 PRA1 YPL154C P2585 |
| 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 | MFSLKALLPLALLLVSANQVAAKVHKAKIYKHELSDEMKEVTFEQHLAHLGQKYLTQFEKANPEVVFSREHPFFTEGGHDVPLTNYLNAQYYTDITLGTPPQNFKVILDTGSSNLWVPSNECGSLACFLHSKYDHEASSSYKANGTEFAIQYGTGSLEGYISQDTLSIGDLTIPKQDFAEATSEPGLTFAFGKFDGILGLGYDTISVDKVVPPFYNAIQQDLLDEKRFAFYLGDTSKDTENGGEATFGGIDESKFKGDITWLPVRRKAYWEVKFEGIGLGDEYAELESHGAAIDTGTSLITLPSGLAEMINAEIGAKKGWTGQYTLDCNTRDNLPDLIFNFNGYNFTIGPYDYTLEVSGSCISAITPMDFPEPVGPLAIVGDAFLRKYYSIYDLGNNAVGLAKAI |
| Enzyme Length | 405 |
| Uniprot Accession Number | P07267 |
| Absorption | |
| Active Site | ACT_SITE 109; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094; ACT_SITE 294; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins with broad specificity for peptide bonds. Cleaves -Leu-Leu-|-Val-Tyr- bond in a synthetic substrate. Does not act on esters of Tyr or Arg.; EC=3.4.23.25; |
| DNA Binding | |
| EC Number | 3.4.23.25 |
| Enzyme Function | FUNCTION: Aspartyl protease implicated in the post-translational regulation of S.cerevisiae vacuolar proteinases. Acts on YSCB, on YSCY and on itself. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (26); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (2); Helix (11); Mutagenesis (1); Propeptide (1); Signal peptide (1); Turn (6) |
| Keywords | 3D-structure;Aspartyl protease;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Protease;Reference proteome;Signal;Vacuole;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Vacuole. Note=Lysosome-like vacuoles. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000269|PubMed:8840499 |
| Structure 3D | X-ray crystallography (11) |
| Cross Reference PDB | 1DP5; 1DPJ; 1FMU; 1FMX; 1FQ4; 1FQ5; 1FQ6; 1FQ7; 1FQ8; 1G0V; 2JXR; |
| Mapped Pubmed ID | 10220001; 10554772; 10649450; 10655612; 10735854; 11042188; 11043985; 11061973; 11168403; 11283351; 11294906; 11416128; 11486014; 11516167; 11805826; 12127998; 12529432; 12857862; 13357487; 1368017; 14616069; 14690591; 14871932; 15016820; 15065849; 15286284; 15350980; 1569061; 15887030; 16183335; 16267277; 1628653; 16429126; 16554755; 16860663; 16884526; 16978354; 17049819; 17087512; 17107617; 17132049; 17159212; 17166847; 1735446; 1735447; 17447722; 17651441; 17932463; 1801748; 18681437; 18698411; 18786576; 18818209; 19013276; 19254955; 19363031; 19421331; 19793921; 19817002; 19955083; 2022624; 20345665; 20498363; 20855568; 20926387; 20931186; 21121900; 21151492; 21179020; 21317551; 21593793; 21871892; 21936842; 21936847; 22069150; 22261724; 22536249; 22653261; 2269659; 22722939; 22768199; 22960621; 23169651; 23217712; 23220089; 23275495; 23322149; 23382696; 23529158; 23599894; 23656787; 23668784; 23708375; 23747013; 23747875; 24148098; 24205865; 24240771; 24753258; 24992019; 25042851; 25043177; 25052096; 25070953; 25126732; 25468960; 25691244; 25704703; 25824091; 25902403; 25937302; 25995378; 26086961; 26344037; 26477382; 26515066; 26527740; 26670610; 2674123; 2676511; 26876173; 26904057; 26916166; 26947009; 27048816; 27050457; 27097106; 27170182; 27385339; 27442630; 27693354; 29124367; 29224051; 2992470; 3049073; 30715625; 31332264; 3308453; 6340101; 6397123; 6749836; 6799292; 7002931; 7593182; 7628461; 7865884; 8001551; 8045256; 8068659; 8129953; 8144575; 8262967; 8269947; 8297512; 8349680; 8416961; 8659917; 8789256; 9529893; 9644256; 9683639; |
| Motif | |
| Gene Encoded By | |
| Mass | 44,499 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.23.25; |