ID INPP_MOUSE Reviewed; 396 AA.
AC P49442; Q8R3L1;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-APR-2013, entry version 105.
DE RecName: Full=Inositol polyphosphate 1-phosphatase;
DE Short=IPP;
DE Short=IPPase;
DE EC=3.1.3.57;
GN Name=Inpp1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8586440; DOI=10.1006/geno.1995.0030;
RA Okabe I., Nussbaum R.L.;
RT "Identification and chromosomal mapping of the mouse inositol
RT polyphosphate 1-phosphatase gene.";
RL Genomics 30:358-360(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- CATALYTIC ACTIVITY: 1D-myo-inositol 1,4-bisphosphate + H(2)O = 1D-
CC myo-inositol 4-phosphate + phosphate.
CC -!- COFACTOR: Magnesium.
CC -!- ENZYME REGULATION: Inhibited by Li(+) (By similarity).
CC -!- PATHWAY: Signal transduction; phosphatidylinositol signaling
CC pathway.
CC -!- SUBUNIT: Monomer (By similarity).
CC -!- SIMILARITY: Belongs to the inositol monophosphatase family.
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DR EMBL; U27295; AAA97574.1; -; mRNA.
DR EMBL; AK078382; BAC37245.1; -; mRNA.
DR EMBL; BC025072; AAH25072.1; -; mRNA.
DR IPI; IPI00114801; -.
DR RefSeq; NP_032410.2; NM_008384.2.
DR UniGene; Mm.917; -.
DR ProteinModelPortal; P49442; -.
DR SMR; P49442; 1-395.
DR IntAct; P49442; 1.
DR STRING; 10090.ENSMUSP00000027271; -.
DR PhosphoSite; P49442; -.
DR UCD-2DPAGE; P49442; -.
DR PaxDb; P49442; -.
DR PRIDE; P49442; -.
DR Ensembl; ENSMUST00000027271; ENSMUSP00000027271; ENSMUSG00000026102.
DR GeneID; 16329; -.
DR KEGG; mmu:16329; -.
DR UCSC; uc007ayo.2; mouse.
DR CTD; 3628; -.
DR MGI; MGI:104848; Inpp1.
DR eggNOG; NOG306469; -.
DR GeneTree; ENSGT00390000014061; -.
DR HOGENOM; HOG000007839; -.
DR HOVERGEN; HBG006163; -.
DR InParanoid; P49442; -.
DR KO; K01107; -.
DR OMA; TFKWDSC; -.
DR OrthoDB; EOG41C6WB; -.
DR BRENDA; 3.1.3.57; 3474.
DR UniPathway; UPA00944; -.
DR NextBio; 289410; -.
DR ArrayExpress; P49442; -.
DR Bgee; P49442; -.
DR CleanEx; MM_INPP1; -.
DR Genevestigator; P49442; -.
DR GermOnline; ENSMUSG00000026102; Mus musculus.
DR GO; GO:0004441; F:inositol-1,4-bisphosphate 1-phosphatase activity; IEA:EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046854; P:phosphatidylinositol phosphorylation; IEA:InterPro.
DR InterPro; IPR020583; Inositol_monoP_metal-BS.
DR InterPro; IPR000760; Inositol_monophosphatase.
DR InterPro; IPR020550; Inositol_monophosphatase_CS.
DR PANTHER; PTHR20854; PTHR20854; 1.
DR Pfam; PF00459; Inositol_P; 1.
DR PROSITE; PS00629; IMP_1; 1.
DR PROSITE; PS00630; IMP_2; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Hydrolase; Lithium; Magnesium; Metal-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1 396 Inositol polyphosphate 1-phosphatase.
FT /FTId=PRO_0000142511.
FT REGION 155 158 Substrate binding (By similarity).
FT METAL 79 79 Magnesium 1 (By similarity).
FT METAL 153 153 Magnesium 1 (By similarity).
FT METAL 153 153 Magnesium 2 (By similarity).
FT METAL 155 155 Magnesium 1; via carbonyl oxygen (By
FT similarity).
FT METAL 156 156 Magnesium 2 (By similarity).
FT METAL 313 313 Magnesium 2 (By similarity).
FT BINDING 119 119 Substrate (By similarity).
FT BINDING 313 313 Substrate (By similarity).
FT MOD_RES 314 314 Phosphoserine (By similarity).
FT CONFLICT 10 10 C -> R (in Ref. 1; AAA97574).
FT CONFLICT 276 276 V -> A (in Ref. 1; AAA97574).
SQ SEQUENCE 396 AA; 43346 MW; 799D555B153FC975 CRC64;
MSDILLELLC VSEKAANIAR ACRQQETLFQ LLIEEKKGAE KNKKFAADFK TLADVLVQEV
IKQNMENKFP GLGKKVFGEE SNEFTNDLGE KITVELQSTE EETAELLSKV LNGNMPASEA
LAQVVHEDVD LTDPTLESLD ISIPHESLGI WVDPIDSTYQ YIKGSANVKS NQGIFPSGLQ
CVTILIGVYD LQTGLPLMGV INQPFASQNL TTLRWKGQCY WGLSYMGTNI HSLQLAISKS
DSETQTENSD REFSSPFSAV ISTSEKDTIK AALSRVCGGS VFPAAGAGYK SLCVIQGLAD
IYIFSEDTTY KWDSCAAHAI LRAMGGGIVD MKECLERSPD TGLDLPQLLY HVENKGASGV
ELWANKGGLI AYRSRNRLDT FLSRLIQNLG PVKTQA
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