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Repressible alkaline phosphatase (EC 3.1.3.1) (Fructose-2,6-bisphosphate 6-phosphatase) (EC 3.1.3.54) (Membrane-bound repressible alkaline phosphatase) [Cleaved into: Soluble alkaline phosphatase (EC 3.1.7.6) (Farnesyl diphosphatase)]

 PPB_YEAST               Reviewed;         566 AA.
P11491; D6VTA4; E9P949; Q03374;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
15-JUL-1998, sequence version 2.
30-AUG-2017, entry version 165.
RecName: Full=Repressible alkaline phosphatase;
EC=3.1.3.1;
AltName: Full=Fructose-2,6-bisphosphate 6-phosphatase;
EC=3.1.3.54;
AltName: Full=Membrane-bound repressible alkaline phosphatase;
Contains:
RecName: Full=Soluble alkaline phosphatase;
EC=3.1.7.6;
AltName: Full=Farnesyl diphosphatase;
Flags: Precursor;
Name=PHO8; OrderedLocusNames=YDR481C; ORFNames=D8035.24;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=P-28-24C;
PubMed=3319783; DOI=10.1016/0378-1119(87)90036-9;
Kaneko Y., Hayashi N., Toh-e A., Banno I., Oshima Y.;
"Structural characteristics of the PHO8 gene encoding repressible
alkaline phosphatase in Saccharomyces cerevisiae.";
Gene 58:137-148(1987).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867;
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[5]
PROTEIN SEQUENCE OF 1-10, TOPOLOGY, AND SUBCELLULAR LOCATION.
PubMed=2676517;
Klionsky D.J., Emr S.D.;
"Membrane protein sorting: biosynthesis, transport and processing of
yeast vacuolar alkaline phosphatase.";
EMBO J. 8:2241-2250(1989).
[6]
PROTEIN SEQUENCE OF 63-79, CATALYTIC ACTIVITY AS FARNESYL
DIPHOSPHATASE, AND PH DEPENDENCE.
PubMed=16484724; DOI=10.1385/ABAB:128:2:149;
Song L.;
"A soluble form of phosphatase in Saccharomyces cerevisiae capable of
converting farnesyl diphosphate into E,E-farnesol.";
Appl. Biochem. Biotechnol. 128:149-158(2006).
[7]
FUNCTION.
PubMed=1848184; DOI=10.1111/j.1432-1033.1991.tb15803.x;
Plankert U., Purwin C., Holzer H.;
"Yeast fructose-2,6-bisphosphate 6-phosphatase is encoded by PHO8, the
gene for nonspecific repressible alkaline phosphatase.";
Eur. J. Biochem. 196:191-196(1991).
[8]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
-!- FUNCTION: Phosphatase with broad substrate specificity. A
truncated (soluble) version of the protein is responsible for the
production of (E,E)-farnesol from (E,E)-farnesyl diphosphate. Acts
as a fructose-2,6-bisphosphate 6-phosphatase (PubMed:1848184).
{ECO:0000269|PubMed:1848184}.
-!- CATALYTIC ACTIVITY: A phosphate monoester + H(2)O = an alcohol +
phosphate. {ECO:0000255|PROSITE-ProRule:PRU10042,
ECO:0000269|PubMed:16484724}.
-!- CATALYTIC ACTIVITY: (2E,6E)-farnesyl diphosphate + H(2)O =
(2E,6E)-farnesol + diphosphate. {ECO:0000269|PubMed:16484724}.
-!- CATALYTIC ACTIVITY: Beta-D-fructose 2,6-bisphosphate + H(2)O =
beta-D-fructofuranose 2-phosphate + phosphate.
{ECO:0000269|PubMed:16484724}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Binds 1 Mg(2+) ion. {ECO:0000250};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 2 Zn(2+) ions. {ECO:0000250};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 7.0 for farnesyl diphosphatase activity.
{ECO:0000269|PubMed:16484724};
-!- SUBCELLULAR LOCATION: Repressible alkaline phosphatase: Vacuole
membrane; Single-pass membrane protein. Note=The full-length
version is found in lysosome-like vacuoles.
-!- SUBCELLULAR LOCATION: Soluble alkaline phosphatase: Cytoplasm.
Note=The truncated version of the protein is soluble.
-!- MISCELLANEOUS: Present with 3060 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the alkaline phosphatase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M21134; AAA34871.1; -; Genomic_DNA.
EMBL; U33050; AAB64930.1; -; Genomic_DNA.
EMBL; AY723794; AAU09711.1; -; Genomic_DNA.
EMBL; BK006938; DAA12314.1; -; Genomic_DNA.
PIR; S69648; S69648.
RefSeq; NP_010769.3; NM_001180789.3.
ProteinModelPortal; P11491; -.
SMR; P11491; -.
BioGrid; 32533; 51.
IntAct; P11491; 2.
MINT; MINT-4482897; -.
STRING; 4932.YDR481C; -.
iPTMnet; P11491; -.
MaxQB; P11491; -.
PRIDE; P11491; -.
EnsemblFungi; YDR481C; YDR481C; YDR481C.
GeneID; 852092; -.
KEGG; sce:YDR481C; -.
EuPathDB; FungiDB:YDR481C; -.
SGD; S000002889; PHO8.
GeneTree; ENSGT00390000008704; -.
HOGENOM; HOG000099116; -.
InParanoid; P11491; -.
KO; K01077; -.
OMA; LKSYNGA; -.
OrthoDB; EOG092C1UXR; -.
BioCyc; MetaCyc:YDR481C-MONOMER; -.
BioCyc; YEAST:YDR481C-MONOMER; -.
Reactome; R-SCE-1483166; Synthesis of PA.
Reactome; R-SCE-163125; Post-translational modification: synthesis of GPI-anchored proteins.
Reactome; R-SCE-8935690; Digestion.
PRO; PR:P11491; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0004035; F:alkaline phosphatase activity; IDA:SGD.
GO; GO:0047386; F:fructose-2,6-bisphosphate 6-phosphatase activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0046496; P:nicotinamide nucleotide metabolic process; IMP:SGD.
GO; GO:0006470; P:protein dephosphorylation; IDA:SGD.
CDD; cd16012; ALP; 1.
Gene3D; 3.40.720.10; -; 1.
InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
InterPro; IPR001952; Alkaline_phosphatase.
InterPro; IPR018299; Alkaline_phosphatase_AS.
InterPro; IPR017850; Alkaline_phosphatase_core.
PANTHER; PTHR11596; PTHR11596; 1.
Pfam; PF00245; Alk_phosphatase; 1.
PRINTS; PR00113; ALKPHPHTASE.
SMART; SM00098; alkPPc; 1.
SUPFAM; SSF53649; SSF53649; 2.
PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Direct protein sequencing; Glycoprotein;
Hydrolase; Magnesium; Membrane; Metal-binding; Phosphoprotein;
Reference proteome; Transmembrane; Transmembrane helix; Vacuole; Zinc.
CHAIN 1 ? Repressible alkaline phosphatase.
/FTId=PRO_0000024017.
CHAIN 63 ? Soluble alkaline phosphatase.
/FTId=PRO_0000401198.
PROPEP ? 566 Removed in mature form.
/FTId=PRO_0000024018.
TOPO_DOM 1 33 Cytoplasmic.
{ECO:0000269|PubMed:2676517}.
TRANSMEM 34 59 Helical. {ECO:0000255}.
TOPO_DOM 60 ? Vacuolar. {ECO:0000269|PubMed:2676517}.
ACT_SITE 123 123 Phosphoserine intermediate.
{ECO:0000255|PROSITE-ProRule:PRU10042}.
METAL 75 75 Magnesium. {ECO:0000250}.
METAL 75 75 Zinc 2. {ECO:0000250}.
METAL 174 174 Magnesium. {ECO:0000250}.
METAL 176 176 Magnesium. {ECO:0000250}.
METAL 325 325 Magnesium. {ECO:0000250}.
METAL 330 330 Zinc 1. {ECO:0000250}.
METAL 334 334 Zinc 1. {ECO:0000250}.
METAL 373 373 Zinc 2. {ECO:0000250}.
METAL 374 374 Zinc 2. {ECO:0000250}.
METAL 484 484 Zinc 1. {ECO:0000250}.
MOD_RES 123 123 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
CARBOHYD 268 268 N-linked (GlcNAc...) asparagine.
CARBOHYD 401 401 N-linked (GlcNAc...) asparagine.
CONFLICT 5 5 T -> R (in Ref. 1; AAA34871).
{ECO:0000305}.
CONFLICT 55 55 S -> T (in Ref. 1; AAA34871).
{ECO:0000305}.
CONFLICT 59 59 L -> I (in Ref. 1; AAA34871).
{ECO:0000305}.
CONFLICT 132 132 C -> S (in Ref. 1; AAA34871).
{ECO:0000305}.
CONFLICT 271 271 L -> F (in Ref. 1; AAA34871).
{ECO:0000305}.
CONFLICT 328 328 R -> G (in Ref. 4; AAU09711).
{ECO:0000305}.
CONFLICT 447 447 D -> E (in Ref. 1; AAA34871).
{ECO:0000305}.
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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