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P49442 (INPP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
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 1-phosphatase
Short name=IPP
Short name=IPPase
EC=3.1.3.57
Gene names
Name:Inpp1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length396 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

Magnesium.

Enzyme regulation

Inhibited by Li+ By similarity.

Pathway

Signal transduction; phosphatidylinositol signaling pathway.

Subunit structure

Monomer By similarity.

Sequence similarities

Belongs to the inositol monophosphatase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 396396Inositol polyphosphate 1-phosphatase
PRO_0000142511

Regions

Region155 – 1584Substrate binding By similarity

Sites

Metal binding791Magnesium 1 By similarity
Metal binding1531Magnesium 1 By similarity
Metal binding1531Magnesium 2 By similarity
Metal binding1551Magnesium 1; via carbonyl oxygen By similarity
Metal binding1561Magnesium 2 By similarity
Metal binding3131Magnesium 2 By similarity
Binding site1191Substrate By similarity
Binding site3131Substrate By similarity

Amino acid modifications

Modified residue3141Phosphoserine By similarity

Experimental info

Sequence conflict101C → R in AAA97574. Ref.1
Sequence conflict2761V → A in AAA97574. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P49442 [UniParc].

Last modified August 31, 2004. Version 2.
Checksum: 799D555B153FC975

FASTA39643,346
        10         20         30         40         50         60 
MSDILLELLC VSEKAANIAR ACRQQETLFQ LLIEEKKGAE KNKKFAADFK TLADVLVQEV 

        70         80         90        100        110        120 
IKQNMENKFP GLGKKVFGEE SNEFTNDLGE KITVELQSTE EETAELLSKV LNGNMPASEA 

       130        140        150        160        170        180 
LAQVVHEDVD LTDPTLESLD ISIPHESLGI WVDPIDSTYQ YIKGSANVKS NQGIFPSGLQ 

       190        200        210        220        230        240 
CVTILIGVYD LQTGLPLMGV INQPFASQNL TTLRWKGQCY WGLSYMGTNI HSLQLAISKS 

       250        260        270        280        290        300 
DSETQTENSD REFSSPFSAV ISTSEKDTIK AALSRVCGGS VFPAAGAGYK SLCVIQGLAD 

       310        320        330        340        350        360 
IYIFSEDTTY KWDSCAAHAI LRAMGGGIVD MKECLERSPD TGLDLPQLLY HVENKGASGV 

       370        380        390 
ELWANKGGLI AYRSRNRLDT FLSRLIQNLG PVKTQA

« Hide

References

« Hide 'large scale' references
[1]"Identification and chromosomal mapping of the mouse inositol polyphosphate 1-phosphatase gene."
Okabe I., Nussbaum R.L.
Genomics 30:358-360(1995) [PubMed: 8586440] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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. 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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Cerebellum.
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U27295 mRNA. Translation: AAA97574.1.
AK078382 mRNA. Translation: BAC37245.1.
BC025072 mRNA. Translation: AAH25072.1.
IPIIPI00114801.
RefSeqNP_032410.2. NM_008384.2.
UniGeneMm.917.

3D structure databases

ProteinModelPortalP49442.
SMRP49442. Positions 1-395.
ModBaseSearch...

Protein-protein interaction databases

IntActP49442. 1 interaction.
STRINGP49442.

PTM databases

PhosphoSiteP49442.

2D gel databases

UCD-2DPAGEP49442.

Proteomic databases

PRIDEP49442.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027271; ENSMUSP00000027271; ENSMUSG00000026102.
GeneID16329.
KEGGmmu:16329.
UCSCuc007ayo.2. mouse.

Organism-specific databases

CTD3628.
MGIMGI:104848. Inpp1.

Phylogenomic databases

eggNOGroNOG15512.
GeneTreeENSGT00390000014061.
HOGENOMHBG443765.
HOVERGENHBG006163.
InParanoidP49442.
OMAECLERNP.
OrthoDBEOG41C6WB.
PhylomeDBP49442.

Enzyme and pathway databases

BRENDA3.1.3.57. 3474.

Gene expression databases

ArrayExpressP49442.
BgeeP49442.
CleanExMM_INPP1.
GenevestigatorP49442.
GermOnlineENSMUSG00000026102. Mus musculus.

Family and domain databases

InterProIPR020583. Inositol_monoP_metal-BS.
IPR000760. Inositol_monophosphatase.
IPR020550. Inositol_monophosphatase_CS.
[Graphical view]
KOK01107.
PANTHERPTHR20854. Inositol_P. 1 hit.
PfamPF00459. Inositol_P. 1 hit.
[Graphical view]
PROSITEPS00629. IMP_1. 1 hit.
PS00630. IMP_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio289410.
SOURCESearch...

Entry information

Entry nameINPP_MOUSE
AccessionPrimary (citable) accession number: P49442
Secondary accession number(s): Q8R3L1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: August 31, 2004
Last modified: November 16, 2011
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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