Q9JMC1 (PI5PA_RAT) Reviewed, UniProtKB/Swiss-Prot

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
Proline-rich inositol polyphosphate 5-phosphatase

Gene names

Name:	Inpp5j
Synonyms:	Pib5pa, Pipp

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	1001 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.
Catalytic activity	D-myo-inositol 1,4,5-trisphosphate + H2O = myo-inositol 1,4-bisphosphate + phosphate. Ref.1 1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate. Ref.1
Subcellular location	Cytoplasm. Note: Predominantly localized to membrane ruffles. Ref.1
Tissue specificity	Expressed in heart, brain, kidney, stomach, small intestine and lung. Not expressed in spleen, thymus, skeletal muscle, testis and skin. Ref.1
Domain	The 5 Arg-Ser-Xaa-Ser-Xaa-Xaa (RSXSXX) motifs may constitute binding sites for the 14-3-3 protein.
Post-translational modification	Phosphorylated on Ser/Thr residues.
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
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	negative regulation of microtubule polymerization Inferred from mutant phenotype. Source: RGD negative regulation of neuron projection development Inferred from mutant phenotype. Source: RGD
Cellular component	cytoplasm Inferred from direct assay. Source: RGD growth cone Inferred from direct assay. Source: RGD ruffle Inferred from direct assay Ref.1. Source: RGD
Molecular function	SH3 domain binding Inferred from electronic annotation. Source: UniProtKB-KW inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity Inferred from electronic annotation. Source: EC inositol-1,4,5-trisphosphate 5-phosphatase activity Inferred from electronic annotation. Source: EC inositol-polyphosphate 5-phosphatase activity Inferred from direct assay Ref.1. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1001	1001	Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A		PRO_0000209740
Regions
	Region	420 – 723	304	Catalytic Potential
	Region	724 – 835	112	Required for ruffle localization By similarity
	Motif	6 – 11	6	RSXSXX motif 1
	Motif	346 – 351	6	SH3-binding Potential
	Motif	351 – 356	6	RSXSXX motif 2
	Motif	869 – 874	6	RSXSXX motif 3
	Motif	880 – 885	6	RSXSXX motif 4
	Motif	906 – 911	6	RSXSXX motif 5
	Compositional bias	50 – 387	338	Pro-rich
	Compositional bias	835 – 932	98	Ser-rich
Amino acid modifications
	Modified residue	348	1	Phosphoserine By similarity
	Modified residue	350	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9JMC1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 7BE7741FEF8F3FAB	FASTA	1,001	107,208
	10 20 30 40 50 60 MEGQSRSGSA KSGTRTGLGP LPGTHGALQT GTPSKKVNSS FQLPAKNTGP TPSEPRLALA 70 80 90 100 110 120 PVGPRAAVSP PSERPRLALS SPRPILAPLS TAGEQKRPPP HRSSKPAPTS VGQLVVSAAA 130 140 150 160 170 180 GPKPPPVASV SILAPKSLGQ LVISASAMPR PTPAPLGPIL SPTSRDQKQL SPTSVGPKPA 190 200 210 220 230 240 LATSGLSLAL ASQEQPPQSP SSPSPVPSPV LSPSQESHLA PATVTSTPAS ERQLPARQKD 250 260 270 280 290 300 TAVRRPIPPA DGCLHTPVQA AGLATSPPRA QTSSDPRLSP SFRARPEAPR HSPEDPVLPP 310 320 330 340 350 360 PPQTLPLDVS SGLPESGTRS PGLLSPTFRP GIPSNQTVPP PLPKPPRSPS RSPSRSPNRS 370 380 390 400 410 420 PCVPPAPEVA LPRPVTQGAG PGKCPSPNLQ TQESPVATAT SPTSSWSAQP TCKSDPGFRI 430 440 450 460 470 480 TVVTWNVGTA MPPDDVTSLL HLGGGHDSDG ADMIAIGLQE VNSMINKRLK DALFTDQWSE 490 500 510 520 530 540 LFMDALGPFN FVLVSTVRMQ GVILLLFAKY YHLPFLRDVQ TDCTRTGLGG YWGNKGGVSV 550 560 570 580 590 600 RLAAFGHMLC FLNCHLPAHM DKAEQRKDNF QTILSLQQFQ GPGAHGILDH DLVFWFGDLN 610 620 630 640 650 660 FRIESYDLHF VKFAIDSNQL HQLWEKDQLN MAKNTWPILK GFQEGPLNFA PTFKFDVGTN 670 680 690 700 710 720 KYDTSAKKRK PAWTDRILWK VKAPSGGPSP SGRESHRLQV TQHSYRSHME YTVSDHKPVA 730 740 750 760 770 780 ARFLLQFAFR DDVPLVRLEV ADEWARPEQA VVRYRVETVF ARSSWDWIGL YRVGFRHCKD 790 800 810 820 830 840 YVAYVWAKHE EVDGNIYQVT FSEESLPKGH GDFILGYYSH HHSILIGVTE PFQISLPTSE 850 860 870 880 890 900 SASSSTDSSG TSSEGEDDST LELLAPKSRS PSPGKSKRHR SRSPGLARFP SLALRPSSRE 910 920 930 940 950 960 RRGGSRSPSP QSRQLPRVAP DRGHSSGSRG SSEEGPSGPP GPWAFPPAVP RSLGLLPALR 970 980 990 1000 LETVDPGGGG SWGPDQEAPD PNSLSPSPQG RLGLEDGGLG P

References

[1]	"Novel inositol polyphosphate 5-phosphatase localizes at membrane ruffles." Mochizuki Y., Takenawa T. J. Biol. Chem. 274:36790-36795(1999) [PubMed: 10593988] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ENZYME ACTIVITY. Tissue: Brain.
[2]	Lubec G., Kang S.U., Lubec S. Submitted (SEP-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1-15 AND 903-917, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB032551 mRNA. Translation: BAA90553.1.
IPI	IPI00204538.
RefSeq	NP_598246.1. NM_133562.1.
UniGene	Rn.23872.
3D structure databases
ProteinModelPortal	Q9JMC1.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9JMC1.
PTM databases
PhosphoSite	Q9JMC1.
Proteomic databases
PRIDE	Q9JMC1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000026293; ENSRNOP00000026293; ENSRNOG00000019361.
GeneID	171088.
KEGG	rno:171088.
UCSC	NM_133562. rat.
Organism-specific databases
CTD	27124.
RGD	620541. Inpp5j.
Phylogenomic databases
eggNOG	roNOG05647.
GeneTree	ENSGT00590000082823.
HOVERGEN	HBG082135.
InParanoid	Q9JMC1.
OMA	APTSVGQ.
OrthoDB	EOG4HDSTN.
PhylomeDB	Q9JMC1.
Gene expression databases
ArrayExpress	Q9JMC1.
Genevestigator	Q9JMC1.
GermOnline	ENSRNOG00000019361. Rattus norvegicus.
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	621732.

Entry information

Entry name

PI5PA_RAT

Accession

Primary (citable) accession number: Q9JMC1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 30, 2003
Last sequence update:	October 1, 2000
Last modified:	November 16, 2011
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program