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Q8C5L6 (INP5K_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inositol polyphosphate 5-phosphatase K

EC=3.1.3.56
Alternative name(s):
Skeletal muscle and kidney-enriched inositol phosphatase
Gene names
Name:Inpp5k
Synonyms:Pps, Skip
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length468 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Inositol 5-phosphatase which acts on inositol 1,4,5-trisphosphate, inositol 1,3,4,5-tetrakisphosphate, phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate. Has 6-fold higher affinity for phosphatidylinositol 4,5-bisphosphate than for inositol 1,4,5-trisphosphate. May negatively regulate assembly of the actin cytoskeleton By similarity. UniProtKB Q9BT40

Catalytic activity

D-myo-inositol 1,4,5-trisphosphate + H2O = myo-inositol 1,4-bisphosphate + phosphate. UniProtKB Q9BT40

Subcellular location

Endoplasmic reticulum. Note: Following stimulation with EGF, translocates to membrane ruffles By similarity.

Sequence similarities

Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase type II family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Inferred from direct assay PubMed 21938401. Source: UniProtKB

cellular response to cAMP

Inferred from direct assay PubMed 21938401. Source: UniProtKB

cellular response to epidermal growth factor stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to hormone stimulus

Inferred from direct assay PubMed 21938401. Source: UniProtKB

cellular response to insulin stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to tumor necrosis factor

Inferred from sequence or structural similarity. Source: UniProtKB

dephosphorylation

Inferred from direct assay PubMed 21938401. Source: UniProtKB

glucose homeostasis

Inferred from mutant phenotype PubMed 19250614. Source: UniProtKB

in utero embryonic development

Inferred from mutant phenotype PubMed 18573875. Source: MGI

inositol phosphate dephosphorylation

Inferred from sequence alignment PubMed 12536145. Source: MGI

negative regulation by host of viral transcription

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of MAP kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of calcium ion transport

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of dephosphorylation

Inferred from mutant phenotype PubMed 19250614. Source: UniProtKB

negative regulation of glucose transport

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of glycogen (starch) synthase activity

Inferred from mutant phenotype PubMed 19250614. Source: UniProtKB

negative regulation of glycogen biosynthetic process

Inferred from mutant phenotype PubMed 19250614. Source: UniProtKB

negative regulation of insulin receptor signaling pathway

Inferred from mutant phenotype PubMed 19250614. Source: UniProtKB

negative regulation of peptidyl-serine phosphorylation

Inferred from mutant phenotype PubMed 19250614. Source: UniProtKB

negative regulation of peptidyl-threonine phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of protein kinase B signaling

Inferred from mutant phenotype PubMed 19250614. Source: UniProtKB

negative regulation of protein kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of protein phosphorylation

Inferred from direct assay PubMed 21938401. Source: UniProtKB

negative regulation of protein targeting to membrane

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of single stranded viral RNA replication via double stranded DNA intermediate

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of stress fiber assembly

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 21938401. Source: UniProtKB

phosphatidylinositol dephosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of renal water transport

Inferred from direct assay PubMed 21938401. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 21938401. Source: UniProtKB

positive regulation of urine volume

Inferred from direct assay PubMed 21938401. Source: UniProtKB

protein targeting to plasma membrane

Inferred from direct assay PubMed 21938401. Source: UniProtKB

regulation of glycogen biosynthetic process

Inferred from mutant phenotype PubMed 19250614. Source: UniProtKB

response to insulin

Inferred from mutant phenotype PubMed 18573875. Source: MGI

ruffle assembly

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 21938401. Source: UniProtKB

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

membrane

Inferred from sequence or structural similarity. Source: UniProtKB

neuron projection

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

ruffle

Inferred from sequence or structural similarity. Source: UniProtKB

ruffle membrane

Inferred from sequence or structural similarity. Source: UniProtKB

trans-Golgi network

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functioninositol bisphosphate phosphatase activity

Inferred from mutant phenotype PubMed 19250614. Source: UniProtKB

inositol trisphosphate phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

inositol-1,4,5-trisphosphate 5-phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

inositol-polyphosphate 5-phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

phosphatidylinositol phosphate 5-phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylinositol trisphosphate phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity

Inferred from direct assay PubMed 21938401. Source: UniProtKB

vasopressin receptor activity

Inferred from direct assay PubMed 21938401. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 468468Inositol polyphosphate 5-phosphatase K
PRO_0000209728

Regions

Region34 – 337304Catalytic Potential
Region340 – 468129Required for ruffle localization UniProtKB Q9BT40

Experimental info

Sequence conflict3291D → E in BAC37126. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q8C5L6 [UniParc].

Last modified March 15, 2004. Version 2.
Checksum: F2E1CA370B97A8A1

FASTA46854,159
        10         20         30         40         50         60 
MQHGDRNTPG YREGIMSAVS LRRPSAPKGF ALSVHVVTWN VASAAPTVDL SDLLQLNNQD 

        70         80         90        100        110        120 
LNLDIYIIGL QEMNFGIISL LSDAAFEDPW SSLFMDMLSP LNFVKISQVR MQGLLLLVFA 

       130        140        150        160        170        180 
KYQHLPYIQI ISTKSTPTGL YGYWGNKGGV NVCLKLYGYY VSIINCHLPP HMYNNDQRLE 

       190        200        210        220        230        240 
HFDRILESLT FEGYDVPNIL DHDLILWFGD MNFRIEDFGL LFVQESITRK YYKELWEKDQ 

       250        260        270        280        290        300 
LFIAKKNDQL LREFQEGPLL FPPTYKFDRH SNNYDTSEKK RKPAWTDRIL WRLKRQPSQA 

       310        320        330        340        350        360 
SPLASSVPTS YFLLTLKNYV SHMAYSISDH KPVTGTFDLE LNPLMSVPLI TMMPEHLWTM 

       370        380        390        400        410        420 
ENDMLISYTS TPEFLSSSWD WIGLYKVGMR HINDYVAYVW VGDNQVSYGN NPNQVYINIS 

       430        440        450        460 
AIPDTEDQFL LCYYSNNLHS VVGISQPFKI PIRSFLREDT LYEPEPQI 

« Hide

References

« Hide 'large scale' references
[1]"The vibrator mutation causes neurodegeneration via reduced expression of PITP alpha: positional complementation cloning and extragenic suppression."
Hamilton B.A., Smith D.J., Mueller K.L., Kerrebrock A.W., Bronson R.T., van Berkel V., Daly M.J., Kruglyak L., Reeve M.P., Nemhauser J.L., Hawkins T.L., Rubin E.M., Lander E.S.
Neuron 18:711-722(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ILS and ISS.
[3]"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. expand/collapse author list , 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.
Tissue: Medulla oblongata and Ovary.
[4]"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/6.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U96724 mRNA. Translation: AAC53265.1.
U96726 Genomic DNA. Translation: AAC60757.1.
AF483522 mRNA. Translation: AAL90796.1.
AF483523 mRNA. Translation: AAL90797.1.
AK054436 mRNA. Translation: BAC35778.1.
AK078104 mRNA. Translation: BAC37126.1.
BC066112 mRNA. Translation: AAH66112.1.
CCDSCCDS25053.1.
RefSeqNP_032942.1. NM_008916.2.
UniGeneMm.1458.

3D structure databases

ProteinModelPortalQ8C5L6.
SMRQ8C5L6. Positions 38-339.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ8C5L6.

Proteomic databases

MaxQBQ8C5L6.
PaxDbQ8C5L6.
PRIDEQ8C5L6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000006286; ENSMUSP00000006286; ENSMUSG00000006127.
GeneID19062.
KEGGmmu:19062.
UCSCuc007kek.1. mouse.

Organism-specific databases

CTD51763.
MGIMGI:1194899. Inpp5k.

Phylogenomic databases

eggNOGCOG5411.
GeneTreeENSGT00750000117675.
HOGENOMHOG000046051.
HOVERGENHBG082135.
InParanoidQ8C5L6.
KOK01106.
OMAGLYGYWG.
OrthoDBEOG79CXZB.
PhylomeDBQ8C5L6.
TreeFamTF317034.

Gene expression databases

ArrayExpressQ8C5L6.
BgeeQ8C5L6.
GenevestigatorQ8C5L6.

Family and domain databases

Gene3D3.60.10.10. 1 hit.
InterProIPR005135. Endo/exonuclease/phosphatase.
IPR000300. IPPc.
[Graphical view]
PfamPF03372. Exo_endo_phos. 1 hit.
[Graphical view]
SMARTSM00128. IPPc. 1 hit.
[Graphical view]
SUPFAMSSF56219. SSF56219. 1 hit.
ProtoNetSearch...

Other

NextBio295566.
PROQ8C5L6.
SOURCESearch...

Entry information

Entry nameINP5K_MOUSE
AccessionPrimary (citable) accession number: Q8C5L6
Secondary accession number(s): O09040
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: March 15, 2004
Last modified: July 9, 2014
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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