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Protein

Cerevisin

Gene

PRB1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei325Charge relay systemBy similarity1
Active sitei357Charge relay systemBy similarity1
Active sitei519Charge relay systemBy similarity1

GO - Molecular functioni

  • serine-type endopeptidase activity Source: SGD

GO - Biological processi

  • cellular response to starvation Source: SGD
  • protein catabolic process in the vacuole Source: SGD
  • sporulation resulting in formation of a cellular spore Source: SGD

Keywordsi

Molecular functionHydrolase, Prion, Protease, Serine protease

Enzyme and pathway databases

BioCyciYEAST:YEL060C-MONOMER
BRENDAi3.4.21.48 984
ReactomeiR-SCE-8866427 VLDLR internalisation and degradation
R-SCE-8964038 LDL clearance

Protein family/group databases

MEROPSiS08.052

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
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome V

Organism-specific databases

EuPathDBiFungiDB:YEL060C
SGDiS000000786 PRB1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Amyloid, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
PropeptideiPRO_000002713620 – 2801 PublicationAdd BLAST261
ChainiPRO_0000027137281 – ?574CerevisinAdd BLAST294
PropeptideiPRO_0000417567?575 – 635Add BLAST61

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi460 ↔ 491Sequence analysis
Glycosylationi594N-linked (GlcNAc...) asparagineCurated1

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, Zymogen

Proteomic databases

MaxQBiP09232
PaxDbiP09232
PRIDEiP09232
TopDownProteomicsiP09232

2D gel databases

UCD-2DPAGEiP09232

PTM databases

iPTMnetiP09232

Miscellaneous databases

PMAP-CutDBiP09232

Expressioni

Inductioni

Repressed by glucose.1 Publication

Interactioni

Protein-protein interaction databases

BioGridi36669, 127 interactors
DIPiDIP-2544N
IntActiP09232, 23 interactors
MINTiP09232
STRINGi4932.YEL060C

Structurei

3D structure databases

ProteinModelPortaliP09232
SMRiP09232
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini322 – 568Peptidase S8Add BLAST247

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi63 – 154Lys-richAdd BLAST92

Sequence similaritiesi

Belongs to the peptidase S8 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

GeneTreeiENSGT00490000043472
HOGENOMiHOG000199176
InParanoidiP09232
KOiK01336
OMAiTKHKGSV
OrthoDBiEOG092C4A4B

Family and domain databases

CDDicd04077 Peptidases_S8_PCSK9_Proteinase, 1 hit
Gene3Di3.30.70.80, 1 hit
3.40.50.200, 1 hit
InterProiView 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
PfamiView protein in Pfam
PF05922 Inhibitor_I9, 1 hit
PF00082 Peptidase_S8, 1 hit
PRINTSiPR00723 SUBTILISIN
SUPFAMiSSF52743 SSF52743, 1 hit
PROSITEiView protein in PROSITE
PS00136 SUBTILASE_ASP, 1 hit
PS00137 SUBTILASE_HIS, 1 hit
PS00138 SUBTILASE_SER, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P09232-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:635
Mass (Da):69,621
Last modified:July 1, 1989 - v1
Checksum:iC346C2B1C7DDDC48
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti622F → K in CAA77886 (Ref. 4) Curated1
Sequence conflicti622F → K in AAA34495 (Ref. 4) Curated1

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
PIRiA29358
RefSeqiNP_010854.1, NM_001178875.1

Genome annotation databases

EnsemblFungiiYEL060C; YEL060C; YEL060C
GeneIDi856649
KEGGisce:YEL060C

Similar proteinsi

Entry informationi

Entry nameiPRTB_YEAST
AccessioniPrimary (citable) accession number: P09232
Secondary accession number(s): D3DLJ0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: May 23, 2018
This is version 181 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome V
    Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

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