ID   PPA3_YEAST              Reviewed;         467 AA.
AC   P24031; D6VQ93;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 2.
DT   27-MAR-2024, entry version 176.
DE   RecName: Full=Constitutive acid phosphatase;
DE            EC=3.1.3.2;
DE   Flags: Precursor;
GN   Name=PHO3; OrderedLocusNames=YBR092C; ORFNames=YBR0813;
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].
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   [2]
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   [3]
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   [4]
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   [5]
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).
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   -!- MISCELLANEOUS: Present with 952 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; X01080; CAA25557.1; -; Genomic_DNA.
DR   EMBL; X78993; CAA55597.1; -; Genomic_DNA.
DR   EMBL; Z35961; CAA85045.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07213.1; -; Genomic_DNA.
DR   PIR; S48259; PABYCC.
DR   RefSeq; NP_009650.1; NM_001178440.1.
DR   AlphaFoldDB; P24031; -.
DR   SMR; P24031; -.
DR   BioGRID; 32798; 77.
DR   STRING; 4932.YBR092C; -.
DR   GlyCosmos; P24031; 12 sites, No reported glycans.
DR   GlyGen; P24031; 12 sites.
DR   iPTMnet; P24031; -.
DR   MaxQB; P24031; -.
DR   PaxDb; 4932-YBR092C; -.
DR   PeptideAtlas; P24031; -.
DR   EnsemblFungi; YBR092C_mRNA; YBR092C; YBR092C.
DR   GeneID; 852389; -.
DR   KEGG; sce:YBR092C; -.
DR   AGR; SGD:S000000296; -.
DR   SGD; S000000296; PHO3.
DR   VEuPathDB; FungiDB:YBR092C; -.
DR   eggNOG; KOG1382; Eukaryota.
DR   GeneTree; ENSGT00390000018409; -.
DR   HOGENOM; CLU_020880_3_1_1; -.
DR   InParanoid; P24031; -.
DR   OMA; TGEMDAK; -.
DR   OrthoDB; 2404758at2759; -.
DR   BioCyc; YEAST:YBR092C-MONOMER; -.
DR   BRENDA; 3.1.3.2; 984.
DR   BioGRID-ORCS; 852389; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P24031; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P24031; Protein.
DR   GO; GO:0030287; C:cell wall-bounded periplasmic space; IMP:SGD.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR   GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
DR   GO; GO:0003993; F:acid phosphatase activity; IMP:SGD.
DR   GO; GO:0006796; P:phosphate-containing compound metabolic process; IDA:SGD.
DR   GO; GO:0042723; P:thiamine-containing compound metabolic process; IDA:SGD.
DR   CDD; cd07061; HP_HAP_like; 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   Glycoprotein; Hydrolase; Reference proteome; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..467
FT                   /note="Constitutive acid phosphatase"
FT                   /id="PRO_0000023953"
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        219..221
FT                   /note="DED -> MKT (in Ref. 1; CAA25557)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   467 AA;  52777 MW;  05FBB80DEB41B0FF CRC64;
     MFKSVVYSVL AAALVNAGTI PLGELADVAK IGTQEDIFPF LGGAGPYFSF PGDYGISRDL
     PEGCEMKQLQ MLARHGERYP TYSKGATIMK TWYKLSNYTR QFNGSLSFLN DDYEFFIRDD
     DDLEMETTFA NSDNVLNPYT GEMDAKRHAR EFLAQYGYMF ENQTSFPIFA ASSERVHDTA
     QYFIDGLGDQ FNISLQTVSE AMSAGANTLS AGNACPGWDE DANDDILDKY DTTYLDDIAK
     RLNKENKGLN LTSKDANTLF AWCAYELNAR GYSDVCDIFT EDELVRYSYG QDLVSFYQDG
     PGYDMIRSVG ANLFNATLKL LKQSETQDLK VWLSFTHDTD ILNYLTTAGI IDDKNNLTAE
     YVPFMGNTFH KSWYVPQGAR VYTEKFQCSN DTYVRYVIND AVVPIETCST GPGFSCEIND
     FYDYAEKRVA GTDFLKVCNV SSVSNVTELT FYWDWNTTHY NDTLLKQ
//