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Reviewed, UniProtKB/Swiss-Prot Q08227 (INP54_YEAST)

Last modified February 9, 2010. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Inositol-1,4,5-trisphosphate 5-phosphatase 4
    EC=3.1.3.36
Gene names
Name: INP54
Ordered Locus Names: YOL065C
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length384 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Regulates the phosphatidylinositol (4,5)-diphosphate levels on the cytoplasmic surface of the endoplasmic reticulum and thereby regulates secretion. Ref.2 Ref.3

Catalytic activity

1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate.

Subcellular location

Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side Ref.3.

Miscellaneous

Present with 1200 molecules/cell in log phase SD medium. Ref.4

Sequence similarities

Belongs to the inositol-1,4,5-trisphosphate 5-phosphatase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 384384Inositol-1,4,5-trisphosphate 5-phosphatase 4
PRO_0000268682

Amino acid modifications

Modified residue2201Phosphoserine Ref.5
Modified residue2211Phosphoserine Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q08227-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: C77711D57C64B365

FASTA38443,799
        10         20         30         40         50         60 
MNKTNWKVSV TTFNCGKEFP VENSKAIVKQ LLFPYDDGIS QLELQDLYVL GFQEVVPIWQ 

        70         80         90        100        110        120 
GSFPAVNRDL IDRITTTAVN CLNEKVSATQ GDEQYSCLGV NSLGAITIIV LYNNNALKVK 

       130        140        150        160        170        180 
DDILKRNGKC GWFGTHLKGG TLISFQMTRN GEENWERFSY ICAHLNANEG VNNRNQRIDD 

       190        200        210        220        230        240 
YKRIMSEVCD SEVAKSDHFF FLGDLNFRVT STYDPTTNYS STTTLRRLLE NHEELNLLRK 

       250        260        270        280        290        300 
GEDEPLCKGF QELKITFPPT YKFKLFEKET YNTKRIPSWC DRILYKSYAV PTFAQEGTYH 

       310        320        330        340        350        360 
SVPRSNALLF SDHQPVNLTV RLPRSTGTPV PLSLHIEKYP LSWSSGLIGQ IGDAVIGYCG 

       370        380 
WLVTKNVHYW ILGSLLLYLL LKIL 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. expand/collapse author list , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
Nature 387:98-102(1997) [PubMed: 9169874] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[2]"Phosphatidylinositol 4,5-bisphosphate functions as a second messenger that regulates cytoskeleton-plasma membrane adhesion."
Raucher D., Stauffer T., Chen W., Shen K., Guo S., York J.D., Sheetz M.P., Meyer T.
Cell 100:221-228(2000) [PubMed: 10660045] [Abstract]
Cited for: FUNCTION.
[3]"The yeast inositol polyphosphate 5-phosphatase Inp54p localizes to the endoplasmic reticulum via a C-terminal hydrophobic anchoring tail: regulation of secretion from the endoplasmic reticulum."
Wiradjaja F., Ooms L.M., Whisstock J.C., McColl B.K., Helfenbaum L., Sambrook J.F., Gething M.J., Mitchell C.A.
J. Biol. Chem. 276:7643-7653(2001) [PubMed: 11116155] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[4]"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: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]"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: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220 AND SER-221, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z74807 Genomic DNA. Translation: CAA99075.1.
PIRS66758.
RefSeqNP_014576.1.

3D structure databases

HSSPHSSP built from PDB template 1I9Z based on UniProtKB O43001.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-2768N.
IntActQ08227. 7 interactions.
STRINGQ08227.

Genome annotation databases

EnsemblYOL065C; YOL065C; YOL065C; Saccharomyces cerevisiae. [Genome view]
GeneID854089.
KEGGsce:YOL065C.
NMPDRfig|4932.3.peg.5668.

Organism-specific databases

CYGDYOL065c.
SGDS000005426. INP54.

Phylogenomic databases

eggNOGfuNOG10764.
HOGENOMHBG202764.
OMAHLNANEG.
OrthoDBEOG9WSXSV.
PhylomeDBQ08227.

Enzyme and pathway databases

BRENDA3.1.3.36. 250.

Gene expression databases

ArrayExpressQ08227.
GenevestigatorQ08227.
GermOnlineYOL065C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR005135. Endo/exonuclease/phosphatase.
IPR000300. IPPc.
[Graphical view]
PfamPF03372. Exo_endo_phos. 1 hit.
[Graphical view]
SMARTSM00128. IPPc. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio975740.

Entry information

Entry nameINP54_YEAST
AccessionPrimary (citable) accession number: Q08227
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: November 1, 1996
Last modified: February 9, 2010
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Yeast

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents