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PPAB_YEAST
ID   PPAB_YEAST              Reviewed;         467 AA.
AC   P35842; D6VPP1;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 163.
DE   RecName: Full=Acid phosphatase PHO11;
DE            EC=3.1.3.2;
DE   AltName: Full=P56;
DE   Flags: Precursor;
GN   Name=PHO11; OrderedLocusNames=YAR071W;
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].
RA   Chen J.Y., Gong Y.I., Ao S.Z.;
RT   "The primary structure of acid phosphatase gene PHO11 in S. cerevisiae and
RT   comparison with other gene families.";
RL   Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 21:437-444(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RA   Bussey H., Keng T., Storms R.K., Vo D., Zhong W., Fortin N., Barton A.B.,
RA   Kaback D.B., Clark M.W.;
RT   "Sequencing of chromosome I of Saccharomyces cerevisiae: analysis of the 52
RT   Kbp CDC15-FLO1-PHO11-YAR074 region.";
RL   Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA   Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA   Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA   Storms R.K.;
RT   "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
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   -!- INDUCTION: S.cerevisiae has 2 types of acid phosphatase: one is
CC       constitutive and the other is repressible by inorganic phosphate.
CC   -!- PTM: Glycosylated during secretion across the membrane.
CC   -!- MISCELLANEOUS: Present with 1460 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; U19789; AAA73479.1; -; Genomic_DNA.
DR   EMBL; L28920; AAC09508.1; -; Genomic_DNA.
DR   EMBL; BK006935; DAA07011.1; -; Genomic_DNA.
DR   PIR; S53476; S53476.
DR   RefSeq; NP_009434.1; NM_001178239.1.
DR   AlphaFoldDB; P35842; -.
DR   SMR; P35842; -.
DR   BioGRID; 31819; 122.
DR   DIP; DIP-4589N; -.
DR   IntAct; P35842; 1.
DR   MINT; P35842; -.
DR   STRING; 4932.YAR071W; -.
DR   MaxQB; P35842; -.
DR   PaxDb; P35842; -.
DR   PRIDE; P35842; -.
DR   EnsemblFungi; YAR071W_mRNA; YAR071W; YAR071W.
DR   GeneID; 851299; -.
DR   KEGG; sce:YAR071W; -.
DR   SGD; S000000094; PHO11.
DR   VEuPathDB; FungiDB:YAR071W; -.
DR   eggNOG; KOG1382; Eukaryota.
DR   GeneTree; ENSGT00390000018409; -.
DR   HOGENOM; CLU_020880_3_1_1; -.
DR   InParanoid; P35842; -.
DR   OMA; WTICAME; -.
DR   BioCyc; YEAST:YAR071W-MON; -.
DR   PRO; PR:P35842; -.
DR   Proteomes; UP000002311; Chromosome I.
DR   RNAct; P35842; protein.
DR   GO; GO:0071944; C:cell periphery; HDA:SGD.
DR   GO; GO:0005576; C:extracellular region; IDA:SGD.
DR   GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
DR   GO; GO:0003993; F:acid phosphatase activity; IDA:SGD.
DR   GO; GO:0006796; P:phosphate-containing compound metabolic process; TAS: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   Glycoprotein; Hydrolase; Reference proteome; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000250"
FT   CHAIN           18..467
FT                   /note="Acid phosphatase PHO11"
FT                   /id="PRO_0000023956"
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        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        461
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        17
FT                   /note="A -> L (in Ref. 1; AAA73479)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        82..83
FT                   /note="VS -> AR (in Ref. 1; AAA73479)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        150
FT                   /note="R -> H (in Ref. 1; AAA73479)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        354
FT                   /note="K -> Q (in Ref. 1; AAA73479)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        423
FT                   /note="D -> G (in Ref. 1; AAA73479)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   467 AA;  52758 MW;  AECDC1C046B326C3 CRC64;
     MLKSAVYSIL AASLVNAGTI PLGKLSDIDK IGTQTEIFPF LGGSGPYYSF PGDYGISRDL
     PESCEMKQVQ MVGRHGERYP TVSKAKSIMT TWYKLSNYTG QFSGALSFLN DDYEFFIRDT
     KNLEMETTLA NSVNVLNPYT GEMNAKRHAR DFLAQYGYMV ENQTSFAVFT SNSNRCHDTA
     QYFIDGLGDK FNISLQTISE AESAGANTLS AHHSCPAWDD DVNDDILKKY DTKYLSGIAK
     RLNKENKGLN LTSSDANTFF AWCAYEINAR GYSDICNIFT KDELVRFSYG QDLETYYQTG
     PGYDVVRSVG ANLFNASVKL LKESEVQDQK VWLSFTHDTD ILNYLTTIGI IDDKNNLTAE
     HVPFMENTFH RSWYVPQGAR VYTEKFQCSN DTYVRYVIND AVVPIETCST GPGFSCEIND
     FYDYAEKRVA GTDFLKVCNV SSVSNSTELT FFWDWNTKHY NDTLLKQ
 
 
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