ID   PPA5_YEAST              Reviewed;         467 AA.
AC   P00635; D6VQ94;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 2.
DT   02-SEP-2026, entry version 207.
DE   RecName: Full=Repressible acid phosphatase;
DE            EC=3.1.3.2;
DE   AltName: Full=P60;
DE   Flags: Precursor;
GN   Name=PHO5; OrderedLocusNames=YBR093C; ORFNames=YBR0814;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 18-26, AND CATALYTIC
RP   ACTIVITY.
RX   PubMed=6300772; DOI=10.1093/nar/11.6.1657;
RA   Arima K., Oshima T., Kubota I., Nakamura N., Mizunaga T., Toh-e A.;
RT   "The nucleotide sequence of the yeast PHO5 gene: a putative precursor of
RT   repressible acid phosphatase contains a signal peptide.";
RL   Nucleic Acids Res. 11:1657-1672(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 18-45.
RX   PubMed=6093051; DOI=10.1093/nar/12.20.7721;
RA   Bajwa W., Meyhack B., Rudolph H., Schweingruber A.-M., Hinnen A.;
RT   "Structural analysis of the two tandemly repeated acid phosphatase genes in
RT   yeast.";
RL   Nucleic Acids Res. 12:7721-7739(1984).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7900426; DOI=10.1002/yea.320101014;
RA   Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.;
RT   "Analysis of a 70 kb region on the right arm of yeast chromosome II.";
RL   Yeast 10:1363-1381(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44, CATALYTIC ACTIVITY, AND
RP   REPRESSION.
RX   PubMed=3537710; DOI=10.1128/mcb.6.6.1855-1865.1986;
RA   Tait-Kamradt A.G., Turner K.J., Kramer R.A., Elliott Q.D., Bostian S.J.,
RA   Thill G.P., Rogers D.T., Bostian K.A.;
RT   "Reciprocal regulation of the tandemly duplicated PHO5/PHO3 gene cluster
RT   within the acid phosphatase multigene family of Saccharomyces cerevisiae.";
RL   Mol. Cell. Biol. 6:1855-1865(1986).
RN   [7]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [8]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=16278456; DOI=10.1128/ec.4.11.1892-1901.2005;
RA   Kennedy E.J., Pillus L., Ghosh G.;
RT   "Pho5p and newly identified nucleotide pyrophosphatases/ phosphodiesterases
RT   regulate extracellular nucleotide phosphate metabolism in Saccharomyces
RT   cerevisiae.";
RL   Eukaryot. Cell 4:1892-1901(2005).
CC   -!- FUNCTION: Partially mediates extracellular nucleotide derived phosphate
CC       hydrolysis along with NPP1 and NPP2. {ECO:0000269|PubMed:16278456}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC         Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2;
CC         Evidence={ECO:0000269|PubMed:3537710, ECO:0000269|PubMed:6300772};
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- INDUCTION: Expression induced during phosphate starvation. Repressed by
CC       inorganic phosphate. {ECO:0000269|PubMed:16278456,
CC       ECO:0000269|PubMed:3537710}.
CC   -!- PTM: Glycosylated during secretion across the membrane.
CC   -!- MISCELLANEOUS: Present with 1110 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC       {ECO:0000305}.
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DR   EMBL; V01320; CAA24630.1; -; Genomic_DNA.
DR   EMBL; X01079; CAA25555.1; -; Genomic_DNA.
DR   EMBL; X78993; CAA55598.1; -; Genomic_DNA.
DR   EMBL; Z35962; CAA85046.1; -; Genomic_DNA.
DR   EMBL; X01080; CAA25556.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07214.1; -; Genomic_DNA.
DR   PIR; S05795; PABYC.
DR   RefSeq; NP_009651.3; NM_001178441.3.
DR   AlphaFoldDB; P00635; -.
DR   SMR; P00635; -.
DR   BioGRID; 32799; 88.
DR   DIP; DIP-4916N; -.
DR   FunCoup; P00635; 613.
DR   IntAct; P00635; 12.
DR   MINT; P00635; -.
DR   STRING; 4932.YBR093C; -.
DR   GlyCosmos; P00635; 12 sites, No reported glycans.
DR   GlyGen; P00635; 12 sites.
DR   iPTMnet; P00635; -.
DR   PaxDb; 4932-YBR093C; -.
DR   PeptideAtlas; P00635; -.
DR   TopDownProteomics; P00635; -.
DR   EnsemblFungi; YBR093C_mRNA; YBR093C; YBR093C.
DR   GeneID; 852390; -.
DR   KEGG; sce:YBR093C; -.
DR   AGR; SGD:S000000297; -.
DR   SGD; S000000297; PHO5.
DR   VEuPathDB; FungiDB:YBR093C; -.
DR   eggNOG; KOG1382; Eukaryota.
DR   HOGENOM; CLU_020880_3_1_1; -.
DR   InParanoid; P00635; -.
DR   OMA; WCAFEVN; -.
DR   OrthoDB; 6509975at2759; -.
DR   BioCyc; YEAST:YBR093C-MONOMER; -.
DR   BioGRID-ORCS; 852390; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P00635; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P00635; protein.
DR   GO; GO:0071944; C:cell periphery; HDA:SGD.
DR   GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
DR   GO; GO:0003993; F:acid phosphatase activity; IDA:SGD.
DR   GO; GO:0047429; F:nucleoside triphosphate diphosphatase activity; IMP:SGD.
DR   GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IMP:SGD.
DR   GO; GO:0016036; P:cellular response to phosphate starvation; IMP:SGD.
DR   GO; GO:0006796; P:phosphate-containing compound metabolic process; IMP:SGD.
DR   GO; GO:0008361; P:regulation of cell size; HMP:SGD.
DR   CDD; cd07061; HP_HAP_like; 1.
DR   FunFam; 3.40.50.1240:FF:000021; Acid phosphatase; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR033379; Acid_Pase_AS.
DR   InterPro; IPR000560; His_Pase_clade-2.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR016274; Histidine_acid_Pase_euk.
DR   PANTHER; PTHR20963:SF18; ACID PHOSPHATASE PHO11-RELATED; 1.
DR   PANTHER; PTHR20963; MULTIPLE INOSITOL POLYPHOSPHATE PHOSPHATASE-RELATED; 1.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   PIRSF; PIRSF000894; Acid_phosphatase; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
DR   PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Hydrolase; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000269|PubMed:6093051,
FT                   ECO:0000269|PubMed:6300772"
FT   CHAIN           18..467
FT                   /note="Repressible acid phosphatase"
FT                   /id="PRO_0000023954"
FT   ACT_SITE        75
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        338
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        97
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        162
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        192
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        250
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        315
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        356
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        390
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        439
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        445
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        456
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        461
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        36
FT                   /note="D -> Y (in Ref. 1; CAA24630)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        130
FT                   /note="A -> G (in Ref. 1; CAA24630)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        294
FT                   /note="H -> Q (in Ref. 1; CAA24630)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        446
FT                   /note="S -> V (in Ref. 1; CAA24630)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        462..463
FT                   /note="AS -> DT (in Ref. 1; CAA24630)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        466
FT                   /note="R -> K (in Ref. 1; CAA24630)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   467 AA;  52859 MW;  DC3C9504BC2D3D0C CRC64;
     MFKSVVYSIL AASLANAGTI PLGKLADVDK IGTQKDIFPF LGGAGPYYSF PGDYGISRDL
     PEGCEMKQLQ MVGRHGERYP TVSLAKTIKS TWYKLSNYTR QFNGSLSFLN DDYEFFIRDD
     DDLEMETTFA NSDDVLNPYT GEMNAKRHAR DFLAQYGYMV ENQTSFAVFT SNSKRCHDTA
     QYFIDGLGDQ FNITLQTVSE AESAGANTLS ACNSCPAWDY DANDDIVNEY DTTYLDDIAK
     RLNKENKGLN LTSTDASTLF SWCAFEVNAK GYSDVCDIFT KDELVHYSYY QDLHTYYHEG
     PGYDIIKSVG SNLFNASVKL LKQSEIQDQK VWLSFTHDTD ILNFLTTAGI IDDKNNLTAE
     YVPFMGNTFH RSWYVPQGAR VYTEKFQCSN DTYVRYVIND AVVPIETCST GPGFSCEIND
     FYDYAEKRVA GTDFLKVCNV SSVSNSTELT FYWDWNTTHY NASLLRQ
//