Reviewed, UniProtKB/Swiss-Prot P09232 (PRTB_YEAST)

Names and origin

Protein names

Recommended name:
    Cerevisin
    EC=3.4.21.48
Alternative name(s):
    Vacuolar protease B
    Proteinase YSCB

Gene names

Name:	PRB1
Ordered Locus Names:	YEL060C

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	635 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Among other substrates, acts on yscA (PEP4) to activate it by processing its Pro-peptide.
Catalytic activity	Hydrolysis of proteins with broad specificity, and of Bz-Arg-OEt > Ac-Tyr-OEt. Does not hydrolyze peptide amides.
Subcellular location	Vacuole. Note: Lysosome-like vacuoles.
Miscellaneous	Present with 1600 molecules/cell in log phase SD medium. Ref.5
Sequence similarities	Belongs to the peptidase S8 family.

Ontologies

Keywords
Cellular component	Vacuole
Domain	Signal
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Glycoprotein Phosphoprotein Zymogen
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cellular response to starvation Inferred from mutant phenotype. Source: SGD negative regulation of catalytic activity Inferred from electronic annotation. Source: InterPro proteolysis Inferred from electronic annotation. Source: InterPro sporulation resulting in formation of a cellular spore Inferred from mutant phenotype. Source: SGD vacuolar protein catabolic process Inferred from mutant phenotype. Source: SGD
Cellular component	fungal-type vacuole lumen Traceable author statement. Source: SGD
Molecular function	identical protein binding Inferred from electronic annotation. Source: InterPro serine-type endopeptidase activity Ref.4 Traceable author statement. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Potential
	Propeptide	20 – 280	261	Ref.1		PRO_0000027136
	Chain	281 – 635	355	Cerevisin		PRO_0000027137
Sites
	Active site	325	1	Charge relay system By similarity
	Active site	357	1	Charge relay system By similarity
	Active site	519	1	Charge relay system By similarity
Amino acid modifications
	Modified residue	58	1	Phosphoserine Ref.6 Ref.7
	Glycosylation	594	1	N-linked (GlcNAc...) Probable
	Disulfide bond	460 ↔ 491		Potential
Experimental info
	Sequence conflict	622	1	F → K in CAA77886. Ref.3
	Sequence conflict	622	1	F → K in AAA34495. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P09232-1 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: C346C2B1C7DDDC48	FASTA	635	69,621
	10 20 30 40 50 60 MKLENTLFTL GALGSISAAL VIPNLENAAD HHELINKEDH HERPRKVEFT KDDDEEPSDS 70 80 90 100 110 120 EDKEHGKFHK KGRKGQDKES PEFNGKRASG SHGSAHEGGK GMKPKHESSN DDDNDDKKKK 130 140 150 160 170 180 PHHKGGCHEN KVEEKKMKGK KVKGKKHHEK TLEKGRHHNR LAPLVSTAQF NPDAISKIIP 190 200 210 220 230 240 NRYIIVFKRG APQEEIDFHK ENVQQAQLQS VENLSAEDAF FISTKDTSLS TSEAGGIQDS 250 260 270 280 290 300 FNIDNLFSGY IGYFTQEIVD LIRQNPLVDF VERDSIVEAT EFDTQNSAPW GLARISHRER 310 320 330 340 350 360 LNLGSFNKYL YDDDAGRGVT SYVIDTGVNI NHKDFEKRAI WGKTIPLNDE DLDGNGHGTH 370 380 390 400 410 420 CAGTIASKHY GVAKNANVVA VKVLRSNGSG TMSDVVKGVE YAAKAHQKEA QEKKKGFKGS 430 440 450 460 470 480 TANMSLGGGK SPALDLAVNA AVEVGIHFAV AAGNENQDAC NTSPASADKA ITVGASTLSD 490 500 510 520 530 540 DRAYFSNWGK CVDVFAPGLN ILSTYIGSDD ATATLSGTSM ASPHVAGLLT YFLSLQPGSD 550 560 570 580 590 600 SEFFELGQDS LTPQQLKKKL IHYSTKDILF DIPEDTPNVL IYNGGGQDLS AFWNDTKKSH 610 620 630 SSGFKQELNM DEFIGSKTDL IFDQVRDILD KLNII

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 3325823] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 281-295. Strain: ATCC 204510 / AB320.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome V." Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W. Nature 387:78-81(1997) [PubMed: 9169868] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	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.
[4]	"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: 1744078] [Abstract] Cited for: PROTEOLYTIC PROCESSING.
[5]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, MASS SPECTROMETRY.
[7]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M18097 Genomic DNA. Translation: AAA34901.1. U18795 Genomic DNA. Translation: AAB65027.1. Z11859 Genomic DNA. Translation: CAA77886.1. M90522 Genomic DNA. Translation: AAA34495.1.
PIR	A29358.
RefSeq	NP_010854.1.
3D structure databases
HSSP	HSSP built from PDB template 1IC6 based on UniProtKB P06873.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:2544N.
IntAct	P09232. 18 interactions.
Protein family/group databases
MEROPS	S08.052.
Proteomic databases
PeptideAtlas	P09232.
PRIDE	P09232.
Genome annotation databases
Ensembl	YEL060C. Saccharomyces cerevisiae. [Contig view]
GeneID	856649.
GenomeReviews	Gene locus YEL060C in contig U00092_GR.
KEGG	sce:YEL060C.
NMPDR	fig|4932.3.peg.1902.
Organism-specific databases
CYGD	YEL060c.
SGD	S000000786. PRB1.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P09232.
OMA	P09232. WGKTIPL.
Enzyme and pathway databases
BRENDA	3.4.21.48. 250.
Gene expression databases
ArrayExpress	P09232.
GermOnline	YEL060C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000209. Pept_S8_S53. IPR015500. Peptidase_S8_subtilisin-rel. IPR010259. Prot_inh_S8A. [Graphical view]
Gene3D	G3DSA:3.40.50.200. Pept_S8_S53. 1 hit.
PANTHER	PTHR10795. SubtilSerProt. 1 hit.
Pfam	PF05922. Inhibitor_I9. 1 hit. PF00082. Peptidase_S8. 1 hit. [Graphical view]
PRINTS	PR00723. SUBTILISIN.
PROSITE	PS00136. SUBTILASE_ASP. 1 hit. PS00137. SUBTILASE_HIS. 1 hit. PS00138. SUBTILASE_SER. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	982625.
PMAP-CutDB	P09232.

Entry information

Entry name

PRTB_YEAST

Accession

Primary (citable) accession number: P09232

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	June 16, 2009
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)