ID   PRTB_YEAST              Reviewed;         635 AA.
AC   P09232;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   16-JUN-2009, entry version 98.
DE   RecName: Full=Cerevisin;
DE            EC=3.4.21.48;
DE   AltName: Full=Vacuolar protease B;
DE   AltName: Full=Proteinase YSCB;
DE   Flags: Precursor;
GN   Name=PRB1; OrderedLocusNames=YEL060C;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 281-295.
RC   STRAIN=ATCC 204510 / AB320;
RX   MEDLINE=88142830; PubMed=3325823;
RA   Moehle C.M., Tizard R., Lemmon S.K., Smart J., Jones E.W.;
RT   "Protease B of the lysosomelike vacuole of the yeast Saccharomyces
RT   cerevisiae is homologous to the subtilisin family of serine
RT   proteases.";
RL   Mol. Cell. Biol. 7:4390-4399(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   MEDLINE=97313264; PubMed=9169868;
RA   Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA   Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G.,
RA   Hunicke-Smith S., Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H.,
RA   Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P.,
RA   Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T.,
RA   Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL   Nature 387:78-81(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 605-635.
RC   STRAIN=ATCC 204508 / S288c;
RA   Saunders W.S., He L., Loo K.K., Hoyt M.;
RL   Submitted (MAR-1992) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PROTEOLYTIC PROCESSING.
RX   MEDLINE=92078140; PubMed=1744078;
RA   Nebes V.L., Jones E.W.;
RT   "Activation of the proteinase B precursor of the yeast Saccharomyces
RT   cerevisiae by autocatalysis and by an internal sequence.";
RL   J. Biol. Chem. 266:22851-22857(1991).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, AND MASS
RP   SPECTROMETRY.
RX   PubMed=17563356; DOI=10.1073/pnas.0701622104;
RA   Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
RT   "Proteome-wide identification of in vivo targets of DNA damage
RT   checkpoint kinases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, AND MASS
RP   SPECTROMETRY.
RX   PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
CC   -!- FUNCTION: Among other substrates, acts on yscA (PEP4) to activate
CC       it by processing its Pro-peptide.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of proteins with broad specificity,
CC       and of Bz-Arg-OEt > Ac-Tyr-OEt. Does not hydrolyze peptide amides.
CC   -!- SUBCELLULAR LOCATION: Vacuole. Note=Lysosome-like vacuoles.
CC   -!- MISCELLANEOUS: Present with 1600 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
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DR   EMBL; M18097; AAA34901.1; -; Genomic_DNA.
DR   EMBL; U18795; AAB65027.1; -; Genomic_DNA.
DR   EMBL; Z11859; CAA77886.1; -; Genomic_DNA.
DR   EMBL; M90522; AAA34495.1; -; Genomic_DNA.
DR   PIR; A29358; A29358.
DR   RefSeq; NP_010854.1; -.
DR   HSSP; P06873; 1IC6.
DR   DIP; DIP:2544N; -.
DR   IntAct; P09232; 18.
DR   MEROPS; S08.052; -.
DR   PeptideAtlas; P09232; -.
DR   PRIDE; P09232; -.
DR   Ensembl; YEL060C; Saccharomyces cerevisiae.
DR   GeneID; 856649; -.
DR   GenomeReviews; U00092_GR; YEL060C.
DR   KEGG; sce:YEL060C; -.
DR   NMPDR; fig|4932.3.peg.1902; -.
DR   CYGD; YEL060c; -.
DR   SGD; S000000786; PRB1.
DR   HOGENOM; P09232; -.
DR   OMA; P09232; WGKTIPL.
DR   BRENDA; 3.4.21.48; 250.
DR   NextBio; 982625; -.
DR   PMAP-CutDB; P09232; -.
DR   ArrayExpress; P09232; -.
DR   GermOnline; YEL060C; Saccharomyces cerevisiae.
DR   GO; GO:0000328; C:fungal-type vacuole lumen; TAS:SGD.
DR   GO; GO:0042802; F:identical protein binding; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; TAS:SGD.
DR   GO; GO:0009267; P:cellular response to starvation; IMP:SGD.
DR   GO; GO:0043086; P:negative regulation of catalytic activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cel...; IMP:SGD.
DR   GO; GO:0007039; P:vacuolar protein catabolic process; IMP:SGD.
DR   InterPro; IPR000209; Pept_S8_S53.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR010259; Prot_inh_S8A.
DR   Gene3D; G3DSA:3.40.50.200; Pept_S8_S53; 1.
DR   PANTHER; PTHR10795; SubtilSerProt; 1.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Direct protein sequencing; Disulfide bond;
KW   Glycoprotein; Hydrolase; Phosphoprotein; Protease; Serine protease;
KW   Signal; Vacuole; Zymogen.
FT   SIGNAL        1     19       Potential.
FT   PROPEP       20    280
FT                                /FTId=PRO_0000027136.
FT   CHAIN       281    635       Cerevisin.
FT                                /FTId=PRO_0000027137.
FT   ACT_SITE    325    325       Charge relay system (By similarity).
FT   ACT_SITE    357    357       Charge relay system (By similarity).
FT   ACT_SITE    519    519       Charge relay system (By similarity).
FT   MOD_RES      58     58       Phosphoserine.
FT   CARBOHYD    594    594       N-linked (GlcNAc...) (Probable).
FT   DISULFID    460    491       Potential.
FT   CONFLICT    622    622       F -> K (in Ref. 3; CAA77886/AAA34495).
SQ   SEQUENCE   635 AA;  69621 MW;  C346C2B1C7DDDC48 CRC64;
     MKLENTLFTL GALGSISAAL VIPNLENAAD HHELINKEDH HERPRKVEFT KDDDEEPSDS
     EDKEHGKFHK KGRKGQDKES PEFNGKRASG SHGSAHEGGK GMKPKHESSN DDDNDDKKKK
     PHHKGGCHEN KVEEKKMKGK KVKGKKHHEK TLEKGRHHNR LAPLVSTAQF NPDAISKIIP
     NRYIIVFKRG APQEEIDFHK ENVQQAQLQS VENLSAEDAF FISTKDTSLS TSEAGGIQDS
     FNIDNLFSGY IGYFTQEIVD LIRQNPLVDF VERDSIVEAT EFDTQNSAPW GLARISHRER
     LNLGSFNKYL YDDDAGRGVT SYVIDTGVNI NHKDFEKRAI WGKTIPLNDE DLDGNGHGTH
     CAGTIASKHY GVAKNANVVA VKVLRSNGSG TMSDVVKGVE YAAKAHQKEA QEKKKGFKGS
     TANMSLGGGK SPALDLAVNA AVEVGIHFAV AAGNENQDAC NTSPASADKA ITVGASTLSD
     DRAYFSNWGK CVDVFAPGLN ILSTYIGSDD ATATLSGTSM ASPHVAGLLT YFLSLQPGSD
     SEFFELGQDS LTPQQLKKKL IHYSTKDILF DIPEDTPNVL IYNGGGQDLS AFWNDTKKSH
     SSGFKQELNM DEFIGSKTDL IFDQVRDILD KLNII
//