ID PPAC_YEAST Reviewed; 467 AA. AC P38693; D3DLH0; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 27-MAR-2024, entry version 161. DE RecName: Full=Acid phosphatase PHO12; DE EC=3.1.3.2; DE Flags: Precursor; GN Name=PHO12; OrderedLocusNames=YHR215W; 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 [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=8091229; DOI=10.1126/science.8091229; RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J., RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., RA Waterston R., Wilson R., Vaudin M.; RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome RT VIII."; RL Science 265:2077-2082(1994). RN [2] 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 [3] 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 3290 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; U00029; AAB69729.1; -; Genomic_DNA. DR EMBL; BK006934; DAA06914.1; -; Genomic_DNA. DR PIR; S48996; S48996. DR RefSeq; NP_012087.1; NM_001179346.1. DR AlphaFoldDB; P38693; -. DR SMR; P38693; -. DR BioGRID; 36650; 26. DR DIP; DIP-1325N; -. DR IntAct; P38693; 2. DR MINT; P38693; -. DR STRING; 4932.YHR215W; -. DR GlyCosmos; P38693; 10 sites, No reported glycans. DR GlyGen; P38693; 10 sites. DR MaxQB; P38693; -. DR PaxDb; 4932-YHR215W; -. DR PeptideAtlas; P38693; -. DR EnsemblFungi; YHR215W_mRNA; YHR215W; YHR215W. DR GeneID; 856625; -. DR KEGG; sce:YHR215W; -. DR AGR; SGD:S000001258; -. DR SGD; S000001258; PHO12. DR VEuPathDB; FungiDB:YHR215W; -. DR eggNOG; KOG1382; Eukaryota. DR GeneTree; ENSGT00390000018409; -. DR HOGENOM; CLU_020880_3_1_1; -. DR InParanoid; P38693; -. DR OMA; LWINDGW; -. DR OrthoDB; 2404758at2759; -. DR BioCyc; YEAST:YHR215W-MONOMER; -. DR BioGRID-ORCS; 856625; 0 hits in 10 CRISPR screens. DR PRO; PR:P38693; -. DR Proteomes; UP000002311; Chromosome VIII. DR RNAct; P38693; Protein. DR GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central. DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD. DR GO; GO:0003993; F:acid phosphatase activity; 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:0000250" FT CHAIN 18..467 FT /note="Acid phosphatase PHO12" FT /id="PRO_0000023957" 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" SQ SEQUENCE 467 AA; 52700 MW; BEC606CDF39B845B 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 IDDQNNLTAE HVPFMENTFH RSWYVPQGAR VYTEKFQCSN DTYVRYVIND AVVPIETCST GPGFSCEIND FYGYAEKRVA GTDFLKVCNV SSVSNSTELT FFWDWNTKHY NDTLLKQ //