| IED ID | IndEnz0002008678 |
| Enzyme Type ID | protease008678 |
| Protein Name |
Cerevisin EC 3.4.21.48 Proteinase YSCB Vacuolar protease B PrB |
| Gene Name | PRB1 YEL060C |
| 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 | MKLENTLFTLGALGSISAALVIPNLENAADHHELINKEDHHERPRKVEFTKDDDEEPSDSEDKEHGKFHKKGRKGQDKESPEFNGKRASGSHGSAHEGGKGMKPKHESSNDDDNDDKKKKPHHKGGCHENKVEEKKMKGKKVKGKKHHEKTLEKGRHHNRLAPLVSTAQFNPDAISKIIPNRYIIVFKRGAPQEEIDFHKENVQQAQLQSVENLSAEDAFFISTKDTSLSTSEAGGIQDSFNIDNLFSGYIGYFTQEIVDLIRQNPLVDFVERDSIVEATEFDTQNSAPWGLARISHRERLNLGSFNKYLYDDDAGRGVTSYVIDTGVNINHKDFEKRAIWGKTIPLNDEDLDGNGHGTHCAGTIASKHYGVAKNANVVAVKVLRSNGSGTMSDVVKGVEYAAKAHQKEAQEKKKGFKGSTANMSLGGGKSPALDLAVNAAVEVGIHFAVAAGNENQDACNTSPASADKAITVGASTLSDDRAYFSNWGKCVDVFAPGLNILSTYIGSDDATATLSGTSMASPHVAGLLTYFLSLQPGSDSEFFELGQDSLTPQQLKKKLIHYSTKDILFDIPEDTPNVLIYNGGGQDLSAFWNDTKKSHSSGFKQELNMDEFIGSKTDLIFDQVRDILDKLNII |
| Enzyme Length | 635 |
| Uniprot Accession Number | P09232 |
| Absorption | |
| Active Site | ACT_SITE 325; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 357; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 519; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins with broad specificity, and of Bz-Arg-OEt > Ac-Tyr-OEt. Does not hydrolyze peptide amides.; EC=3.4.21.48; |
| DNA Binding | |
| EC Number | 3.4.21.48 |
| Enzyme Function | FUNCTION: Vacuolar proteinase B involved in protein degradation in the vacuole. Among other substrates, acts on carboxypeptidase Y (cpY/PRC1) to activate it by processing its Pro-peptide. Required for meiosis and spore formation, and for optimal survival in stationary phase. {ECO:0000269|PubMed:6764902, ECO:0000269|PubMed:7021321}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Compositional bias (4); Disulfide bond (1); Domain (2); Glycosylation (1); Propeptide (2); Region (1); Sequence conflict (2); Signal peptide (1) |
| Keywords | Amyloid;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Prion;Protease;Reference proteome;Serine protease;Signal;Vacuole;Zymogen |
| Interact With | |
| Induction | INDUCTION: Repressed by glucose. {ECO:0000269|PubMed:2407604}. |
| Subcellular Location | SUBCELLULAR LOCATION: Vacuole. |
| Modified Residue | |
| Post Translational Modification | PTM: Activated by N- and C-terminal proteolytic cleavage. Protease B (PrB/PRB1) processing requires at least 4 cleavages. First, the signal peptide is removed from the 76 kDa preproprotease B by signal peptidase in the ER. Then, PrB removes its own Pro-region (in trans) at the N-terminus, producing a 39 kDa form before exiting the ER. In the Golgi complex, the C-terminal Post-region of the 40 kDa proprotease B undergoes protease A (PrA/PEP4)-mediated processing to a 37 kDa intermediate, which in turn is quickly processed again by PrB in trans to yield the 31 kDa mature PrB.; PTM: Glycosylated. Preproprotease B is a 76 kDa unglycosylated precursor that enters the endoplasmic reticulum (ER), where it receives one Asn-linked and an undetermined number of non-Asn-linked carbohydrate side chains. In the Golgi complex, the 39 kDa form becomes 40 kDa, due to elaboration of the Asn-linked side chain. The ultimate processing step removes a peptide containing the Asn-linked chain. Mature PrB has only non-Asn-linked carbohydrates. |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10554772; 10688190; 10735854; 10900456; 11099404; 11486014; 11805837; 12455710; 13357487; 1400575; 14660704; 14712063; 1499562; 15286284; 15350980; 1569061; 1626428; 16554755; 16860663; 17107617; 1735446; 1735447; 17632572; 17651441; 18786576; 19001347; 19363031; 19421331; 19536198; 19882662; 2015274; 2015812; 2022624; 20498363; 20726897; 20926387; 21179020; 21339834; 21936842; 2215422; 22156731; 22261724; 22660740; 22727375; 2284; 23071575; 23169651; 23217712; 23275495; 23379365; 23660403; 23747013; 24148098; 24587380; 25052096; 25468960; 25631286; 25902403; 26161950; 26344037; 26362128; 26407534; 26713322; 2674123; 26915272; 27481532; 27693354; 319838; 3549451; 377296; 385314; 6452; 6749836; 7593182; 7765580; 8119286; 8129953; 8262967; 8416961; 8789256; 9045801; 9287023; 9529893; 9649520; |
| Motif | |
| Gene Encoded By | |
| Mass | 69,621 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |