ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P00635


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name PPA5_YEAST
Primary accession number P00635
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on October 1, 1994 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 86)
Name and origin of the protein
Protein name Repressible acid phosphatase [Precursor]
Synonyms EC 3.1.3.2
P60
Gene name
Name: PHO5
OrderedLocusNames: YBR093C
ORFNames: YBR0814
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 18-26, AND CATALYTIC ACTIVITY.
DOI=10.1093/nar/11.6.1657; PubMed=6300772 [NCBI, ExPASy, EBI, Israel, Japan]
Arima K., Oshima T., Kubota I., Nakamura N., Mizunaga T., Toh-e A.;
"The nucleotide sequence of the yeast PHO5 gene: a putative precursor of repressible acid phosphatase contains a signal peptide.";
Nucleic Acids Res. 11:1657-1672(1983).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 18-45.
DOI=10.1093/nar/12.20.7721; PubMed=6093051 [NCBI, ExPASy, EBI, Israel, Japan]
Bajwa W., Meyhack B., Rudolph H., Schweingruber A.-M., Hinnen A.;
"Structural analysis of the two tandemly repeated acid phosphatase genes in yeast.";
Nucleic Acids Res. 12:7721-7739(1984).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1002/yea.320101014; PubMed=7900426 [NCBI, ExPASy, EBI, Israel, Japan]
Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.;
"Analysis of a 70 kb region on the right arm of yeast chromosome II.";
Yeast 10:1363-1381(1994).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7813418 [NCBI, ExPASy, EBI, Israel, Japan]
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.;
"Complete DNA sequence of yeast chromosome II.";
EMBO J. 13:5795-5809(1994).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44, CATALYTIC ACTIVITY, AND REPRESSION.
PubMed=3537710 [NCBI, ExPASy, EBI, Israel, Japan]
Tait-Kamradt A.G., Turner K.J., Kramer R.A., Elliott Q.D., Bostian S.J., Thill G.P., Rogers D.T., Bostian K.A.;
"Reciprocal regulation of the tandemly duplicated PHO5/PHO3 gene cluster within the acid phosphatase multigene family of Saccharomyces cerevisiae.";
Mol. Cell. Biol. 6:1855-1865(1986).
[6]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[7]
FUNCTION, AND INDUCTION.
DOI=10.1128/EC.4.11.1892-1901.2005; PubMed=16278456 [NCBI, ExPASy, EBI, Israel, Japan]
Kennedy E.J., Pillus L., Ghosh G.;
"Pho5p and newly identified nucleotide pyrophosphatases/ phosphodiesterases regulate extracellular nucleotide phosphate metabolism in Saccharomyces cerevisiae.";
Eukaryot. Cell 4:1892-1901(2005).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
V01320; CAA24630.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X01079; CAA25555.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X78993; CAA55598.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z35962; CAA85046.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X01080; CAA25556.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S05795; PABYC.
RefSeq NP_009651.1; -.
3D structure databases
HSSP P34755; 1QFX. [HSSP ENTRY / PDB]
ModBase P00635.
Protein-protein interaction databases
DIP DIP:4916N; -.
IntAct P00635; -.
Organism-specific databases
CYGD YBR093c; -.
SGD S000000297; PHO5.
Yeast-GFP YBR093C.
Gene expression databases
ArrayExpress P00635; -.
GermOnline YBR093C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0030287; Cellular component: cell wall-bounded periplasmic space (non-traceable author statement from SGD).
GO:0009277; Cellular component: fungal-type cell wall (inferred from direct assay from SGD).
GO:0003993; Molecular function: acid phosphatase activity (traceable author statement from SGD).
GO:0017111; Molecular function: nucleoside-triphosphatase activity (inferred from genetic interaction from SGD).
GO:0047429; Molecular function: nucleoside-triphosphate diphosphatase activity (inferred from genetic interaction from SGD).
GO:0016036; Biological process: cellular response to phosphate starvation (inferred from expression pattern from SGD).
GO:0006796; Biological process: phosphate metabolic process (inferred from mutant phenotype from SGD).
GO:0008361; Biological process: regulation of cell size (inferred from mutant phenotype from SGD).
QuickGo view.
Family and domain databases
InterPro IPR000560; Histidine_acid_Pase.
IPR016274; Histidine_acid_Pase_euk.
Graphical view of domain structure.
Pfam PF00328; Acid_phosphat_A; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000894; Acid_phosphatase; 1.
PROSITE PS00616; HIS_ACID_PHOSPHAT_1; 1.
PS00778; HIS_ACID_PHOSPHAT_2; 1.
BLOCKS P00635.
ProtoNet P00635.
Proteomic databases
PeptideAtlas P00635; -.
Genome annotation databases
Ensembl YBR093C; Saccharomyces cerevisiae. [Contig view]
GeneID 852390; -.
GenomeReviews Y13134_GR; YBR093C.
KEGG sce:YBR093C; -.
NMPDR fig|4932.3.peg.350; -.
Phylogenomic databases
HOGENOM P00635; -.
Other
LinkHub P00635; -.
NextBio 971207; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Direct protein sequencing; Glycoprotein; Hydrolase; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    17  17      
CHAIN   18   467  450     Repressible acid phosphatase. PRO_0000023954
ACT_SITE   75    75        Nucleophile (By similarity). 
ACT_SITE   338   338        Proton donor (By similarity). 
CARBOHYD   97    97        N-linked (GlcNAc...) (Potential). 
CARBOHYD   103   103        N-linked (GlcNAc...) (Potential). 
CARBOHYD   162   162        N-linked (GlcNAc...) (Potential). 
CARBOHYD   192   192        N-linked (GlcNAc...) (Potential). 
CARBOHYD   250   250        N-linked (GlcNAc...) (Potential). 
CARBOHYD   315   315        N-linked (GlcNAc...) (Potential). 
CARBOHYD   356   356        N-linked (GlcNAc...) (Potential). 
CARBOHYD   390   390        N-linked (GlcNAc...) (Potential). 
CARBOHYD   439   439        N-linked (GlcNAc...) (Potential). 
CARBOHYD   445   445        N-linked (GlcNAc...) (Potential). 
CARBOHYD   456   456        N-linked (GlcNAc...) (Potential). 
CARBOHYD   461   461        N-linked (GlcNAc...) (Potential). 
CONFLICT   36    36        D -> Y (in Ref. 1; CAA24630). 
CONFLICT   130   130        A -> G (in Ref. 1; CAA24630). 
CONFLICT   294   294        H -> Q (in Ref. 1; CAA24630). 
CONFLICT   446   446        S -> V (in Ref. 1; CAA24630). 
CONFLICT   462   463        AS -> DT (in Ref. 1; CAA24630). 
CONFLICT   466   466        R -> K (in Ref. 1; CAA24630). 
Sequence information
Length: 467 AA [This is the length of the unprocessed precursor] Molecular weight: 52859 Da [This is the MW of the unprocessed precursor] CRC64: DC3C9504BC2D3D0C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MFKSVVYSIL AASLANAGTI PLGKLADVDK IGTQKDIFPF LGGAGPYYSF PGDYGISRDL 

        70         80         90        100        110        120 
PEGCEMKQLQ MVGRHGERYP TVSLAKTIKS TWYKLSNYTR QFNGSLSFLN DDYEFFIRDD 

       130        140        150        160        170        180 
DDLEMETTFA NSDDVLNPYT GEMNAKRHAR DFLAQYGYMV ENQTSFAVFT SNSKRCHDTA 

       190        200        210        220        230        240 
QYFIDGLGDQ FNITLQTVSE AESAGANTLS ACNSCPAWDY DANDDIVNEY DTTYLDDIAK 

       250        260        270        280        290        300 
RLNKENKGLN LTSTDASTLF SWCAFEVNAK GYSDVCDIFT KDELVHYSYY QDLHTYYHEG 

       310        320        330        340        350        360 
PGYDIIKSVG SNLFNASVKL LKQSEIQDQK VWLSFTHDTD ILNFLTTAGI IDDKNNLTAE 

       370        380        390        400        410        420 
YVPFMGNTFH RSWYVPQGAR VYTEKFQCSN DTYVRYVIND AVVPIETCST GPGFSCEIND 

       430        440        450        460 
FYDYAEKRVA GTDFLKVCNV SSVSNSTELT FYWDWNTTHY NASLLRQ 

P00635 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!