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Protein

72 kDa inositol polyphosphate 5-phosphatase

Gene

Inpp5e

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Converts phosphatidylinositol 3,4,5-trisphosphate (PtdIns 3,4,5-P3) to PtdIns-P2, and phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol 4-phosphate. Specific for lipid substrates, inactive towards water soluble inositol phosphates.1 Publication

Catalytic activityi

1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate.1 Publication

GO - Molecular functioni

GO - Biological processi

  • inositol phosphate dephosphorylation Source: MGI
  • phosphatidylinositol dephosphorylation Source: MGI
  • phosphatidylinositol metabolic process Source: MGI
  • positive regulation of neuron projection development Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid metabolism

Enzyme and pathway databases

BRENDAi3.1.3.36. 3474.
ReactomeiR-MMU-1660514. Synthesis of PIPs at the Golgi membrane.
R-MMU-5624958. ARL13B-mediated ciliary trafficking of INPP5E.

Names & Taxonomyi

Protein namesi
Recommended name:
72 kDa inositol polyphosphate 5-phosphatase (EC:3.1.3.361 Publication)
Alternative name(s):
Phosphatidylinositol 4,5-bisphosphate 5-phosphatase
Phosphatidylinositol polyphosphate 5-phosphatase type IV
Gene namesi
Name:Inpp5e
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1927753. Inpp5e.

Subcellular locationi

GO - Cellular componenti

  • axoneme Source: UniProtKB
  • cytoskeleton Source: UniProtKB-KW
  • Golgi cisterna membrane Source: UniProtKB-SubCell
  • Golgi membrane Source: MGI
  • plasma membrane Source: UniProtKB-SubCell
  • ruffle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cilium, Cytoplasm, Cytoskeleton, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 64464472 kDa inositol polyphosphate 5-phosphataseBy similarityPRO_0000209748Add
BLAST
Propeptidei645 – 6473Removed in mature formBy similarityPRO_0000431689

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei103 – 1031PhosphoserineCombined sources
Modified residuei197 – 1971PhosphothreonineCombined sources
Modified residuei245 – 2451PhosphoserineBy similarity
Modified residuei259 – 2591PhosphoserineCombined sources
Modified residuei644 – 6441Cysteine methyl esterBy similarity
Lipidationi644 – 6441S-farnesyl cysteineBy similarity

Keywords - PTMi

Lipoprotein, Methylation, Phosphoprotein, Prenylation

Proteomic databases

MaxQBiQ9JII1.
PaxDbiQ9JII1.
PRIDEiQ9JII1.

PTM databases

iPTMnetiQ9JII1.
PhosphoSiteiQ9JII1.

Expressioni

Tissue specificityi

Highly expressed in testis, in pachytene and diplotene spermatocytes, but not in more mature elongating spermatids. Detected in neurons throughout the brain.1 Publication

Gene expression databases

BgeeiQ9JII1.
CleanExiMM_INPP5E.
ExpressionAtlasiQ9JII1. baseline and differential.
GenevisibleiQ9JII1. MM.

Interactioni

Subunit structurei

Interacts (when prenylated) with PDE6D; this is important for normal location in cilia.By similarity

Protein-protein interaction databases

BioGridi211076. 2 interactions.
STRINGi10090.ENSMUSP00000119485.

Structurei

3D structure databases

ProteinModelPortaliQ9JII1.
SMRiQ9JII1. Positions 285-626.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati52 – 5541
Repeati76 – 7942
Repeati240 – 24343

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni52 – 2431923 X 4 AA repeats of P-X-X-PAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi96 – 1016Poly-Arg

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0565. Eukaryota.
COG5411. LUCA.
GeneTreeiENSGT00760000119075.
HOGENOMiHOG000231541.
HOVERGENiHBG052132.
InParanoidiQ9JII1.
KOiK01099.
OMAiSCSPPCL.
OrthoDBiEOG70KGPF.
PhylomeDBiQ9JII1.
TreeFamiTF323475.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9JII1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSKSACLRH TEAPGQLEGR MLQGQPPNTE KKLIPTPGFL PASDSQGSET
60 70 80 90 100
NPMPPFSIPA KTSNQNPQTK ANLITPQPPI RPKLERTLSL DDKGWRRRRF
110 120 130 140 150
RGSQEDLTVQ NGASPCRGSL QDSVAQSPAY SRPLPCLSTS LQEIPKSRRA
160 170 180 190 200
TGSEGGSPSL WSDCLSGMIS TSLDLLHRDA ASGGPPSRLA SLHASHTPPA
210 220 230 240 250
MDLSIASSSL RTANKVDPEH TDYKLRMQTR LVRAHSNLGP SRPRSPLAGD
260 270 280 290 300
DHSIHSARSF SLLAPIRTKD IRSRSYLEGS LLASGALLGA EELARYFPDR
310 320 330 340 350
NMALFVATWN MQGQKELPAS LDEFLLPTEA DYTQDLYVIG IQEGCSDRRE
360 370 380 390 400
WETRLQETLG PQYVLLSSAA HGVLYMSLFI RRDLIWFCSE VEYSTVTTRI
410 420 430 440 450
VSQIKTKGAL GVSFTFFGTS FLFITSHFTS GDGKVAERLL DYSRTIQALA
460 470 480 490 500
LPRNVPDTNP YRSSAGDVTT RFDEVFWFGD FNFRLSGGRV AVEAFLKQKP
510 520 530 540 550
EVDVLALLQH DQLTREMKKG SIFRGFEEAE IHFLPSYKFD IGKDTYDSTS
560 570 580 590 600
KQRTPSYTDR VLYKSRHKGD ICPMKYSSCP GIKTSDHRPV YGLFQVKVRP
610 620 630 640
GRDNIPLAAG KFDRELYLIG IKRRISKEIQ RQEALKSQSS SAVCTVS
Length:647
Mass (Da):71,915
Last modified:October 1, 2000 - v1
Checksum:i4BBE3A39DB7ECB0E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS15805.1.
RefSeqiNP_001277366.1. NM_001290437.1.
NP_149125.1. NM_033134.3.
UniGeneiMm.330070.

Genome annotation databases

EnsembliENSMUST00000145701; ENSMUSP00000119485; ENSMUSG00000026925.
GeneIDi64436.
KEGGimmu:64436.
UCSCiuc008ivf.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS15805.1.
RefSeqiNP_001277366.1. NM_001290437.1.
NP_149125.1. NM_033134.3.
UniGeneiMm.330070.

3D structure databases

ProteinModelPortaliQ9JII1.
SMRiQ9JII1. Positions 285-626.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211076. 2 interactions.
STRINGi10090.ENSMUSP00000119485.

PTM databases

iPTMnetiQ9JII1.
PhosphoSiteiQ9JII1.

Proteomic databases

MaxQBiQ9JII1.
PaxDbiQ9JII1.
PRIDEiQ9JII1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000145701; ENSMUSP00000119485; ENSMUSG00000026925.
GeneIDi64436.
KEGGimmu:64436.
UCSCiuc008ivf.2. mouse.

Organism-specific databases

CTDi56623.
MGIiMGI:1927753. Inpp5e.

Phylogenomic databases

eggNOGiKOG0565. Eukaryota.
COG5411. LUCA.
GeneTreeiENSGT00760000119075.
HOGENOMiHOG000231541.
HOVERGENiHBG052132.
InParanoidiQ9JII1.
KOiK01099.
OMAiSCSPPCL.
OrthoDBiEOG70KGPF.
PhylomeDBiQ9JII1.
TreeFamiTF323475.

Enzyme and pathway databases

BRENDAi3.1.3.36. 3474.
ReactomeiR-MMU-1660514. Synthesis of PIPs at the Golgi membrane.
R-MMU-5624958. ARL13B-mediated ciliary trafficking of INPP5E.

Miscellaneous databases

NextBioi320083.
PROiQ9JII1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JII1.
CleanExiMM_INPP5E.
ExpressionAtlasiQ9JII1. baseline and differential.
GenevisibleiQ9JII1. MM.

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. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain.
  4. "INPP5E mutations cause primary cilium signaling defects, ciliary instability and ciliopathies in human and mouse."
    Jacoby M., Cox J.J., Gayral S., Hampshire D.J., Ayub M., Blockmans M., Pernot E., Kisseleva M.V., Compere P., Schiffmann S.N., Gergely F., Riley J.H., Perez-Morga D., Woods C.G., Schurmans S.
    Nat. Genet. 41:1027-1031(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103; THR-197 AND SER-259, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Lung and Spleen.

Entry informationi

Entry nameiINP5E_MOUSE
AccessioniPrimary (citable) accession number: Q9JII1
Secondary accession number(s): Q3TCC9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: October 1, 2000
Last modified: February 17, 2016
This is version 118 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, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.