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 27-MAR-2024, entry version 169. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 123. DR DIP; DIP-4589N; -. DR IntAct; P35842; 1. DR MINT; P35842; -. DR STRING; 4932.YAR071W; -. DR GlyCosmos; P35842; 10 sites, No reported glycans. DR GlyGen; P35842; 10 sites. DR MaxQB; P35842; -. DR PaxDb; 4932-YAR071W; -. DR PeptideAtlas; P35842; -. DR EnsemblFungi; YAR071W_mRNA; YAR071W; YAR071W. DR GeneID; 851299; -. DR KEGG; sce:YAR071W; -. DR AGR; SGD:S000000094; -. 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 OrthoDB; 2404758at2759; -. DR BioCyc; YEAST:YAR071W-MONOMER; -. 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; 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: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 //