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P42837 (FIG4_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polyphosphoinositide phosphatase

EC=3.1.3.-
Alternative name(s):
Factor-induced gene 4 protein
Phosphatidylinositol 3,5-bisphosphate 5-phosphatase
Gene names
Name:FIG4
Ordered Locus Names:YNL325C
ORF Names:N0330
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length879 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.5 Ref.7 Ref.9

Catalytic activity

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

Cofactor

Magnesium. Ref.5

Subunit structure

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. Ref.9 Ref.10

Subcellular location

Vacuole membrane; Peripheral membrane protein. Note: Localized to the limiting membrane of the vacuole. Localization requires VAC14 and FAB1. Ref.1 Ref.5 Ref.9 Ref.10

Miscellaneous

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

Sequence similarities

Contains 1 SAC domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FAB1P347564EBI-28407,EBI-6754
VAC14Q067087EBI-28407,EBI-27189

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 879879Polyphosphoinositide phosphatase
PRO_0000209742

Regions

Domain166 – 528363SAC
Region761 – 879119Required for vacuolar localization

Amino acid modifications

Modified residue8291Phosphoserine Ref.11

Experimental info

Mutagenesis591I → T: Defective activation of FAB1. Ref.8
Mutagenesis4691D → N: Partially defective in both hyperosmotic shock-induced PtdIns(3,5)P2 elevation and turnover. Ref.7
Mutagenesis5191G → 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. Ref.1 Ref.5 Ref.7

Sequences

Sequence LengthMass (Da)Tools
P42837 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 872B3231104185FA

FASTA879101,746
        10         20         30         40         50         60 
MNNDAMEHTL GGGILTTSGS KQRKTSKFVM GKYTLYETKD RMYIVGSNKR ETMFRILEID 

        70         80         90        100        110        120 
LTVPRGELTV LEDNVFFTRN EIMNVLASLE EATEDGLHKK ITGYGLLGFI KFTCWYYLIM 

       130        140        150        160        170        180 
VTKYSQVAVI GGHGIYHIDG IDIIPITNNY KKPEKSSDEA RLLNIFKDLD LTKTFYFSYT 

       190        200        210        220        230        240 
YDITNTLQTN ILREKLKAVD RCDITIPCGI TDYNEMFVWN NNLLSPIFAC IDTVFDWFQC 

       250        260        270        280        290        300 
IIHGFIDQVN VSVLGKSIYI TLIARRSHHF AGARFLKRGV NNKGHVANEV ETEQIVTDMI 

       310        320        330        340        350        360 
LTPFHQPGNG FFDSDRYTSF VQHRGSIPLY WTQDASNLTT KPPIRINVVD PFFSPAALHF 

       370        380        390        400        410        420 
DNLFQRYGGG TIQILNLIKT KEKTPRETKL LWEFEQCIDY LNEFLPTLKK LDYTSWDMSR 

       430        440        450        460        470        480 
ASKQDGQGVI EFLEKYAVNT VTTTGIFHNG PDFASTKIQE GICRSNCIDC LDRTNAAQFV 

       490        500        510        520        530        540 
IGKRALGCQL KSLGIIDNSY LEYDSDIVNI LTELFHDLGD TIALQYGGSH LVNTMETYRK 

       550        560        570        580        590        600 
INQWSSHSRD MIESIKRFYS NSFVDAQRQD AINLFLGHYS WREGFPSLWE MNTDFYLHNA 

       610        620        630        640        650        660 
YSLNMPKRSY IHWWNDYNIK SVKELINEEL IATGNDVTRE KIIKNVRGYP GAFDNYWNEY 

       670        680        690        700        710        720 
YLPRSVTWIR DLFAYNMNST RRYHNALSKQ DKAMSPFTSR KQSWLNNKLK MITSSKSLEK 

       730        740        750        760        770        780 
AEGRVVETTD LDRDTSPKQE LELYEHYLHI ISDRSQKLEE KMNSFSYSKY PIFISHESSE 

       790        800        810        820        830        840 
IPPMRKVIGE PLVDIAEDFT DVYDDDDDGD DENDEMTTEA LLIAPDHVSV DEKFYEKVLN 

       850        860        870 
VDDYKPALDD YSAVIHIKPD NLQLYRDLCF SKDIQLDFQ 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z46259 Genomic DNA. Translation: CAA86373.1.
Z71601 Genomic DNA. Translation: CAA96256.1.
BK006947 Genomic DNA. Translation: DAA10238.1.
PIRS55864.
RefSeqNP_014074.1. NM_001183163.1.

3D structure databases

ProteinModelPortalP42837.
SMRP42837. Positions 106-529.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35516. 33 interactions.
IntActP42837. 3 interactions.
MINTMINT-2781314.
STRING4932.YNL325C.

Proteomic databases

PaxDbP42837.
PRIDEP42837.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYNL325C; YNL325C; YNL325C.
GeneID855392.
KEGGsce:YNL325C.

Organism-specific databases

CYGDYNL325c.
SGDS000005269. FIG4.

Phylogenomic databases

eggNOGCOG5329.
GeneTreeENSGT00550000074943.
HOGENOMHOG000168063.
OMARDFMPKN.
OrthoDBEOG7DRJBN.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-15183.
YEAST:G3O-33309-MONOMER.
YEAST:MONOMER3O-86.

Gene expression databases

GenevestigatorP42837.

Family and domain databases

InterProIPR002013. Syja_N.
[Graphical view]
PfamPF02383. Syja_N. 1 hit.
[Graphical view]
PROSITEPS50275. SAC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio979202.
PROP42837.

Entry information

Entry nameFIG4_YEAST
AccessionPrimary (citable) accession number: P42837
Secondary accession number(s): D6W0M2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIV

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

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families