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Reviewed, UniProtKB/Swiss-Prot P00635 (PPA5_YEAST)

Last modified February 9, 2010. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Repressible acid phosphatase
    EC=3.1.3.2
Alternative name(s):
    P60
Gene names
Name: PHO5
Ordered Locus Names: YBR093C
ORF Names: YBR0814
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length467 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Partially mediates extracellular nucleotide derived phosphate hydrolysis along with NPP1 and NPP2. Ref.7

Catalytic activity

A phosphate monoester + H2O = an alcohol + phosphate. Ref.1 Ref.5

Subcellular location

Secreted.

Induction

Expression induced during phosphate starvation. Repressed by inorganic phosphate. Ref.7

Post-translational modification

Glycosylated during secretion across the membrane.

Miscellaneous

Present with 1110 molecules/cell in log phase SD medium. Ref.6

Sequence similarities

Belongs to the histidine acid phosphatase family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Ref.1 Ref.2
Chain18 – 467450Repressible acid phosphatase
PRO_0000023954

Sites

Active site751Nucleophile By similarity
Active site3381Proton donor By similarity

Amino acid modifications

Glycosylation971N-linked (GlcNAc...) Potential
Glycosylation1031N-linked (GlcNAc...) Potential
Glycosylation1621N-linked (GlcNAc...) Potential
Glycosylation1921N-linked (GlcNAc...) Potential
Glycosylation2501N-linked (GlcNAc...) Potential
Glycosylation3151N-linked (GlcNAc...) Potential
Glycosylation3561N-linked (GlcNAc...) Potential
Glycosylation3901N-linked (GlcNAc...) Potential
Glycosylation4391N-linked (GlcNAc...) Potential
Glycosylation4451N-linked (GlcNAc...) Potential
Glycosylation4561N-linked (GlcNAc...) Potential
Glycosylation4611N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict361D → Y in CAA24630. Ref.1
Sequence conflict1301A → G in CAA24630. Ref.1
Sequence conflict2941H → Q in CAA24630. Ref.1
Sequence conflict4461S → V in CAA24630. Ref.1
Sequence conflict462 – 4632AS → DT in CAA24630. Ref.1
Sequence conflict4661R → K in CAA24630. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
P00635-1 [UniParc].

Last modified October 1, 1994. Version 2.
Checksum: DC3C9504BC2D3D0C

FASTA46752,859
        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

« Hide

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References

« Hide 'large scale' references
[1]"The nucleotide sequence of the yeast PHO5 gene: a putative precursor of repressible acid phosphatase contains a signal peptide."
Arima K., Oshima T., Kubota I., Nakamura N., Mizunaga T., Toh-e A.
Nucleic Acids Res. 11:1657-1672(1983) [PubMed: 6300772] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 18-26, CATALYTIC ACTIVITY.
[2]"Structural analysis of the two tandemly repeated acid phosphatase genes in yeast."
Bajwa W., Meyhack B., Rudolph H., Schweingruber A.-M., Hinnen A.
Nucleic Acids Res. 12:7721-7739(1984) [PubMed: 6093051] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 18-45.
[3]"Analysis of a 70 kb region on the right arm of yeast chromosome II."
Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.
Yeast 10:1363-1381(1994) [PubMed: 7900426] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"Complete DNA sequence of yeast chromosome II."
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. expand/collapse author list , 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.
EMBO J. 13:5795-5809(1994) [PubMed: 7813418] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"Reciprocal regulation of the tandemly duplicated PHO5/PHO3 gene cluster within the acid phosphatase multigene family of Saccharomyces cerevisiae."
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.
Mol. Cell. Biol. 6:1855-1865(1986) [PubMed: 3537710] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44, CATALYTIC ACTIVITY, REPRESSION.
[6]"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].
[7]"Pho5p and newly identified nucleotide pyrophosphatases/ phosphodiesterases regulate extracellular nucleotide phosphate metabolism in Saccharomyces cerevisiae."
Kennedy E.J., Pillus L., Ghosh G.
Eukaryot. Cell 4:1892-1901(2005) [PubMed: 16278456] [Abstract]
Cited for: FUNCTION, INDUCTION.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		V01320 Genomic DNA. Translation: CAA24630.1.
X01079 Genomic DNA. Translation: CAA25555.1.
X78993 Genomic DNA. Translation: CAA55598.1.
Z35962 Genomic DNA. Translation: CAA85046.1.
X01080 Genomic DNA. Translation: CAA25556.1.
PIRPABYC. S05795.
RefSeqNP_009651.1.

3D structure databases

SMRP00635. Positions 9-466.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-4916N.
IntActP00635. 3 interactions.
STRINGP00635.

Proteomic databases

PeptideAtlasP00635.

Genome annotation databases

EnsemblYBR093C; YBR093C; YBR093C; Saccharomyces cerevisiae. [Genome view]
GeneID852390.
KEGGsce:YBR093C.
NMPDRfig|4932.3.peg.350.

Organism-specific databases

CYGDYBR093c.
SGDS000000297. PHO5.

Phylogenomic databases

eggNOGfuNOG08329.
HOGENOMHBG331692.
OMACAYELAT.
OrthoDBEOG9RBS1T.
PhylomeDBP00635.

Enzyme and pathway databases

BRENDA3.1.3.2. 250.

Gene expression databases

ArrayExpressP00635.
GenevestigatorP00635.
GermOnlineYBR093C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR000560. Histidine_acid_Pase.
IPR016274. Histidine_acid_Pase_euk.
[Graphical view]
PfamPF00328. Acid_phosphat_A. 1 hit.
[Graphical view]
PIRSFPIRSF000894. Acid_phosphatase. 1 hit.
PROSITEPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
PS00778. HIS_ACID_PHOSPHAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio971207.

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Entry information

Entry namePPA5_YEAST
AccessionPrimary (citable) accession number: P00635
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1994
Last modified: February 9, 2010
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome II

Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents