Reviewed, UniProtKB/Swiss-Prot P59644 (PI5PA_MOUSE)

Names and origin

Protein names

Recommended name:
    Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A
    EC=3.1.3.56
Alternative name(s):
    Inositol polyphosphate 5-phosphatase J

Gene names

Name:	Inpp5j
Synonyms:	Pib5pa

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	1003 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Inositol 5-phosphatase, which converts inositol 1,4,5-trisphosphate to inositol 1,4-bisphosphate. Also converts phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol 4-phosphate and inositol 1,3,4,5-tetrakisphosphate to inositol 1,3,4-trisphosphate in vitro. May be involved in modulation of the function of inositol and phosphatidylinositol polyphosphate-binding proteins that are present at membranes ruffles By similarity.
Catalytic activity	D-myo-inositol 1,4,5-trisphosphate + H2O = myo-inositol 1,4-bisphosphate + phosphate. 1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate.
Subcellular location	Cytoplasm. Note: Predominantly localized to membrane ruffles. Ref.2
Domain	The 5 Arg-Ser-Xaa-Ser-Xaa-Xaa (RSXSXX) motifs may constitute binding sites for the 14-3-3 protein. Ref.2
Sequence similarities	Belongs to the inositol-1,4,5-trisphosphate 5-phosphatase type II family.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Repeat SH3-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	negative regulation of neuron projection development Inferred from direct assay. Source: MGI negative regulation of peptidyl-serine phosphorylation Inferred from direct assay. Source: MGI
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell dendritic shaft Inferred from direct assay. Source: MGI growth cone Inferred from direct assay. Source: MGI plasma membrane Inferred from direct assay. Source: MGI
Molecular function	SH3 domain binding Inferred from electronic annotation. Source: UniProtKB-KW inositol-polyphosphate 5-phosphatase activity Inferred from electronic annotation. Source: EC phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity 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 – 1003	1003	Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A		PRO_0000209739
Regions
	Region	422 – 725	304	Catalytic Potential
	Region	726 – 837	112	Required for ruffle localization
	Motif	6 – 11	6	RSXSXX motif 1
	Motif	346 – 351	6	SH3-binding Potential
	Motif	351 – 356	6	RSXSXX motif 2
	Motif	871 – 876	6	RSXSXX motif 3
	Motif	882 – 887	6	RSXSXX motif 4
	Motif	908 – 913	6	RSXSXX motif 5
	Compositional bias	50 – 374	325	Pro-rich
	Compositional bias	837 – 934	98	Ser-rich
Amino acid modifications
	Modified residue	348	1	Phosphoserine Ref.3
	Modified residue	350	1	Phosphoserine Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P59644-1 [UniParc]. Last modified April 30, 2003. Version 1. Checksum: AFF4FD929CFCB6BA	FASTA	1,003	107,603
	10 20 30 40 50 60 MEGQTRSGSA RPGTRTGLGP LPGTHGVLQA EIPSKKVNSS FQLPAKNSGP ASSEPRLTLA 70 80 90 100 110 120 PVGPRAAVSP PSERPRLVLS SPRPVLAPLS IAGEQKRPPP PHSSNRAAKS VGQLVVSAAA 130 140 150 160 170 180 ASKPPPVASV SILAPKSLGQ LVISASAMPR PSPAPLGSVL TPTSRDQKQL SPTSVGPKPA 190 200 210 220 230 240 LATSGLSLAL ASQEQPPQSP SSPSPVPSPV LSPSQEGHLA AASVTSTPAS ERQLPARQKD 250 260 270 280 290 300 TAVPRPTPPA DKCLYTPERA AGPATSPPRA QAFSDPRLSP SFRARPEAPR HSPEDPVLPP 310 320 330 340 350 360 PPQTLPLDVS PGLPESGTRS PGLLSPTFRP GIPSSQTVPP PLRKPPRSPS RSPSRSPNRS 370 380 390 400 410 420 PCLPPAPEVA LPKPVTQAAG SGRCPSPNLQ AQESPAAATT TTSPTSSWSA QPTCKSDPGF 430 440 450 460 470 480 RITVVTWNVG TAMPPDDVTS LLHLGSGHDN DGADMIAIGL QEVNSMINKR LKDALFTDQW 490 500 510 520 530 540 SELFMDALGP FNFVLVSTVR MQGVILLLFA KYYHLPFLRD VQTDCTRTGL GGYWGNKGGV 550 560 570 580 590 600 SVRLAAFGHM LCFLNCHLPA HMDKAEQRKD NFQTILSLQQ FQGPGAHGIL DHDLVFWFGD 610 620 630 640 650 660 LNFRIESYDL HFVKFAIDSN QLHQLWEKDQ LNMAKNTWPI LKGFQEGPLN FAPTFKFDVG 670 680 690 700 710 720 TNKYDTSAKK RKPAWTDRIL WKVKAPSGGP SPSGRESHRL QVTQHSYRSH MEYTVSDHKP 730 740 750 760 770 780 VAAQFILQFA FRDDVPLVRL EVADEWARPE QAVVRYRVET VFARSSWDWI GLYRVGFRHC 790 800 810 820 830 840 KDYVAYVWAK HEEVDGNIYQ VTFSEESLPK GHGDFILGYY SHHHSILIGV TEPFQISLPT 850 860 870 880 890 900 SESASSSTDS SGTSSEGEDD STLELLAPKS RSPSPGKSKR HRSRSPGLAR FPSLALHPSS 910 920 930 940 950 960 RERRGGSRSP SPQSRQLPRV APDRGHSSSS RGSSEEGPSG LPGPWAFPPS VPRSLGLLPA 970 980 990 1000 LRLETVDPGG GGSWGADQEA PDPNSLSPSP QGRLGLEEGG LGP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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. Tissue: Diencephalon.
[2]	"Identification of a novel domain in two mammalian inositol-polyphosphate 5-phosphatases that mediates membrane ruffle localization. The inositol 5-phosphatase SKIP localizes to the endoplasmic reticulum and translocates to membrane ruffles following epidermal growth factor stimulation." Gurung R., Tan A., Ooms L.M., McGrath M.J., Huysmans R.D., Munday A.D., Prescott M., Whisstock J.C., Mitchell C.A. J. Biol. Chem. 278:11376-11385(2003) [PubMed: 12536145] [Abstract] Cited for: SUBCELLULAR LOCATION, IDENTIFICATION OF DOMAIN REQUIRED FOR MEMBRANE RUFFLE LOCALIZATION.
[3]	"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-348 AND SER-350, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK034272 mRNA. Translation: BAC28654.1.
IPI	IPI00173277.
UniGene	Mm.24313
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	P59644.
PTM databases
PhosphoSite	P59644.
Proteomic databases
PRIDE	P59644.
Genome annotation databases
Ensembl	ENSMUST00000044507; ENSMUSP00000046625; ENSMUSG00000034570; Mus musculus. [Genome view]
UCSC	uc007hta.1. mouse.
Organism-specific databases
MGI	MGI:2158663. Inpp5j.
Phylogenomic databases
HOGENOM	HBG125086.
HOVERGEN	P59644.
InParanoid	P59644.
PhylomeDB	P59644.
Enzyme and pathway databases
BRENDA	3.1.3.56. 244.
Gene expression databases
ArrayExpress	P59644.
Bgee	P59644.
Genevestigator	P59644.
GermOnline	ENSMUSG00000034570. 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	370509.
SOURCE	Search...

Entry information

Entry name

PI5PA_MOUSE

Accession

Primary (citable) accession number: P59644

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 30, 2003
Last sequence update:	April 30, 2003
Last modified:	February 9, 2010
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)