ID PPB_YEAST Reviewed; 566 AA. AC P11491; D6VTA4; E9P949; Q03374; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 27-MAR-2024, entry version 206. DE RecName: Full=Repressible alkaline phosphatase; DE EC=3.1.3.1 {ECO:0000269|PubMed:16484724}; DE AltName: Full=Fructose-2,6-bisphosphate 6-phosphatase; DE EC=3.1.3.54 {ECO:0000269|PubMed:1848184}; DE AltName: Full=Membrane-bound repressible alkaline phosphatase; DE Contains: DE RecName: Full=Soluble alkaline phosphatase; DE EC=3.1.7.6 {ECO:0000269|PubMed:16484724}; DE AltName: Full=Farnesyl diphosphatase; DE Flags: Precursor; GN Name=PHO8; OrderedLocusNames=YDR481C; ORFNames=D8035.24; 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]. RC STRAIN=P-28-24C; RX PubMed=3319783; DOI=10.1016/0378-1119(87)90036-9; RA Kaneko Y., Hayashi N., Toh-e A., Banno I., Oshima Y.; RT "Structural characteristics of the PHO8 gene encoding repressible alkaline RT phosphatase in Saccharomyces cerevisiae."; RL Gene 58:137-148(1987). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169867; RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., RA Mewes H.-W., Zollner A., Zaccaria P.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."; RL Nature 387:75-78(1997). RN [3] 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 [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., RA LaBaer J.; RT "Approaching a complete repository of sequence-verified protein-encoding RT clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [5] RP PROTEIN SEQUENCE OF 1-10, TOPOLOGY, AND SUBCELLULAR LOCATION. RX PubMed=2676517; DOI=10.1002/j.1460-2075.1989.tb08348.x; RA Klionsky D.J., Emr S.D.; RT "Membrane protein sorting: biosynthesis, transport and processing of yeast RT vacuolar alkaline phosphatase."; RL EMBO J. 8:2241-2250(1989). RN [6] RP PROTEIN SEQUENCE OF 63-79, CATALYTIC ACTIVITY AS FARNESYL DIPHOSPHATASE, RP AND PH DEPENDENCE. RX PubMed=16484724; DOI=10.1385/abab:128:2:149; RA Song L.; RT "A soluble form of phosphatase in Saccharomyces cerevisiae capable of RT converting farnesyl diphosphate into E,E-farnesol."; RL Appl. Biochem. Biotechnol. 128:149-158(2006). RN [7] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=1848184; DOI=10.1111/j.1432-1033.1991.tb15803.x; RA Plankert U., Purwin C., Holzer H.; RT "Yeast fructose-2,6-bisphosphate 6-phosphatase is encoded by PHO8, the gene RT for nonspecific repressible alkaline phosphatase."; RL Eur. J. Biochem. 196:191-196(1991). RN [8] 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=ADR376; RX PubMed=17330950; DOI=10.1021/pr060559j; RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., RA Elias J.E., Gygi S.P.; RT "Large-scale phosphorylation analysis of alpha-factor-arrested RT Saccharomyces cerevisiae."; RL J. Proteome Res. 6:1190-1197(2007). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth phosphoproteome RT analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19779198; DOI=10.1126/science.1172867; RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.; RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights RT into evolution."; RL Science 325:1682-1686(2009). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). CC -!- FUNCTION: Phosphatase with broad substrate specificity. A truncated CC (soluble) version of the protein is responsible for the production of CC (E,E)-farnesol from (E,E)-farnesyl diphosphate. Acts as a fructose-2,6- CC bisphosphate 6-phosphatase (PubMed:1848184). CC {ECO:0000269|PubMed:1848184}. 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=3.1.3.1; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10042, CC ECO:0000269|PubMed:16484724}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E,6E)-farnesyl diphosphate + H2O = (2E,6E)-farnesol + CC diphosphate; Xref=Rhea:RHEA:27526, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:16619, ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=3.1.7.6; CC Evidence={ECO:0000269|PubMed:16484724}; CC -!- CATALYTIC ACTIVITY: CC Reaction=beta-D-fructose 2,6-bisphosphate + H2O = beta-D-fructose 2- CC phosphate + phosphate; Xref=Rhea:RHEA:13333, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57267, ChEBI:CHEBI:58579; EC=3.1.3.54; CC Evidence={ECO:0000269|PubMed:1848184}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 1 Mg(2+) ion. {ECO:0000250}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 2 Zn(2+) ions. {ECO:0000250}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 7.0 for farnesyl diphosphatase activity. CC {ECO:0000269|PubMed:16484724}; CC -!- SUBCELLULAR LOCATION: [Repressible alkaline phosphatase]: Vacuole CC membrane; Single-pass membrane protein. Note=The full-length version is CC found in lysosome-like vacuoles. CC -!- SUBCELLULAR LOCATION: [Soluble alkaline phosphatase]: Cytoplasm. CC Note=The truncated version of the protein is soluble. CC -!- MISCELLANEOUS: Present with 3060 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the alkaline phosphatase family. {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; M21134; AAA34871.1; -; Genomic_DNA. DR EMBL; U33050; AAB64930.1; -; Genomic_DNA. DR EMBL; AY723794; AAU09711.1; -; Genomic_DNA. DR EMBL; BK006938; DAA12314.1; -; Genomic_DNA. DR PIR; S69648; S69648. DR RefSeq; NP_010769.3; NM_001180789.3. DR AlphaFoldDB; P11491; -. DR SMR; P11491; -. DR BioGRID; 32533; 113. DR IntAct; P11491; 2. DR MINT; P11491; -. DR STRING; 4932.YDR481C; -. DR GlyCosmos; P11491; 2 sites, No reported glycans. DR GlyGen; P11491; 2 sites. DR iPTMnet; P11491; -. DR MaxQB; P11491; -. DR PaxDb; 4932-YDR481C; -. DR PeptideAtlas; P11491; -. DR EnsemblFungi; YDR481C_mRNA; YDR481C; YDR481C. DR GeneID; 852092; -. DR KEGG; sce:YDR481C; -. DR AGR; SGD:S000002889; -. DR SGD; S000002889; PHO8. DR VEuPathDB; FungiDB:YDR481C; -. DR eggNOG; KOG4126; Eukaryota. DR GeneTree; ENSGT00950000183063; -. DR HOGENOM; CLU_008539_6_0_1; -. DR InParanoid; P11491; -. DR OMA; HAGHQND; -. DR OrthoDB; 35876at2759; -. DR BioCyc; MetaCyc:YDR481C-MONOMER; -. DR BioCyc; YEAST:YDR481C-MONOMER; -. DR BioGRID-ORCS; 852092; 1 hit in 10 CRISPR screens. DR PRO; PR:P11491; -. DR Proteomes; UP000002311; Chromosome IV. DR RNAct; P11491; Protein. DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD. DR GO; GO:0004035; F:alkaline phosphatase activity; IDA:SGD. DR GO; GO:0047386; F:fructose-2,6-bisphosphate 6-phosphatase activity; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016311; P:dephosphorylation; IBA:GO_Central. DR GO; GO:0046496; P:nicotinamide nucleotide metabolic process; IMP:SGD. DR CDD; cd16012; ALP; 1. DR Gene3D; 1.10.60.40; -; 1. DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1. DR InterPro; IPR001952; Alkaline_phosphatase. DR InterPro; IPR018299; Alkaline_phosphatase_AS. DR InterPro; IPR017850; Alkaline_phosphatase_core_sf. DR PANTHER; PTHR11596; ALKALINE PHOSPHATASE; 1. DR PANTHER; PTHR11596:SF5; ALKALINE PHOSPHATASE; 1. DR Pfam; PF00245; Alk_phosphatase; 1. DR PRINTS; PR00113; ALKPHPHTASE. DR SMART; SM00098; alkPPc; 1. DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1. DR PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1. PE 1: Evidence at protein level; KW Cytoplasm; Direct protein sequencing; Glycoprotein; Hydrolase; Magnesium; KW Membrane; Metal-binding; Phosphoprotein; Reference proteome; Transmembrane; KW Transmembrane helix; Vacuole; Zinc. FT CHAIN 1..? FT /note="Repressible alkaline phosphatase" FT /id="PRO_0000024017" FT CHAIN 63..? FT /note="Soluble alkaline phosphatase" FT /id="PRO_0000401198" FT PROPEP ?..566 FT /note="Removed in mature form" FT /id="PRO_0000024018" FT TOPO_DOM 1..33 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:2676517" FT TRANSMEM 34..59 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 60..? FT /note="Vacuolar" FT /evidence="ECO:0000269|PubMed:2676517" FT REGION 1..27 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..18 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 123 FT /note="Phosphoserine intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10042" FT BINDING 75 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 75 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 174 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 176 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 325 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 330 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 334 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 373 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 374 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 484 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250" FT MOD_RES 123 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198" FT CARBOHYD 268 FT /note="N-linked (GlcNAc...) asparagine" FT CARBOHYD 401 FT /note="N-linked (GlcNAc...) asparagine" FT CONFLICT 5 FT /note="T -> R (in Ref. 1; AAA34871)" FT /evidence="ECO:0000305" FT CONFLICT 55 FT /note="S -> T (in Ref. 1; AAA34871)" FT /evidence="ECO:0000305" FT CONFLICT 59 FT /note="L -> I (in Ref. 1; AAA34871)" FT /evidence="ECO:0000305" FT CONFLICT 132 FT /note="C -> S (in Ref. 1; AAA34871)" FT /evidence="ECO:0000305" FT CONFLICT 271 FT /note="L -> F (in Ref. 1; AAA34871)" FT /evidence="ECO:0000305" FT CONFLICT 328 FT /note="R -> G (in Ref. 4; AAU09711)" FT /evidence="ECO:0000305" FT CONFLICT 447 FT /note="D -> E (in Ref. 1; AAA34871)" FT /evidence="ECO:0000305" SQ SEQUENCE 566 AA; 63004 MW; 9FA2E87B068FF0DB CRC64; MMTHTLPSEQ TRLVPGSDSS SRPKKRRISK RSKIIVSTVV CIGLLLVLVQ LAFPSSFALR SASHKKKNVI FFVTDGMGPA SLSMARSFNQ HVNDLPIDDI LTLDEHFIGS SRTRSSDSLV TDSAAGATAF ACALKSYNGA IGVDPHHRPC GTVLEAAKLA GYLTGLVVTT RITDATPASF SSHVDYRWQE DLIATHQLGE YPLGRVVDLL MGGGRSHFYP QGEKASPYGH HGARKDGRDL IDEAQSNGWQ YVGDRKNFDS LLKSHGENVT LPFLGLFADN DIPFEIDRDE KEYPSLKEQV KVALGALEKA SNEDKDSNGF FLMVEGSRID HAGHQNDPAS QVREVLAFDE AFQYVLEFAE NSDTETVLVS TSDHETGGLV TSRQVTASYP QYVWYPQVLA NATHSGEFLK RKLVDFVHEH KGASSKIENF IKHEILEKDL GIYDYTDSDL ETLIHLDDNA NAIQDKLNDM VSFRAQIGWT THGHSAVDVN IYAYANKKAT WSYVLNNLQG NHENTEVGQF LENFLELNLN EVTDLIRDTK HTSDFDATEI ASEVQHYDEY YHELTN //