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Database: UniProt/SWISS-PROT
Entry: PPB_YEAST
LinkDB: PPB_YEAST
Original site: PPB_YEAST 
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   20-JUN-2018, entry version 174.
DE   RecName: Full=Repressible alkaline phosphatase;
DE            EC=3.1.3.1;
DE   AltName: Full=Fructose-2,6-bisphosphate 6-phosphatase;
DE            EC=3.1.3.54;
DE   AltName: Full=Membrane-bound repressible alkaline phosphatase;
DE   Contains:
DE     RecName: Full=Soluble alkaline phosphatase;
DE              EC=3.1.7.6;
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;
OC   Saccharomycetes; 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
RT   alkaline 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.,
RA   Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
RA   Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
RA   Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
RA   Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
RA   Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
RA   Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
RA   Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
RA   Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
RA   Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
RA   Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
RA   Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
RA   Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
RA   Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
RA   Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
RA   Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
RA   Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
RA   Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
RA   Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
RA   Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
RA   Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
RA   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.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   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.,
RA   Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
RA   Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
RA   Kolodner R.D., LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-
RT   encoding 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;
RA   Klionsky D.J., Emr S.D.;
RT   "Membrane protein sorting: biosynthesis, transport and processing of
RT   yeast vacuolar alkaline phosphatase.";
RL   EMBO J. 8:2241-2250(1989).
RN   [6]
RP   PROTEIN SEQUENCE OF 63-79, CATALYTIC ACTIVITY AS FARNESYL
RP   DIPHOSPHATASE, 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.
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
RT   gene 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.,
RA   Dephoure N., 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
RP   BY 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
RP   BY 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
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123, AND IDENTIFICATION
RP   BY 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
RT   insights 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.,
RA   Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA   Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-
RT   terminal acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: Phosphatase with broad substrate specificity. A
CC       truncated (soluble) version of the protein is responsible for the
CC       production of (E,E)-farnesol from (E,E)-farnesyl diphosphate. Acts
CC       as a fructose-2,6-bisphosphate 6-phosphatase (PubMed:1848184).
CC       {ECO:0000269|PubMed:1848184}.
CC   -!- CATALYTIC ACTIVITY: A phosphate monoester + H(2)O = an alcohol +
CC       phosphate. {ECO:0000255|PROSITE-ProRule:PRU10042,
CC       ECO:0000269|PubMed:16484724}.
CC   -!- CATALYTIC ACTIVITY: (2E,6E)-farnesyl diphosphate + H(2)O =
CC       (2E,6E)-farnesol + diphosphate. {ECO:0000269|PubMed:16484724}.
CC   -!- CATALYTIC ACTIVITY: Beta-D-fructose 2,6-bisphosphate + H(2)O =
CC       beta-D-fructofuranose 2-phosphate + phosphate.
CC       {ECO:0000269|PubMed:16484724}.
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
CC       version is 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
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the alkaline phosphatase family.
CC       {ECO:0000305}.
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   ProteinModelPortal; P11491; -.
DR   SMR; P11491; -.
DR   BioGrid; 32533; 53.
DR   IntAct; P11491; 2.
DR   MINT; P11491; -.
DR   STRING; 4932.YDR481C; -.
DR   iPTMnet; P11491; -.
DR   MaxQB; P11491; -.
DR   PaxDb; P11491; -.
DR   PRIDE; P11491; -.
DR   EnsemblFungi; YDR481C; YDR481C; YDR481C.
DR   GeneID; 852092; -.
DR   KEGG; sce:YDR481C; -.
DR   EuPathDB; FungiDB:YDR481C; -.
DR   SGD; S000002889; PHO8.
DR   GeneTree; ENSGT00390000008704; -.
DR   HOGENOM; HOG000099116; -.
DR   InParanoid; P11491; -.
DR   KO; K01077; -.
DR   OMA; FEIDRRN; -.
DR   OrthoDB; EOG092C1UXR; -.
DR   BioCyc; MetaCyc:YDR481C-MONOMER; -.
DR   BioCyc; YEAST:YDR481C-MONOMER; -.
DR   Reactome; R-SCE-1483166; Synthesis of PA.
DR   Reactome; R-SCE-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR   Reactome; R-SCE-8935690; Digestion.
DR   PRO; PR:P11491; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0046496; P:nicotinamide nucleotide metabolic process; IMP:SGD.
DR   GO; GO:0006470; P:protein dephosphorylation; IDA:SGD.
DR   CDD; cd16012; ALP; 1.
DR   Gene3D; 3.40.720.10; -; 2.
DR   InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
DR   InterPro; IPR001952; Alkaline_phosphatase.
DR   InterPro; IPR018299; Alkaline_phosphatase_AS.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   PANTHER; PTHR11596; PTHR11596; 1.
DR   Pfam; PF00245; Alk_phosphatase; 1.
DR   PRINTS; PR00113; ALKPHPHTASE.
DR   SMART; SM00098; alkPPc; 1.
DR   SUPFAM; SSF53649; SSF53649; 2.
DR   PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Cytoplasm; Direct protein sequencing; Glycoprotein;
KW   Hydrolase; Magnesium; Membrane; Metal-binding; Phosphoprotein;
KW   Reference proteome; Transmembrane; Transmembrane helix; Vacuole; Zinc.
FT   CHAIN         1      ?       Repressible alkaline phosphatase.
FT                                /FTId=PRO_0000024017.
FT   CHAIN        63      ?       Soluble alkaline phosphatase.
FT                                /FTId=PRO_0000401198.
FT   PROPEP        ?    566       Removed in mature form.
FT                                /FTId=PRO_0000024018.
FT   TOPO_DOM      1     33       Cytoplasmic.
FT                                {ECO:0000269|PubMed:2676517}.
FT   TRANSMEM     34     59       Helical. {ECO:0000255}.
FT   TOPO_DOM     60      ?       Vacuolar. {ECO:0000269|PubMed:2676517}.
FT   ACT_SITE    123    123       Phosphoserine intermediate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10042}.
FT   METAL        75     75       Magnesium. {ECO:0000250}.
FT   METAL        75     75       Zinc 2. {ECO:0000250}.
FT   METAL       174    174       Magnesium. {ECO:0000250}.
FT   METAL       176    176       Magnesium. {ECO:0000250}.
FT   METAL       325    325       Magnesium. {ECO:0000250}.
FT   METAL       330    330       Zinc 1. {ECO:0000250}.
FT   METAL       334    334       Zinc 1. {ECO:0000250}.
FT   METAL       373    373       Zinc 2. {ECO:0000250}.
FT   METAL       374    374       Zinc 2. {ECO:0000250}.
FT   METAL       484    484       Zinc 1. {ECO:0000250}.
FT   MOD_RES     123    123       Phosphoserine.
FT                                {ECO:0000244|PubMed:17330950,
FT                                ECO:0000244|PubMed:18407956,
FT                                ECO:0000244|PubMed:19779198}.
FT   CARBOHYD    268    268       N-linked (GlcNAc...) asparagine.
FT   CARBOHYD    401    401       N-linked (GlcNAc...) asparagine.
FT   CONFLICT      5      5       T -> R (in Ref. 1; AAA34871).
FT                                {ECO:0000305}.
FT   CONFLICT     55     55       S -> T (in Ref. 1; AAA34871).
FT                                {ECO:0000305}.
FT   CONFLICT     59     59       L -> I (in Ref. 1; AAA34871).
FT                                {ECO:0000305}.
FT   CONFLICT    132    132       C -> S (in Ref. 1; AAA34871).
FT                                {ECO:0000305}.
FT   CONFLICT    271    271       L -> F (in Ref. 1; AAA34871).
FT                                {ECO:0000305}.
FT   CONFLICT    328    328       R -> G (in Ref. 4; AAU09711).
FT                                {ECO:0000305}.
FT   CONFLICT    447    447       D -> E (in Ref. 1; AAA34871).
FT                                {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
//
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