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Protein

Polyphosphoinositide phosphatase

Gene

FIG4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Mg2+1 Publication

GO - Molecular functioni

  • phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity Source: SGD

GO - Biological processi

  • phosphatidylinositol-3-phosphate biosynthetic process Source: GOC
  • phosphatidylinositol dephosphorylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15183.
YEAST:G3O-33309-MONOMER.
YEAST:MONOMER3O-86.
ReactomeiREACT_275163. Synthesis of PIPs at the early endosome membrane.
REACT_282840. Synthesis of PIPs at the late endosome membrane.
REACT_318087. Synthesis of PIPs at the Golgi 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 Componenti: Chromosome XIV

Organism-specific databases

CYGDiYNL325c.
EuPathDBiFungiDB:YNL325C.
SGDiS000005269. FIG4.

Subcellular locationi

GO - Cellular componenti

  • extrinsic component of membrane Source: SGD
  • fungal-type vacuole membrane Source: SGD
  • nuclear periphery Source: SGD
  • PAS complex Source: SGD
Complete GO annotation...

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.

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.
InParanoidiP42837.
OMAiPIYCIDE.
OrthoDBiEOG7DRJBN.

Family and domain databases

InterProiIPR002013. SAC_dom.
[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

        10         20         30         40         50
MNNDAMEHTL GGGILTTSGS KQRKTSKFVM GKYTLYETKD RMYIVGSNKR
60 70 80 90 100
ETMFRILEID LTVPRGELTV LEDNVFFTRN EIMNVLASLE EATEDGLHKK
110 120 130 140 150
ITGYGLLGFI KFTCWYYLIM VTKYSQVAVI GGHGIYHIDG IDIIPITNNY
160 170 180 190 200
KKPEKSSDEA RLLNIFKDLD LTKTFYFSYT YDITNTLQTN ILREKLKAVD
210 220 230 240 250
RCDITIPCGI TDYNEMFVWN NNLLSPIFAC IDTVFDWFQC IIHGFIDQVN
260 270 280 290 300
VSVLGKSIYI TLIARRSHHF AGARFLKRGV NNKGHVANEV ETEQIVTDMI
310 320 330 340 350
LTPFHQPGNG FFDSDRYTSF VQHRGSIPLY WTQDASNLTT KPPIRINVVD
360 370 380 390 400
PFFSPAALHF DNLFQRYGGG TIQILNLIKT KEKTPRETKL LWEFEQCIDY
410 420 430 440 450
LNEFLPTLKK LDYTSWDMSR ASKQDGQGVI EFLEKYAVNT VTTTGIFHNG
460 470 480 490 500
PDFASTKIQE GICRSNCIDC LDRTNAAQFV IGKRALGCQL KSLGIIDNSY
510 520 530 540 550
LEYDSDIVNI LTELFHDLGD TIALQYGGSH LVNTMETYRK INQWSSHSRD
560 570 580 590 600
MIESIKRFYS NSFVDAQRQD AINLFLGHYS WREGFPSLWE MNTDFYLHNA
610 620 630 640 650
YSLNMPKRSY IHWWNDYNIK SVKELINEEL IATGNDVTRE KIIKNVRGYP
660 670 680 690 700
GAFDNYWNEY YLPRSVTWIR DLFAYNMNST RRYHNALSKQ DKAMSPFTSR
710 720 730 740 750
KQSWLNNKLK MITSSKSLEK AEGRVVETTD LDRDTSPKQE LELYEHYLHI
760 770 780 790 800
ISDRSQKLEE KMNSFSYSKY PIFISHESSE IPPMRKVIGE PLVDIAEDFT
810 820 830 840 850
DVYDDDDDGD DENDEMTTEA LLIAPDHVSV DEKFYEKVLN VDDYKPALDD
860 870
YSAVIHIKPD NLQLYRDLCF SKDIQLDFQ
Length:879
Mass (Da):101,746
Last modified:November 1, 1995 - v1
Checksum:i872B3231104185FA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

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

Proteomic databases

MaxQBiP42837.
PaxDbiP42837.
PRIDEiP42837.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CYGDiYNL325c.
EuPathDBiFungiDB:YNL325C.
SGDiS000005269. FIG4.

Phylogenomic databases

eggNOGiCOG5329.
GeneTreeiENSGT00550000074943.
HOGENOMiHOG000168063.
InParanoidiP42837.
OMAiPIYCIDE.
OrthoDBiEOG7DRJBN.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15183.
YEAST:G3O-33309-MONOMER.
YEAST:MONOMER3O-86.
ReactomeiREACT_275163. Synthesis of PIPs at the early endosome membrane.
REACT_282840. Synthesis of PIPs at the late endosome membrane.
REACT_318087. Synthesis of PIPs at the Golgi membrane.

Miscellaneous databases

NextBioi979202.
PROiP42837.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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: June 24, 2015
This is version 116 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.