Reviewed, UniProtKB/Swiss-Prot Q9JII1 (INP5E_MOUSE)

Names and origin

Protein names

Recommended name:
    72 kDa inositol polyphosphate 5-phosphatase
    EC=3.1.3.36
Alternative name(s):
    Phosphatidylinositol-4,5-bisphosphate 5-phosphatase
    Phosphatidylinositol polyphosphate 5-phosphatase type IV

Gene names

Name:

Inpp5e

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	647 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Converts phosphatidylinositol-3,4,5-triphosphate (PtdIns 3,4,5-P3) to PtdIns-P2. Specific for lipid substrates, inactive towards water soluble inositol phosphates. Ref.1
Catalytic activity	1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate.
Subcellular location	Golgi apparatus › Golgi stack membrane; Peripheral membrane protein; Cytoplasmic side. Note: Peripheral membrane protein associated with Golgi stacks. Ref.1
Tissue specificity	Highly expressed in testis, in pachytene and diplotene spermatocytes, but not in more mature elongating spermatids. Detected in neurons throughout the brain. Ref.1
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR By similarity.
Sequence similarities	Belongs to the inositol-1,4,5-trisphosphate 5-phosphatase type IV family.

Ontologies

Keywords
Biological process	Lipid metabolism
Cellular component	Golgi apparatus Membrane
Domain	Repeat
Molecular function	Hydrolase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	phosphoinositide metabolic process Ref.1 Inferred from direct assay. Source: MGI
Cellular component	Golgi membrane Ref.1 Inferred from direct assay. Source: MGI internal side of plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity Ref.1 Inferred from direct assay. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 647	647	72 kDa inositol polyphosphate 5-phosphatase		PRO_0000209748
Regions
	Repeat	52 – 55	4	1
	Repeat	76 – 79	4	2
	Repeat	240 – 243	4	3
	Region	52 – 243	192	3 X 4 AA repeats of P-X-X-P
	Compositional bias	96 – 101	6	Poly-Arg
Amino acid modifications
	Modified residue	103	1	Phosphoserine By similarity
	Modified residue	245	1	Phosphoserine Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q9JII1-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 4BBE3A39DB7ECB0E	FASTA	647	71,915
	10 20 30 40 50 60 MPSKSACLRH TEAPGQLEGR MLQGQPPNTE KKLIPTPGFL PASDSQGSET NPMPPFSIPA 70 80 90 100 110 120 KTSNQNPQTK ANLITPQPPI RPKLERTLSL DDKGWRRRRF RGSQEDLTVQ NGASPCRGSL 130 140 150 160 170 180 QDSVAQSPAY SRPLPCLSTS LQEIPKSRRA TGSEGGSPSL WSDCLSGMIS TSLDLLHRDA 190 200 210 220 230 240 ASGGPPSRLA SLHASHTPPA MDLSIASSSL RTANKVDPEH TDYKLRMQTR LVRAHSNLGP 250 260 270 280 290 300 SRPRSPLAGD DHSIHSARSF SLLAPIRTKD IRSRSYLEGS LLASGALLGA EELARYFPDR 310 320 330 340 350 360 NMALFVATWN MQGQKELPAS LDEFLLPTEA DYTQDLYVIG IQEGCSDRRE WETRLQETLG 370 380 390 400 410 420 PQYVLLSSAA HGVLYMSLFI RRDLIWFCSE VEYSTVTTRI VSQIKTKGAL GVSFTFFGTS 430 440 450 460 470 480 FLFITSHFTS GDGKVAERLL DYSRTIQALA LPRNVPDTNP YRSSAGDVTT RFDEVFWFGD 490 500 510 520 530 540 FNFRLSGGRV AVEAFLKQKP EVDVLALLQH DQLTREMKKG SIFRGFEEAE IHFLPSYKFD 550 560 570 580 590 600 IGKDTYDSTS KQRTPSYTDR VLYKSRHKGD ICPMKYSSCP GIKTSDHRPV YGLFQVKVRP 610 620 630 640 GRDNIPLAAG KFDRELYLIG IKRRISKEIQ RQEALKSQSS SAVCTVS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of a 72-kDa inositol-polyphosphate 5-phosphatase localized to the Golgi network." Kong A.M., Speed C.J., O'Malley C.J., Layton M.J., Meehan T., Loveland K.L., Cheema S., Ooms L.M., Mitchell C.A. J. Biol. Chem. 275:24052-24064(2000) [PubMed: 10806194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Brain.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Aorta and Vein.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Brain.
[4]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed: 18973353] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF226683 mRNA. Translation: AAF86957.1. AK080075 mRNA. Translation: BAC37823.1. AK154097 mRNA. Translation: BAE32374.1. AK170786 mRNA. Translation: BAE42028.1. BC052717 mRNA. Translation: AAH52717.1. BC080295 mRNA. Translation: AAH80295.1.
IPI	IPI00120602.
RefSeq	NP_149125.1.
UniGene	Mm.330070
3D structure databases
HSSP	HSSP built from PDB template 1I9Z based on UniProtKB O43001.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9JII1.
PTM databases
PhosphoSite	Q9JII1.
Proteomic databases
PRIDE	Q9JII1.
Genome annotation databases
Ensembl	ENSMUST00000028291; ENSMUSP00000028291; ENSMUSG00000026925; Mus musculus. [Genome view]
GeneID	64436.
KEGG	mmu:64436.
UCSC	uc008ivf.1. mouse.
Organism-specific databases
CTD	64436.
MGI	MGI:1927753. Inpp5e.
Phylogenomic databases
HOGENOM	Q9JII1.
HOVERGEN	Q9JII1.
OMA	SGMISTS.
Enzyme and pathway databases
BRENDA	3.1.3.36. 244.
Gene expression databases
ArrayExpress	Q9JII1.
Bgee	Q9JII1.
CleanEx	MM_INPP5E.
Genevestigator	Q9JII1.
GermOnline	ENSMUSG00000026925. Mus musculus.
Family and domain databases
InterPro	IPR005135. Endo/exonuclease/phosphatase. IPR000300. IPPc. [Graphical view]
Pfam	PF03372. Exo_endo_phos. 1 hit. [Graphical view]
SMART	SM00128. IPPc. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	320083.
SOURCE	Search...

Entry information

Entry name

INP5E_MOUSE

Accession

Primary (citable) accession number: Q9JII1
Secondary accession number(s): Q3TCC9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2004
Last sequence update:	October 1, 2000
Last modified:	November 3, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)