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Protein

Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A

Gene

Inpp5j

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

D-myo-inositol 1,4,5-trisphosphate + H2O = myo-inositol 1,4-bisphosphate + phosphate.1 Publication
1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate.1 Publication

GO - Molecular functioni

GO - Biological processi

  • negative regulation of microtubule polymerization Source: RGD
  • negative regulation of neuron projection development Source: RGD
  • negative regulation of peptidyl-serine phosphorylation Source: Ensembl
  • phosphatidylinositol dephosphorylation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

ReactomeiR-RNO-1660499. Synthesis of PIPs at the plasma membrane.
R-RNO-1855183. Synthesis of IP2, IP, and Ins in the cytosol.
R-RNO-1855204. Synthesis of IP3 and IP4 in the cytosol.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Inpp5j
Synonyms:Pib5pa, Pipp
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 14

Organism-specific databases

RGDi620541. Inpp5j.

Subcellular locationi

  • Cytoplasm 1 Publication

  • Note: Predominantly localized to membrane ruffles.

GO - Cellular componenti

  • cytoplasm Source: RGD
  • dendritic shaft Source: Ensembl
  • growth cone Source: RGD
  • plasma membrane Source: Ensembl
  • ruffle Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10011001Phosphatidylinositol 4,5-bisphosphate 5-phosphatase APRO_0000209740Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei171 – 1711PhosphoserineCombined sources
Modified residuei292 – 2921PhosphoserineBy similarity
Modified residuei325 – 3251PhosphoserineBy similarity
Modified residuei898 – 8981PhosphoserineBy similarity
Modified residuei985 – 9851PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated on Ser/Thr residues.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9JMC1.
PRIDEiQ9JMC1.

PTM databases

iPTMnetiQ9JMC1.
PhosphoSiteiQ9JMC1.

Expressioni

Tissue specificityi

Expressed in heart, brain, kidney, stomach, small intestine and lung. Not expressed in spleen, thymus, skeletal muscle, testis and skin.1 Publication

Gene expression databases

GenevisibleiQ9JMC1. RN.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000026293.

Structurei

3D structure databases

ProteinModelPortaliQ9JMC1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni420 – 723304CatalyticSequence analysisAdd
BLAST
Regioni724 – 835112Required for ruffle localizationBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi6 – 116RSXSXX motif 1
Motifi346 – 3516SH3-bindingSequence analysis
Motifi351 – 3566RSXSXX motif 2
Motifi869 – 8746RSXSXX motif 3
Motifi880 – 8856RSXSXX motif 4
Motifi906 – 9116RSXSXX motif 5

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi50 – 387338Pro-richAdd
BLAST
Compositional biasi835 – 93298Ser-richAdd
BLAST

Domaini

The 5 Arg-Ser-Xaa-Ser-Xaa-Xaa (RSXSXX) motifs may constitute binding sites for the 14-3-3 protein.

Sequence similaritiesi

Keywords - Domaini

Repeat, SH3-binding

Phylogenomic databases

eggNOGiKOG0565. Eukaryota.
COG5411. LUCA.
GeneTreeiENSGT00760000119075.
HOGENOMiHOG000046051.
HOVERGENiHBG082135.
InParanoidiQ9JMC1.
KOiK01106.
OMAiNIYQVTF.
OrthoDBiEOG789CB4.
PhylomeDBiQ9JMC1.
TreeFamiTF317034.

Family and domain databases

Gene3Di3.60.10.10. 1 hit.
InterProiIPR005135. Endo/exonuclease/phosphatase.
IPR000300. IPPc.
[Graphical view]
PfamiPF03372. Exo_endo_phos. 1 hit.
[Graphical view]
SMARTiSM00128. IPPc. 1 hit.
[Graphical view]
SUPFAMiSSF56219. SSF56219. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9JMC1-1 [UniParc]FASTAAdd to basket

« Hide

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

P
Length:1,001
Mass (Da):107,208
Last modified:October 1, 2000 - v1
Checksum:i7BE7741FEF8F3FAB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB032551 mRNA. Translation: BAA90553.1.
RefSeqiNP_598246.1. NM_133562.1.
UniGeneiRn.23872.

Genome annotation databases

EnsembliENSRNOT00000026293; ENSRNOP00000026293; ENSRNOG00000019361.
GeneIDi171088.
KEGGirno:171088.
UCSCiRGD:620541. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB032551 mRNA. Translation: BAA90553.1.
RefSeqiNP_598246.1. NM_133562.1.
UniGeneiRn.23872.

3D structure databases

ProteinModelPortaliQ9JMC1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000026293.

PTM databases

iPTMnetiQ9JMC1.
PhosphoSiteiQ9JMC1.

Proteomic databases

PaxDbiQ9JMC1.
PRIDEiQ9JMC1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000026293; ENSRNOP00000026293; ENSRNOG00000019361.
GeneIDi171088.
KEGGirno:171088.
UCSCiRGD:620541. rat.

Organism-specific databases

CTDi27124.
RGDi620541. Inpp5j.

Phylogenomic databases

eggNOGiKOG0565. Eukaryota.
COG5411. LUCA.
GeneTreeiENSGT00760000119075.
HOGENOMiHOG000046051.
HOVERGENiHBG082135.
InParanoidiQ9JMC1.
KOiK01106.
OMAiNIYQVTF.
OrthoDBiEOG789CB4.
PhylomeDBiQ9JMC1.
TreeFamiTF317034.

Enzyme and pathway databases

ReactomeiR-RNO-1660499. Synthesis of PIPs at the plasma membrane.
R-RNO-1855183. Synthesis of IP2, IP, and Ins in the cytosol.
R-RNO-1855204. Synthesis of IP3 and IP4 in the cytosol.

Miscellaneous databases

PROiQ9JMC1.

Gene expression databases

GenevisibleiQ9JMC1. RN.

Family and domain databases

Gene3Di3.60.10.10. 1 hit.
InterProiIPR005135. Endo/exonuclease/phosphatase.
IPR000300. IPPc.
[Graphical view]
PfamiPF03372. Exo_endo_phos. 1 hit.
[Graphical view]
SMARTiSM00128. IPPc. 1 hit.
[Graphical view]
SUPFAMiSSF56219. SSF56219. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Novel inositol polyphosphate 5-phosphatase localizes at membrane ruffles."
    Mochizuki Y., Takenawa T.
    J. Biol. Chem. 274:36790-36795(1999) [PubMed] [Europe PMC] [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, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPI5PA_RAT
AccessioniPrimary (citable) accession number: Q9JMC1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: October 1, 2000
Last modified: July 6, 2016
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.