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UniProtKB/Swiss-Prot entry P24031


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

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Entry information
Entry name PPA3_YEAST
Primary accession number P24031
Secondary accession numbers None
Integrated into Swiss-Prot on March 1, 1992
Sequence was last modified on October 1, 1994 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 74)
Name and origin of the protein
Protein name Constitutive acid phosphatase [Precursor]
Synonym EC 3.1.3.2
Gene name
Name: PHO3
OrderedLocusNames: YBR092C
ORFNames: YBR0813
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].
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).
[2]
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).
[3]
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).
[4]
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).
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
X01080; CAA25557.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X78993; CAA55597.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z35961; CAA85045.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S48259; PABYCC.
RefSeq NP_009650.1; -.
3D structure databases
HSSP P34755; 1QFX. [HSSP ENTRY / PDB]
ModBase P24031.
Protein-protein interaction databases
IntAct P24031; -.
Organism-specific databases
CYGD YBR092c; -.
SGD S000000296; PHO3.
Yeast-GFP YBR092C.
Gene expression databases
GermOnline YBR092C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0030287; Cellular component: cell wall-bounded periplasmic space (inferred from mutant phenotype from SGD).
GO:0003993; Molecular function: acid phosphatase activity (inferred from electronic annotation from InterPro).
GO:0042802; Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0006796; Biological process: phosphate metabolic process (inferred from direct assay from SGD).
GO:0042723; Biological process: thiamin and derivative metabolic process (inferred from direct assay 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 P24031.
ProtoNet P24031.
Proteomic databases
PeptideAtlas P24031; -.
Genome annotation databases
Ensembl YBR092C; Saccharomyces cerevisiae. [Contig view]
GeneID 852389; -.
GenomeReviews Y13134_GR; YBR092C.
KEGG sce:YBR092C; -.
NMPDR fig|4932.3.peg.349; -.
Phylogenomic databases
HOGENOM P24031; -.
Other
LinkHub P24031; -.
NextBio 971204; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Glycoprotein; Hydrolase; Signal.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    17  17     Potential. 
CHAIN   18   467  450     Constitutive acid phosphatase. PRO_0000023953
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   219   221        DED -> MKT (in Ref. 1; CAA25557). 
Sequence information
Length: 467 AA [This is the length of the unprocessed precursor] Molecular weight: 52777 Da [This is the MW of the unprocessed precursor] CRC64: 05FBB80DEB41B0FF [This is a checksum on the sequence]
        10         20         30         40         50         60 
MFKSVVYSVL AAALVNAGTI PLGELADVAK IGTQEDIFPF LGGAGPYFSF PGDYGISRDL 

        70         80         90        100        110        120 
PEGCEMKQLQ MLARHGERYP TYSKGATIMK TWYKLSNYTR QFNGSLSFLN DDYEFFIRDD 

       130        140        150        160        170        180 
DDLEMETTFA NSDNVLNPYT GEMDAKRHAR EFLAQYGYMF ENQTSFPIFA ASSERVHDTA 

       190        200        210        220        230        240 
QYFIDGLGDQ FNISLQTVSE AMSAGANTLS AGNACPGWDE DANDDILDKY DTTYLDDIAK 

       250        260        270        280        290        300 
RLNKENKGLN LTSKDANTLF AWCAYELNAR GYSDVCDIFT EDELVRYSYG QDLVSFYQDG 

       310        320        330        340        350        360 
PGYDMIRSVG ANLFNATLKL LKQSETQDLK VWLSFTHDTD ILNYLTTAGI IDDKNNLTAE 

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

       430        440        450        460 
FYDYAEKRVA GTDFLKVCNV SSVSNVTELT FYWDWNTTHY NDTLLKQ 

P24031 in FASTA format

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View entry in raw text format (no links)
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