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P11491

- PPB_YEAST

UniProt

P11491 - PPB_YEAST

Protein

Repressible alkaline phosphatase

Gene

PHO8

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 2 (15 Jul 1998)
      Previous versions | rss
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    Functioni

    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).1 Publication

    Catalytic activityi

    A phosphate monoester + H2O = an alcohol + phosphate.1 PublicationPROSITE-ProRule annotation
    (2E,6E)-farnesyl diphosphate + H2O = (2E,6E)-farnesol + diphosphate.1 Publication
    Beta-D-fructose 2,6-bisphosphate + H2O = beta-D-fructofuranose 2-phosphate + phosphate.1 Publication

    Cofactori

    Binds 1 magnesium ion.By similarity
    Binds 2 zinc ions.By similarity

    pH dependencei

    Optimum pH is 7.0 for farnesyl diphosphatase activity.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi75 – 751MagnesiumBy similarity
    Metal bindingi75 – 751Zinc 2By similarity
    Active sitei123 – 1231Phosphoserine intermediatePROSITE-ProRule annotation
    Metal bindingi174 – 1741MagnesiumBy similarity
    Metal bindingi176 – 1761MagnesiumBy similarity
    Metal bindingi325 – 3251MagnesiumBy similarity
    Metal bindingi330 – 3301Zinc 1By similarity
    Metal bindingi334 – 3341Zinc 1By similarity
    Metal bindingi373 – 3731Zinc 2By similarity
    Metal bindingi374 – 3741Zinc 2By similarity
    Metal bindingi484 – 4841Zinc 1By similarity

    GO - Molecular functioni

    1. alkaline phosphatase activity Source: SGD
    2. fructose-2,6-bisphosphate 6-phosphatase activity Source: UniProtKB
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. nicotinamide nucleotide metabolic process Source: SGD
    2. protein dephosphorylation Source: SGD

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Magnesium, Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-16788.
    YEAST:YDR481C-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Repressible alkaline phosphatase (EC:3.1.3.1)
    Alternative name(s):
    Fructose-2,6-bisphosphate 6-phosphatase (EC:3.1.3.54)
    Membrane-bound repressible alkaline phosphatase
    Cleaved into the following chain:
    Alternative name(s):
    Farnesyl diphosphatase
    Gene namesi
    Name:PHO8
    Ordered Locus Names:YDR481C
    ORF Names:D8035.24
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDR481c.
    SGDiS000002889. PHO8.

    Subcellular locationi

    Chain Repressible alkaline phosphatase : Vacuole membrane; Single-pass membrane protein
    Note: The full-length version is found in lysosome-like vacuoles.
    Chain Soluble alkaline phosphatase : Cytoplasm
    Note: The truncated version of the protein is soluble.

    GO - Cellular componenti

    1. fungal-type vacuole membrane Source: SGD
    2. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Vacuole

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei? – 566Removed in mature formPRO_0000024018
    Chaini1 – ?Repressible alkaline phosphatasePRO_0000024017
    Chaini63 – ?Soluble alkaline phosphatasePRO_0000401198

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei123 – 1231Phosphoserine3 Publications
    Glycosylationi268 – 2681N-linked (GlcNAc...)
    Glycosylationi401 – 4011N-linked (GlcNAc...)

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP11491.
    PaxDbiP11491.
    PeptideAtlasiP11491.

    Expressioni

    Gene expression databases

    GenevestigatoriP11491.

    Interactioni

    Protein-protein interaction databases

    BioGridi32533. 21 interactions.
    IntActiP11491. 2 interactions.
    MINTiMINT-4482897.

    Structurei

    3D structure databases

    ProteinModelPortaliP11491.
    SMRiP11491. Positions 67-525.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 3333Cytoplasmic1 PublicationAdd
    BLAST
    Topological domaini60 – ?Vacuolar1 Publication

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei34 – 5926HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the alkaline phosphatase family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1785.
    GeneTreeiENSGT00390000008704.
    HOGENOMiHOG000099116.
    KOiK01077.
    OMAiLKSYNGA.
    OrthoDBiEOG71K6C1.

    Family and domain databases

    Gene3Di3.40.720.10. 1 hit.
    InterProiIPR017849. Alkaline_Pase-like_a/b/a.
    IPR001952. Alkaline_phosphatase.
    IPR018299. Alkaline_phosphatase_AS.
    IPR017850. Alkaline_phosphatase_core.
    [Graphical view]
    PfamiPF00245. Alk_phosphatase. 1 hit.
    [Graphical view]
    PRINTSiPR00113. ALKPHPHTASE.
    SMARTiSM00098. alkPPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF53649. SSF53649. 2 hits.
    PROSITEiPS00123. ALKALINE_PHOSPHATASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P11491-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMTHTLPSEQ TRLVPGSDSS SRPKKRRISK RSKIIVSTVV CIGLLLVLVQ    50
    LAFPSSFALR SASHKKKNVI FFVTDGMGPA SLSMARSFNQ HVNDLPIDDI 100
    LTLDEHFIGS SRTRSSDSLV TDSAAGATAF ACALKSYNGA IGVDPHHRPC 150
    GTVLEAAKLA GYLTGLVVTT RITDATPASF SSHVDYRWQE DLIATHQLGE 200
    YPLGRVVDLL MGGGRSHFYP QGEKASPYGH HGARKDGRDL IDEAQSNGWQ 250
    YVGDRKNFDS LLKSHGENVT LPFLGLFADN DIPFEIDRDE KEYPSLKEQV 300
    KVALGALEKA SNEDKDSNGF FLMVEGSRID HAGHQNDPAS QVREVLAFDE 350
    AFQYVLEFAE NSDTETVLVS TSDHETGGLV TSRQVTASYP QYVWYPQVLA 400
    NATHSGEFLK RKLVDFVHEH KGASSKIENF IKHEILEKDL GIYDYTDSDL 450
    ETLIHLDDNA NAIQDKLNDM VSFRAQIGWT THGHSAVDVN IYAYANKKAT 500
    WSYVLNNLQG NHENTEVGQF LENFLELNLN EVTDLIRDTK HTSDFDATEI 550
    ASEVQHYDEY YHELTN 566
    Length:566
    Mass (Da):63,004
    Last modified:July 15, 1998 - v2
    Checksum:i9FA2E87B068FF0DB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti5 – 51T → R in AAA34871. (PubMed:3319783)Curated
    Sequence conflicti55 – 551S → T in AAA34871. (PubMed:3319783)Curated
    Sequence conflicti59 – 591L → I in AAA34871. (PubMed:3319783)Curated
    Sequence conflicti132 – 1321C → S in AAA34871. (PubMed:3319783)Curated
    Sequence conflicti271 – 2711L → F in AAA34871. (PubMed:3319783)Curated
    Sequence conflicti328 – 3281R → G in AAU09711. (PubMed:17322287)Curated
    Sequence conflicti447 – 4471D → E in AAA34871. (PubMed:3319783)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M21134 Genomic DNA. Translation: AAA34871.1.
    U33050 Genomic DNA. Translation: AAB64930.1.
    AY723794 Genomic DNA. Translation: AAU09711.1.
    BK006938 Genomic DNA. Translation: DAA12314.1.
    PIRiS69648.
    RefSeqiNP_010769.3. NM_001180789.3.

    Genome annotation databases

    EnsemblFungiiYDR481C; YDR481C; YDR481C.
    GeneIDi852092.
    KEGGisce:YDR481C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M21134 Genomic DNA. Translation: AAA34871.1 .
    U33050 Genomic DNA. Translation: AAB64930.1 .
    AY723794 Genomic DNA. Translation: AAU09711.1 .
    BK006938 Genomic DNA. Translation: DAA12314.1 .
    PIRi S69648.
    RefSeqi NP_010769.3. NM_001180789.3.

    3D structure databases

    ProteinModelPortali P11491.
    SMRi P11491. Positions 67-525.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32533. 21 interactions.
    IntActi P11491. 2 interactions.
    MINTi MINT-4482897.

    Proteomic databases

    MaxQBi P11491.
    PaxDbi P11491.
    PeptideAtlasi P11491.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDR481C ; YDR481C ; YDR481C .
    GeneIDi 852092.
    KEGGi sce:YDR481C.

    Organism-specific databases

    CYGDi YDR481c.
    SGDi S000002889. PHO8.

    Phylogenomic databases

    eggNOGi COG1785.
    GeneTreei ENSGT00390000008704.
    HOGENOMi HOG000099116.
    KOi K01077.
    OMAi LKSYNGA.
    OrthoDBi EOG71K6C1.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-16788.
    YEAST:YDR481C-MONOMER.

    Miscellaneous databases

    NextBioi 970421.

    Gene expression databases

    Genevestigatori P11491.

    Family and domain databases

    Gene3Di 3.40.720.10. 1 hit.
    InterProi IPR017849. Alkaline_Pase-like_a/b/a.
    IPR001952. Alkaline_phosphatase.
    IPR018299. Alkaline_phosphatase_AS.
    IPR017850. Alkaline_phosphatase_core.
    [Graphical view ]
    Pfami PF00245. Alk_phosphatase. 1 hit.
    [Graphical view ]
    PRINTSi PR00113. ALKPHPHTASE.
    SMARTi SM00098. alkPPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53649. SSF53649. 2 hits.
    PROSITEi PS00123. ALKALINE_PHOSPHATASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structural characteristics of the PHO8 gene encoding repressible alkaline phosphatase in Saccharomyces cerevisiae."
      Kaneko Y., Hayashi N., Toh-e A., Banno I., Oshima Y.
      Gene 58:137-148(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: P-28-24C.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      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.
      Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. "Membrane protein sorting: biosynthesis, transport and processing of yeast vacuolar alkaline phosphatase."
      Klionsky D.J., Emr S.D.
      EMBO J. 8:2241-2250(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-10, TOPOLOGY, SUBCELLULAR LOCATION.
    6. "A soluble form of phosphatase in Saccharomyces cerevisiae capable of converting farnesyl diphosphate into E,E-farnesol."
      Song L.
      Appl. Biochem. Biotechnol. 128:149-158(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 63-79, CATALYTIC ACTIVITY AS FARNESYL DIPHOSPHATASE, PH DEPENDENCE.
    7. "Yeast fructose-2,6-bisphosphate 6-phosphatase is encoded by PHO8, the gene for nonspecific repressible alkaline phosphatase."
      Plankert U., Purwin C., Holzer H.
      Eur. J. Biochem. 196:191-196(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    9. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    10. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPPB_YEAST
    AccessioniPrimary (citable) accession number: P11491
    Secondary accession number(s): D6VTA4, E9P949, Q03374
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: July 15, 1998
    Last modified: October 1, 2014
    This is version 139 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 3060 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    External Data

    Dasty 3