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Protein

Cerevisin

Gene

PRB1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei325 – 3251Charge relay systemBy similarity
Active sitei357 – 3571Charge relay systemBy similarity
Active sitei519 – 5191Charge relay systemBy similarity

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
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Prion, Protease, Serine protease

Enzyme and pathway databases

BioCyciYEAST:YEL060C-MONOMER.
BRENDAi3.4.21.48. 984.

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

GO - Cellular componenti

  • fungal-type vacuole Source: SGD
  • fungal-type vacuole lumen Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Amyloid, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Propeptidei20 – 2802611 PublicationPRO_0000027136Add
BLAST
Chaini281 – ?574294CerevisinPRO_0000027137Add
BLAST
Propeptidei?575 – 63561PRO_0000417567Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi460 ↔ 491Sequence analysis
Glycosylationi594 – 5941N-linked (GlcNAc...)Curated

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.
PeptideAtlasiP09232.
TopDownProteomicsiP09232.

2D gel databases

UCD-2DPAGEP09232.

PTM databases

iPTMnetiP09232.

Miscellaneous databases

PMAP-CutDBP09232.

Expressioni

Inductioni

Repressed by glucose.1 Publication

Interactioni

Protein-protein interaction databases

BioGridi36669. 77 interactions.
DIPiDIP-2544N.
IntActiP09232. 8 interactions.
MINTiMINT-407740.

Structurei

3D structure databases

ProteinModelPortaliP09232.
SMRiP09232. Positions 180-583.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini322 – 568247Peptidase S8Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi63 – 15492Lys-richAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S8 family.Curated
Contains 1 peptidase S8 domain.Curated

Keywords - Domaini

Signal

Phylogenomic databases

GeneTreeiENSGT00490000043472.
HOGENOMiHOG000199176.
InParanoidiP09232.
KOiK01336.
OMAiHKEWVAL.
OrthoDBiEOG7WT4B5.

Family and domain databases

Gene3Di3.30.70.80. 2 hits.
3.40.50.200. 1 hit.
InterProiIPR000209. Peptidase_S8/S53_dom.
IPR023827. Peptidase_S8_Asp-AS.
IPR022398. Peptidase_S8_His-AS.
IPR023828. Peptidase_S8_Ser-AS.
IPR015500. Peptidase_S8_subtilisin-rel.
IPR009020. Prot_inh_propept.
IPR010259. S8pro/Inhibitor_I9.
[Graphical view]
PANTHERiPTHR10795. PTHR10795. 2 hits.
PfamiPF05922. Inhibitor_I9. 1 hit.
PF00082. Peptidase_S8. 1 hit.
[Graphical view]
PRINTSiPR00723. SUBTILISIN.
SUPFAMiSSF52743. SSF52743. 1 hit.
SSF54897. SSF54897. 2 hits.
PROSITEiPS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti622 – 6221F → K in CAA77886 (Ref. 4) Curated
Sequence conflicti622 – 6221F → K in AAA34495 (Ref. 4) Curated

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.

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.
PIRiA29358.
RefSeqiNP_010854.1. NM_001178875.1.

3D structure databases

ProteinModelPortaliP09232.
SMRiP09232. Positions 180-583.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36669. 77 interactions.
DIPiDIP-2544N.
IntActiP09232. 8 interactions.
MINTiMINT-407740.

Protein family/group databases

MEROPSiS08.052.

PTM databases

iPTMnetiP09232.

2D gel databases

UCD-2DPAGEP09232.

Proteomic databases

MaxQBiP09232.
PeptideAtlasiP09232.
TopDownProteomicsiP09232.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYEL060C; YEL060C; YEL060C.
GeneIDi856649.
KEGGisce:YEL060C.

Organism-specific databases

EuPathDBiFungiDB:YEL060C.
SGDiS000000786. PRB1.

Phylogenomic databases

GeneTreeiENSGT00490000043472.
HOGENOMiHOG000199176.
InParanoidiP09232.
KOiK01336.
OMAiHKEWVAL.
OrthoDBiEOG7WT4B5.

Enzyme and pathway databases

BioCyciYEAST:YEL060C-MONOMER.
BRENDAi3.4.21.48. 984.

Miscellaneous databases

NextBioi982625.
PMAP-CutDBP09232.
PROiP09232.

Family and domain databases

Gene3Di3.30.70.80. 2 hits.
3.40.50.200. 1 hit.
InterProiIPR000209. Peptidase_S8/S53_dom.
IPR023827. Peptidase_S8_Asp-AS.
IPR022398. Peptidase_S8_His-AS.
IPR023828. Peptidase_S8_Ser-AS.
IPR015500. Peptidase_S8_subtilisin-rel.
IPR009020. Prot_inh_propept.
IPR010259. S8pro/Inhibitor_I9.
[Graphical view]
PANTHERiPTHR10795. PTHR10795. 2 hits.
PfamiPF05922. Inhibitor_I9. 1 hit.
PF00082. Peptidase_S8. 1 hit.
[Graphical view]
PRINTSiPR00723. SUBTILISIN.
SUPFAMiSSF52743. SSF52743. 1 hit.
SSF54897. SSF54897. 2 hits.
PROSITEiPS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Protease B of the lysosomelike vacuole of the yeast Saccharomyces cerevisiae is homologous to the subtilisin family of serine proteases."
    Moehle C.M., Tizard R., Lemmon S.K., Smart J., Jones E.W.
    Mol. Cell. Biol. 7:4390-4399(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 281-295.
    Strain: ATCC 204510 / AB320.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Saunders W.S., He L., Loo K.K., Hoyt M.
    Submitted (MAR-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 605-635.
    Strain: ATCC 204508 / S288c.
  5. "Protein degradation, meiosis and sporulation in proteinase-deficient mutants of Saccharomyces cerevisiae."
    Zubenko G.S., Jones E.W.
    Genetics 97:45-64(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Genetic properties of mutations at the PEP4 locus in Saccharomyces cerevisiae."
    Zubenko G.S., Park F.J., Jones E.W.
    Genetics 102:679-690(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Processing pathway for protease B of Saccharomyces cerevisiae."
    Moehle C.M., Dixon C.K., Jones E.W.
    J. Cell Biol. 108:309-325(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING.
  8. "Consequences of growth media, gene copy number, and regulatory mutations on the expression of the PRB1 gene of Saccharomyces cerevisiae."
    Moehle C.M., Jones E.W.
    Genetics 124:39-55(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  9. "Activation of the proteinase B precursor of the yeast Saccharomyces cerevisiae by autocatalysis and by an internal sequence."
    Nebes V.L., Jones E.W.
    J. Biol. Chem. 266:22851-22857(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING.
  10. "Heritable activity: a prion that propagates by covalent autoactivation."
    Roberts B.T., Wickner R.B.
    Genes Dev. 17:2083-2087(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRION IDENTIFICATION.
  11. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  12. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPRTB_YEAST
AccessioniPrimary (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: May 11, 2016
This is version 163 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.