Q08227 (INP54_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Inositol-1,4,5-trisphosphate 5-phosphatase 4
EC=3.1.3.36

Gene names

Name:	INP54
Ordered Locus Names:	YOL065C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	384 AA.
Sequence status	Complete.
Protein existence	Evidence 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.3 Ref.4
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.4.
Miscellaneous	Present with 1200 molecules/cell in log phase SD medium. Ref.5
Sequence similarities	Belongs to the inositol-1,4,5-trisphosphate 5-phosphatase family.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Endoplasmic reticulum Membrane
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	phosphatidylinositol dephosphorylation Inferred from direct assay Ref.3. Source: SGD protein transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity Inferred from direct assay Ref.3. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 384	384	Inositol-1,4,5-trisphosphate 5-phosphatase 4		PRO_0000268682
Amino acid modifications
	Modified residue	220	1	Phosphoserine Ref.6
	Modified residue	221	1	Phosphoserine Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Q08227 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: C77711D57C64B365	FASTA	384	43,799
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"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.
[4]	"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.
[5]	"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].
[6]	"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. BK006948 Genomic DNA. Translation: DAA10718.1.
PIR	S66758.
RefSeq	NP_014576.1. NM_001183320.1.
3D structure databases
HSSP	HSSP built from PDB template 1I9Z based on UniProtKB O43001.
ProteinModelPortal	Q08227.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2768N.
IntAct	Q08227. 5 interactions.
MINT	MINT-566375.
STRING	Q08227.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YOL065C; YOL065C; YOL065C.
GeneID	854089.
KEGG	sce:YOL065C.
NMPDR	fig|4932.3.peg.5668.
Organism-specific databases
CYGD	YOL065c.
SGD	S000005426. INP54.
Phylogenomic databases
eggNOG	fuNOG10764.
HOGENOM	HBG202764.
OMA	HLNANEG.
OrthoDB	EOG41NXVK.
Gene expression databases
ArrayExpress	Q08227.
Genevestigator	Q08227.
GermOnline	YOL065C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR005135. Endo/exonuclease/phosphatase. IPR000300. IPPc. [Graphical view]
KO	K01106.
Pfam	PF03372. Exo_endo_phos. 1 hit. [Graphical view]
SMART	SM00128. IPPc. 1 hit. [Graphical view]
SUPFAM	SSF56219. Exo_endo_phos. 1 hit.
ProtoNet	Search...
Other
NextBio	975740.

Entry information

Entry name

INP54_YEAST

Accession

Primary (citable) accession number: Q08227
Secondary accession number(s): D6W202

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	November 1, 1996
Last modified:	December 14, 2011
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program