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P42837

- FIG4_YEAST

UniProt

P42837 - FIG4_YEAST

Protein

Polyphosphoinositide phosphatase

Gene

FIG4

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 110 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Major enzyme required for hyperosmotic shock-induced turnover of PtdIns(3,5)P2 and requires VAC14 for this function. In vivo, mediates turnover of PtdIns(3,5)P2 at the vacuole membrane necessary for vacuolar size control. In vitro, catalyzes the removal of phosphate from the fifth hydroxyl of the myo-inositol ring of phosphatidylinositol 3,5-bisphosphate.4 Publications

    Catalytic activityi

    1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 3-phosphate + phosphate.1 Publication

    Cofactori

    Magnesium.1 Publication

    GO - Molecular functioni

    1. phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity Source: SGD
    2. protein binding Source: IntAct

    GO - Biological processi

    1. phosphatidylinositol-3-phosphate biosynthetic process Source: GOC
    2. phosphatidylinositol dephosphorylation Source: SGD

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-15183.
    YEAST:G3O-33309-MONOMER.
    YEAST:MONOMER3O-86.
    ReactomeiREACT_188955. Synthesis of PIPs at the Golgi membrane.
    REACT_188958. Synthesis of PIPs at the late endosome membrane.
    REACT_188968. Synthesis of PIPs at the early endosome membrane.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Polyphosphoinositide phosphatase (EC:3.1.3.-)
    Alternative name(s):
    Factor-induced gene 4 protein
    Phosphatidylinositol 3,5-bisphosphate 5-phosphatase
    Gene namesi
    Name:FIG4
    Ordered Locus Names:YNL325C
    ORF Names:N0330
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XIV

    Organism-specific databases

    CYGDiYNL325c.
    SGDiS000005269. FIG4.

    Subcellular locationi

    Vacuole membrane 4 Publications; Peripheral membrane protein 4 Publications
    Note: Localized to the limiting membrane of the vacuole. Localization requires VAC14 and FAB1.

    GO - Cellular componenti

    1. extrinsic component of membrane Source: SGD
    2. fungal-type vacuole membrane Source: SGD
    3. PAS complex Source: SGD

    Keywords - Cellular componenti

    Membrane, Vacuole

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi59 – 591I → T: Defective activation of FAB1. 1 Publication
    Mutagenesisi469 – 4691D → N: Partially defective in both hyperosmotic shock-induced PtdIns(3,5)P2 elevation and turnover. 1 Publication
    Mutagenesisi519 – 5191G → R in FIG4-1; loss of catalytic activity in vitro. Almost 3-fold increase in PtdIns(3,5)P2 level in vivo. Partially defective in both hyperosmotic shock-induced PtdIns(3,5)P2 elevation and turnover. 3 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 879879Polyphosphoinositide phosphatasePRO_0000209742Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei829 – 8291Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP42837.
    PaxDbiP42837.
    PRIDEiP42837.

    Expressioni

    Gene expression databases

    GenevestigatoriP42837.

    Interactioni

    Subunit structurei

    Component of the PI(3,5)P2 regulatory complex, composed of ATG18, FIG4, FAB1, VAC14 and VAC7. VAC14 nucleates the assembly of the complex and serves as a scaffold.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FAB1P347564EBI-28407,EBI-6754
    VAC14Q067087EBI-28407,EBI-27189

    Protein-protein interaction databases

    BioGridi35516. 34 interactions.
    IntActiP42837. 3 interactions.
    MINTiMINT-2781314.
    STRINGi4932.YNL325C.

    Structurei

    3D structure databases

    ProteinModelPortaliP42837.
    SMRiP42837. Positions 106-529.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini166 – 528363SACPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni761 – 879119Required for vacuolar localizationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 SAC domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5329.
    GeneTreeiENSGT00550000074943.
    HOGENOMiHOG000168063.
    OMAiDCVTMLE.
    OrthoDBiEOG7DRJBN.

    Family and domain databases

    InterProiIPR002013. Syja_N.
    [Graphical view]
    PfamiPF02383. Syja_N. 1 hit.
    [Graphical view]
    PROSITEiPS50275. SAC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P42837-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNNDAMEHTL GGGILTTSGS KQRKTSKFVM GKYTLYETKD RMYIVGSNKR    50
    ETMFRILEID LTVPRGELTV LEDNVFFTRN EIMNVLASLE EATEDGLHKK 100
    ITGYGLLGFI KFTCWYYLIM VTKYSQVAVI GGHGIYHIDG IDIIPITNNY 150
    KKPEKSSDEA RLLNIFKDLD LTKTFYFSYT YDITNTLQTN ILREKLKAVD 200
    RCDITIPCGI TDYNEMFVWN NNLLSPIFAC IDTVFDWFQC IIHGFIDQVN 250
    VSVLGKSIYI TLIARRSHHF AGARFLKRGV NNKGHVANEV ETEQIVTDMI 300
    LTPFHQPGNG FFDSDRYTSF VQHRGSIPLY WTQDASNLTT KPPIRINVVD 350
    PFFSPAALHF DNLFQRYGGG TIQILNLIKT KEKTPRETKL LWEFEQCIDY 400
    LNEFLPTLKK LDYTSWDMSR ASKQDGQGVI EFLEKYAVNT VTTTGIFHNG 450
    PDFASTKIQE GICRSNCIDC LDRTNAAQFV IGKRALGCQL KSLGIIDNSY 500
    LEYDSDIVNI LTELFHDLGD TIALQYGGSH LVNTMETYRK INQWSSHSRD 550
    MIESIKRFYS NSFVDAQRQD AINLFLGHYS WREGFPSLWE MNTDFYLHNA 600
    YSLNMPKRSY IHWWNDYNIK SVKELINEEL IATGNDVTRE KIIKNVRGYP 650
    GAFDNYWNEY YLPRSVTWIR DLFAYNMNST RRYHNALSKQ DKAMSPFTSR 700
    KQSWLNNKLK MITSSKSLEK AEGRVVETTD LDRDTSPKQE LELYEHYLHI 750
    ISDRSQKLEE KMNSFSYSKY PIFISHESSE IPPMRKVIGE PLVDIAEDFT 800
    DVYDDDDDGD DENDEMTTEA LLIAPDHVSV DEKFYEKVLN VDDYKPALDD 850
    YSAVIHIKPD NLQLYRDLCF SKDIQLDFQ 879
    Length:879
    Mass (Da):101,746
    Last modified:November 1, 1995 - v1
    Checksum:i872B3231104185FA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z46259 Genomic DNA. Translation: CAA86373.1.
    Z71601 Genomic DNA. Translation: CAA96256.1.
    BK006947 Genomic DNA. Translation: DAA10238.1.
    PIRiS55864.
    RefSeqiNP_014074.1. NM_001183163.1.

    Genome annotation databases

    EnsemblFungiiYNL325C; YNL325C; YNL325C.
    GeneIDi855392.
    KEGGisce:YNL325C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z46259 Genomic DNA. Translation: CAA86373.1 .
    Z71601 Genomic DNA. Translation: CAA96256.1 .
    BK006947 Genomic DNA. Translation: DAA10238.1 .
    PIRi S55864.
    RefSeqi NP_014074.1. NM_001183163.1.

    3D structure databases

    ProteinModelPortali P42837.
    SMRi P42837. Positions 106-529.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35516. 34 interactions.
    IntActi P42837. 3 interactions.
    MINTi MINT-2781314.
    STRINGi 4932.YNL325C.

    Proteomic databases

    MaxQBi P42837.
    PaxDbi P42837.
    PRIDEi P42837.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YNL325C ; YNL325C ; YNL325C .
    GeneIDi 855392.
    KEGGi sce:YNL325C.

    Organism-specific databases

    CYGDi YNL325c.
    SGDi S000005269. FIG4.

    Phylogenomic databases

    eggNOGi COG5329.
    GeneTreei ENSGT00550000074943.
    HOGENOMi HOG000168063.
    OMAi DCVTMLE.
    OrthoDBi EOG7DRJBN.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-15183.
    YEAST:G3O-33309-MONOMER.
    YEAST:MONOMER3O-86.
    Reactomei REACT_188955. Synthesis of PIPs at the Golgi membrane.
    REACT_188958. Synthesis of PIPs at the late endosome membrane.
    REACT_188968. Synthesis of PIPs at the early endosome membrane.

    Miscellaneous databases

    NextBioi 979202.
    PROi P42837.

    Gene expression databases

    Genevestigatori P42837.

    Family and domain databases

    InterProi IPR002013. Syja_N.
    [Graphical view ]
    Pfami PF02383. Syja_N. 1 hit.
    [Graphical view ]
    PROSITEi PS50275. SAC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Regulation of Fab1 phosphatidylinositol 3-phosphate 5-kinase pathway by Vac7 protein and Fig4, a polyphosphoinositide phosphatase family member."
      Gary J.D., Sato T.K., Stefan C.J., Bonangelino C.J., Weisman L.S., Emr S.D.
      Mol. Biol. Cell 13:1238-1251(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-519.
    2. "Sequencing analysis of a 15.4 kb fragment of yeast chromosome XIV identifies the RPD3, PAS8 and KRE1 loci, five new open reading frames."
      Maftahi M., Nicaud J.-M., Levesque H., Gaillardin C.
      Yeast 11:567-572(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: S288c / FY1676.
    3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
      Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
      , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
      Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "Vacuole size control: regulation of PtdIns(3,5)P2 levels by the vacuole-associated Vac14-Fig4 complex, a PtdIns(3,5)P2-specific phosphatase."
      Rudge S.A., Anderson D.M., Emr S.D.
      Mol. Biol. Cell 15:24-36(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH VAC14, SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-519.
    6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    7. "The Vac14p-Fig4p complex acts independently of Vac7p and couples PI3,5P2 synthesis and turnover."
      Duex J.E., Tang F., Weisman L.S.
      J. Cell Biol. 172:693-704(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF ASP-469 AND GLY-519.
    8. "Mutation of FIG4 causes neurodegeneration in the pale tremor mouse and patients with CMT4J."
      Chow C.Y., Zhang Y., Dowling J.J., Jin N., Adamska M., Shiga K., Szigeti K., Shy M.E., Li J., Zhang X., Lupski J.R., Weisman L.S., Meisler M.H.
      Nature 448:68-72(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ILE-59.
    9. "VAC14 nucleates a protein complex essential for the acute interconversion of PI3P and PI(3,5)P(2) in yeast and mouse."
      Jin N., Chow C.Y., Liu L., Zolov S.N., Bronson R., Davisson M., Petersen J.L., Zhang Y., Park S., Duex J.E., Goldowitz D., Meisler M.H., Weisman L.S.
      EMBO J. 27:3221-3234(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE PI(3,5)P2 REGULATORY COMPLEX, FUNCTION, SUBCELLULAR LOCATION.
    10. "Assembly of a Fab1 phosphoinositide kinase signaling complex requires the Fig4 phosphoinositide phosphatase."
      Botelho R.J., Efe J.A., Teis D., Emr S.D.
      Mol. Biol. Cell 19:4273-4286(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE PI(3,5)P2 REGULATORY COMPLEX, SUBCELLULAR LOCATION.
    11. "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-829, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiFIG4_YEAST
    AccessioniPrimary (citable) accession number: P42837
    Secondary accession number(s): D6W0M2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 110 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 339 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, 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 XIV
      Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

    External Data

    Dasty 3