Q8C5L6 (INP5K_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	468 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Endoplasmic reticulum
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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 insulin stimulus Inferred from sequence or structural similarity. Source: UniProtKB cellular response to tumor necrosis factor Inferred from sequence or structural similarity. 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 cascade Inferred from mutant phenotype PubMed 19250614. Source: UniProtKB negative regulation of protein targeting to membrane Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of retroviral genome replication 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-dependent Inferred from direct assay PubMed 21938401. Source: UniProtKB phosphatidylinositol dephosphorylation Inferred from sequence or structural similarity. Source: UniProtKB phosphatidylinositol phosphorylation Inferred from electronic annotation. Source: InterPro positive regulation of renal water transport Inferred from direct assay PubMed 21938401. Source: UniProtKB positive regulation of transcription, DNA-dependent 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 ruffle assembly Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytosol Inferred from sequence or structural similarity. Source: UniProtKB endoplasmic reticulum 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 ruffle membrane Inferred from sequence or structural similarity. Source: UniProtKB trans-Golgi network Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	inositol 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: EC inositol-1,4,5-trisphosphate 5-phosphatase activity Inferred from electronic annotation. Source: EC inositol-polyphosphate 5-phosphatase activity Inferred from electronic annotation. Source: EC 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 468	468	Inositol polyphosphate 5-phosphatase K		PRO_0000209728
Regions
	Region	34 – 337	304	Catalytic Potential
	Region	340 – 468	129	Required for ruffle localization UniProtKB Q9BT40
Experimental info
	Sequence conflict	329	1	D → E in BAC37126. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q8C5L6 [UniParc]. Last modified March 15, 2004. Version 2. Checksum: F2E1CA370B97A8A1	FASTA	468	54,159
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00113796.
RefSeq	NP_032942.1. NM_008916.2.
UniGene	Mm.1458.
3D structure databases
ProteinModelPortal	Q8C5L6.
SMR	Q8C5L6. Positions 38-339.
ModBase	Search...
PTM databases
PhosphoSite	Q8C5L6.
Proteomic databases
PaxDb	Q8C5L6.
PRIDE	Q8C5L6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000006286; ENSMUSP00000006286; ENSMUSG00000006127.
GeneID	19062.
KEGG	mmu:19062.
Organism-specific databases
CTD	51763.
MGI	MGI:1194899. Inpp5k.
Phylogenomic databases
eggNOG	COG5411.
GeneTree	ENSGT00700000104268.
HOGENOM	HOG000046051.
HOVERGEN	HBG082135.
InParanoid	Q8C5L6.
KO	K01106.
OMA	TEDQFLL.
OrthoDB	EOG4NZTTB.
Gene expression databases
ArrayExpress	Q8C5L6.
Bgee	Q8C5L6.
Genevestigator	Q8C5L6.
GermOnline	ENSMUSG00000006127. 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]
SUPFAM	SSF56219. Exo_endo_phos. 1 hit.
ProtoNet	Search...
Other
NextBio	295566.
SOURCE	Search...

Entry information

Entry name

INP5K_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 83 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program