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}.
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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
//
