UniProtKB - P09232 (PRTB_YEAST)
Protein
Cerevisin
Gene
PRB1
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Functioni
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.2 Publications
Miscellaneous
[beta] is the prion form of PrB. In contrast to other prions, [beta] is not the result of a conformational change of the cellular PrB, but distinguishes itself by autoactivation in trans. Usually, PrB is already involved in its own maturatiuon, but PrA plays a critical role. PrpA mutants lack PrB. However, in growth conditions that favor PRB1 expression, PrB activity persists in PrA mutants due to autocleavage of PrB in trans. This condition is stably transmitted to daughter cells in mitosis. [beta] can be cured by growing in PRB1-repressing conditions. Once a cell has lost PrB activity, it remains stably inactive. Thus, there are 2 alternative states, that are chromosomally identical, but phenotypically distinct. Since PrA is able to activate PrB, normal cells always carry the [beta] prion. Its absence and transmission are only observable in the absence of PrA.1 Publication
Present with 1600 molecules/cell in log phase SD medium.1 Publication
Catalytic activityi
- Hydrolysis of proteins with broad specificity, and of Bz-Arg-OEt > Ac-Tyr-OEt. Does not hydrolyze peptide amides. EC:3.4.21.48
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 325 | Charge relay systemPROSITE-ProRule annotation | 1 | |
Active sitei | 357 | Charge relay systemPROSITE-ProRule annotation | 1 | |
Active sitei | 519 | Charge relay systemPROSITE-ProRule annotation | 1 |
GO - Molecular functioni
- serine-type endopeptidase activity Source: SGD
GO - Biological processi
- cellular response to starvation Source: SGD
- pexophagy Source: SGD
- protein catabolic process in the vacuole Source: SGD
- sporulation resulting in formation of a cellular spore Source: SGD
Keywordsi
Molecular function | Hydrolase, Prion, Protease, Serine protease |
Enzyme and pathway databases
BRENDAi | 3.4.21.48, 984 |
Reactomei | R-SCE-8866427, VLDLR internalisation and degradation R-SCE-8964038, LDL clearance |
Protein family/group databases
MEROPSi | S08.052 |
Names & Taxonomyi
Protein namesi | Recommended name: Cerevisin (EC:3.4.21.48)Alternative name(s): Proteinase YSCB Vacuolar protease B Short name: PrB |
Gene namesi | Name:PRB1 Ordered Locus Names:YEL060C |
Organismi | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Taxonomic identifieri | 559292 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › |
Proteomesi |
|
Organism-specific databases
SGDi | S000000786, PRB1 |
VEuPathDBi | FungiDB:YEL060C |
Subcellular locationi
Vacuole
Extracellular region or secreted
- extracellular space Source: GO_Central
Vacuole
- fungal-type vacuole Source: SGD
- fungal-type vacuole lumen Source: SGD
Keywords - Cellular componenti
Amyloid, VacuolePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 19 | Sequence analysisAdd BLAST | 19 | |
PropeptideiPRO_0000027136 | 20 – 280 | 1 PublicationAdd BLAST | 261 | |
ChainiPRO_0000027137 | 281 – ?574 | CerevisinAdd BLAST | 294 | |
PropeptideiPRO_0000417567 | ?575 – 635 | Add BLAST | 61 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 460 ↔ 491 | Sequence analysis | ||
Glycosylationi | 594 | N-linked (GlcNAc...) asparagineCurated | 1 |
Post-translational modificationi
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.
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.
Keywords - PTMi
Disulfide bond, Glycoprotein, ZymogenProteomic databases
MaxQBi | P09232 |
PaxDbi | P09232 |
PRIDEi | P09232 |
TopDownProteomicsi | P09232 |
2D gel databases
UCD-2DPAGEi | P09232 |
PTM databases
iPTMneti | P09232 |
Expressioni
Inductioni
Repressed by glucose.1 Publication
Interactioni
Protein-protein interaction databases
BioGRIDi | 36669, 133 interactors |
DIPi | DIP-2544N |
IntActi | P09232, 23 interactors |
MINTi | P09232 |
STRINGi | 4932.YEL060C |
Miscellaneous databases
RNActi | P09232, protein |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 182 – 278 | Inhibitor I9Sequence analysisAdd BLAST | 97 | |
Domaini | 289 – 614 | Peptidase S8PROSITE-ProRule annotationAdd BLAST | 326 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 63 – 154 | Lys-richAdd BLAST | 92 |
Sequence similaritiesi
Belongs to the peptidase S8 family.Curated
Keywords - Domaini
SignalPhylogenomic databases
eggNOGi | KOG1153, Eukaryota |
GeneTreei | ENSGT00940000176425 |
HOGENOMi | CLU_011263_3_0_1 |
InParanoidi | P09232 |
OMAi | WIGSKHA |
Family and domain databases
CDDi | cd04077, Peptidases_S8_PCSK9_ProteinaseK_like, 1 hit |
Gene3Di | 3.30.70.80, 1 hit 3.40.50.200, 1 hit |
InterProi | View protein in InterPro IPR034193, PCSK9_ProteinaseK-like IPR000209, Peptidase_S8/S53_dom IPR036852, Peptidase_S8/S53_dom_sf IPR023827, Peptidase_S8_Asp-AS IPR022398, Peptidase_S8_His-AS IPR023828, Peptidase_S8_Ser-AS IPR015500, Peptidase_S8_subtilisin-rel IPR010259, S8pro/Inhibitor_I9 IPR037045, S8pro/Inhibitor_I9_sf |
Pfami | View protein in Pfam PF05922, Inhibitor_I9, 1 hit PF00082, Peptidase_S8, 1 hit |
PRINTSi | PR00723, SUBTILISIN |
SUPFAMi | SSF52743, SSF52743, 1 hit |
PROSITEi | View protein in PROSITE PS51892, SUBTILASE, 1 hit PS00136, SUBTILASE_ASP, 1 hit PS00137, SUBTILASE_HIS, 1 hit PS00138, SUBTILASE_SER, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P09232-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MKLENTLFTL GALGSISAAL VIPNLENAAD HHELINKEDH HERPRKVEFT
60 70 80 90 100
KDDDEEPSDS EDKEHGKFHK KGRKGQDKES PEFNGKRASG SHGSAHEGGK
110 120 130 140 150
GMKPKHESSN DDDNDDKKKK PHHKGGCHEN KVEEKKMKGK KVKGKKHHEK
160 170 180 190 200
TLEKGRHHNR LAPLVSTAQF NPDAISKIIP NRYIIVFKRG APQEEIDFHK
210 220 230 240 250
ENVQQAQLQS VENLSAEDAF FISTKDTSLS TSEAGGIQDS FNIDNLFSGY
260 270 280 290 300
IGYFTQEIVD LIRQNPLVDF VERDSIVEAT EFDTQNSAPW GLARISHRER
310 320 330 340 350
LNLGSFNKYL YDDDAGRGVT SYVIDTGVNI NHKDFEKRAI WGKTIPLNDE
360 370 380 390 400
DLDGNGHGTH CAGTIASKHY GVAKNANVVA VKVLRSNGSG TMSDVVKGVE
410 420 430 440 450
YAAKAHQKEA QEKKKGFKGS TANMSLGGGK SPALDLAVNA AVEVGIHFAV
460 470 480 490 500
AAGNENQDAC NTSPASADKA ITVGASTLSD DRAYFSNWGK CVDVFAPGLN
510 520 530 540 550
ILSTYIGSDD ATATLSGTSM ASPHVAGLLT YFLSLQPGSD SEFFELGQDS
560 570 580 590 600
LTPQQLKKKL IHYSTKDILF DIPEDTPNVL IYNGGGQDLS AFWNDTKKSH
610 620 630
SSGFKQELNM DEFIGSKTDL IFDQVRDILD KLNII
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 622 | F → K in CAA77886 (Ref. 4) Curated | 1 | |
Sequence conflicti | 622 | F → K in AAA34495 (Ref. 4) Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M18097 Genomic DNA Translation: AAA34901.1 U18795 Genomic DNA Translation: AAB65027.1 Z11859 Genomic DNA Translation: CAA77886.1 M90522 Genomic DNA Translation: AAA34495.1 BK006939 Genomic DNA Translation: DAA07594.1 |
PIRi | A29358 |
RefSeqi | NP_010854.1, NM_001178875.1 |
Genome annotation databases
EnsemblFungii | YEL060C_mRNA; YEL060C; YEL060C |
GeneIDi | 856649 |
KEGGi | sce:YEL060C |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M18097 Genomic DNA Translation: AAA34901.1 U18795 Genomic DNA Translation: AAB65027.1 Z11859 Genomic DNA Translation: CAA77886.1 M90522 Genomic DNA Translation: AAA34495.1 BK006939 Genomic DNA Translation: DAA07594.1 |
PIRi | A29358 |
RefSeqi | NP_010854.1, NM_001178875.1 |
3D structure databases
SMRi | P09232 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 36669, 133 interactors |
DIPi | DIP-2544N |
IntActi | P09232, 23 interactors |
MINTi | P09232 |
STRINGi | 4932.YEL060C |
Protein family/group databases
MEROPSi | S08.052 |
PTM databases
iPTMneti | P09232 |
2D gel databases
UCD-2DPAGEi | P09232 |
Proteomic databases
MaxQBi | P09232 |
PaxDbi | P09232 |
PRIDEi | P09232 |
TopDownProteomicsi | P09232 |
Genome annotation databases
EnsemblFungii | YEL060C_mRNA; YEL060C; YEL060C |
GeneIDi | 856649 |
KEGGi | sce:YEL060C |
Organism-specific databases
SGDi | S000000786, PRB1 |
VEuPathDBi | FungiDB:YEL060C |
Phylogenomic databases
eggNOGi | KOG1153, Eukaryota |
GeneTreei | ENSGT00940000176425 |
HOGENOMi | CLU_011263_3_0_1 |
InParanoidi | P09232 |
OMAi | WIGSKHA |
Enzyme and pathway databases
BRENDAi | 3.4.21.48, 984 |
Reactomei | R-SCE-8866427, VLDLR internalisation and degradation R-SCE-8964038, LDL clearance |
Miscellaneous databases
PROi | PR:P09232 |
RNActi | P09232, protein |
Family and domain databases
CDDi | cd04077, Peptidases_S8_PCSK9_ProteinaseK_like, 1 hit |
Gene3Di | 3.30.70.80, 1 hit 3.40.50.200, 1 hit |
InterProi | View protein in InterPro IPR034193, PCSK9_ProteinaseK-like IPR000209, Peptidase_S8/S53_dom IPR036852, Peptidase_S8/S53_dom_sf IPR023827, Peptidase_S8_Asp-AS IPR022398, Peptidase_S8_His-AS IPR023828, Peptidase_S8_Ser-AS IPR015500, Peptidase_S8_subtilisin-rel IPR010259, S8pro/Inhibitor_I9 IPR037045, S8pro/Inhibitor_I9_sf |
Pfami | View protein in Pfam PF05922, Inhibitor_I9, 1 hit PF00082, Peptidase_S8, 1 hit |
PRINTSi | PR00723, SUBTILISIN |
SUPFAMi | SSF52743, SSF52743, 1 hit |
PROSITEi | View protein in PROSITE PS51892, SUBTILASE, 1 hit PS00136, SUBTILASE_ASP, 1 hit PS00137, SUBTILASE_HIS, 1 hit PS00138, SUBTILASE_SER, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | PRTB_YEAST | |
Accessioni | P09232Primary (citable) accession number: P09232 Secondary accession number(s): D3DLJ0 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 1, 1989 |
Last sequence update: | July 1, 1989 | |
Last modified: | February 10, 2021 | |
This is version 200 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencing, Reference proteomeDocuments
- Yeast
Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD - Yeast chromosome V
Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names - Peptidase families
Classification of peptidase families and list of entries - SIMILARITY comments
Index of protein domains and families