PPA5_YEAST
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 03-AUG-2022, entry version 191.
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; 81.
DR DIP; DIP-4916N; -.
DR IntAct; P00635; 8.
DR MINT; P00635; -.
DR STRING; 4932.YBR093C; -.
DR MaxQB; P00635; -.
DR PaxDb; P00635; -.
DR PRIDE; P00635; -.
DR TopDownProteomics; P00635; -.
DR EnsemblFungi; YBR093C_mRNA; YBR093C; YBR093C.
DR GeneID; 852390; -.
DR KEGG; sce:YBR093C; -.
DR SGD; S000000297; PHO5.
DR VEuPathDB; FungiDB:YBR093C; -.
DR eggNOG; KOG1382; Eukaryota.
DR GeneTree; ENSGT00390000018409; -.
DR HOGENOM; CLU_020880_3_1_1; -.
DR InParanoid; P00635; -.
DR OMA; WDYDAND; -.
DR BioCyc; YEAST:YBR093C-MON; -.
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:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
DR GO; GO:0003993; F:acid phosphatase activity; IDA:SGD.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IMP:SGD.
DR GO; GO:0047429; F:nucleoside-triphosphate diphosphatase 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 Gene3D; 3.40.50.1240; -; 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 Pfam; PF00328; His_Phos_2; 1.
DR PIRSF; PIRSF000894; Acid_phosphatase; 1.
DR SUPFAM; SSF53254; SSF53254; 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
