INPP_MOUSE
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-AUG-2022, entry version 164.
DE RecName: Full=Inositol polyphosphate 1-phosphatase {ECO:0000305};
DE Short=IPP;
DE Short=IPPase;
DE EC=3.1.3.57 {ECO:0000250|UniProtKB:P21327};
GN Name=Inpp1 {ECO:0000312|MGI:MGI:104848};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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 polyphosphate
RT 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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Mg(2+)-dependent phosphatase that catalyzes the hydrolysis of
CC the 1-position phosphate from inositol 1,4-bisphosphate and inositol
CC 1,3,4-trisphosphate and participates in inositol phosphate metabolism.
CC {ECO:0000250|UniProtKB:P21327}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,4-bisphosphate + H2O = 1D-myo-inositol 4-
CC phosphate + phosphate; Xref=Rhea:RHEA:15553, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58282, ChEBI:CHEBI:58469; EC=3.1.3.57;
CC Evidence={ECO:0000250|UniProtKB:P21327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15554;
CC Evidence={ECO:0000250|UniProtKB:P21327};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,3,4-trisphosphate + H2O = 1D-myo-inositol
CC 3,4-bisphosphate + phosphate; Xref=Rhea:RHEA:70319,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58414,
CC ChEBI:CHEBI:83241; Evidence={ECO:0000250|UniProtKB:P21327};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70320;
CC Evidence={ECO:0000250|UniProtKB:P21327};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P21327};
CC -!- ACTIVITY REGULATION: Inhibited by Li(+).
CC {ECO:0000250|UniProtKB:P21327}.
CC -!- PATHWAY: Signal transduction; phosphatidylinositol signaling pathway.
CC {ECO:0000250|UniProtKB:P21327}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P21327}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
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DR EMBL; U27295; AAA97574.1; -; mRNA.
DR EMBL; AK078382; BAC37245.1; -; mRNA.
DR EMBL; BC025072; AAH25072.1; -; mRNA.
DR CCDS; CCDS14947.1; -.
DR RefSeq; NP_032410.2; NM_008384.2.
DR RefSeq; XP_011236743.1; XM_011238441.2.
DR RefSeq; XP_011236744.1; XM_011238442.2.
DR AlphaFoldDB; P49442; -.
DR SMR; P49442; -.
DR BioGRID; 200767; 2.
DR IntAct; P49442; 2.
DR MINT; P49442; -.
DR STRING; 10090.ENSMUSP00000027271; -.
DR iPTMnet; P49442; -.
DR PhosphoSitePlus; P49442; -.
DR SwissPalm; P49442; -.
DR UCD-2DPAGE; P49442; -.
DR EPD; P49442; -.
DR jPOST; P49442; -.
DR MaxQB; P49442; -.
DR PaxDb; P49442; -.
DR PeptideAtlas; P49442; -.
DR PRIDE; P49442; -.
DR ProteomicsDB; 266993; -.
DR Antibodypedia; 34038; 151 antibodies from 22 providers.
DR DNASU; 16329; -.
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 VEuPathDB; HostDB:ENSMUSG00000026102; -.
DR eggNOG; KOG3099; Eukaryota.
DR GeneTree; ENSGT00940000156785; -.
DR HOGENOM; CLU_043868_2_0_1; -.
DR InParanoid; P49442; -.
DR OMA; ANIARVC; -.
DR OrthoDB; 1096950at2759; -.
DR PhylomeDB; P49442; -.
DR TreeFam; TF314300; -.
DR BRENDA; 3.1.3.57; 3474.
DR Reactome; R-MMU-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
DR UniPathway; UPA00944; -.
DR BioGRID-ORCS; 16329; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Inpp1; mouse.
DR PRO; PR:P49442; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P49442; protein.
DR Bgee; ENSMUSG00000026102; Expressed in granulocyte and 243 other tissues.
DR ExpressionAtlas; P49442; baseline and differential.
DR Genevisible; P49442; MM.
DR GO; GO:0052829; F:inositol-1,3,4-trisphosphate 1-phosphatase activity; ISS:UniProtKB.
DR GO; GO:0004441; F:inositol-1,4-bisphosphate 1-phosphatase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IBA:GO_Central.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR Gene3D; 4.10.460.10; -; 1.
DR InterPro; IPR020583; Inositol_monoP_metal-BS.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR InterPro; IPR020550; Inositol_monophosphatase_CS.
DR InterPro; IPR044897; INPP1_dom_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 Hydrolase; Lithium; Magnesium; Metal-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..396
FT /note="Inositol polyphosphate 1-phosphatase"
FT /id="PRO_0000142511"
FT BINDING 54
FT /ligand="Li(+)"
FT /ligand_id="ChEBI:CHEBI:49713"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000250|UniProtKB:P21327"
FT BINDING 79
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P21327"
FT BINDING 80
FT /ligand="Li(+)"
FT /ligand_id="ChEBI:CHEBI:49713"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000250|UniProtKB:P21327"
FT BINDING 153
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P21327"
FT BINDING 153
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P21327"
FT BINDING 155
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P21327"
FT BINDING 156
FT /ligand="1D-myo-inositol 1,4-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58282"
FT /evidence="ECO:0000250|UniProtKB:P21327"
FT BINDING 157
FT /ligand="1D-myo-inositol 1,4-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58282"
FT /evidence="ECO:0000250|UniProtKB:P21327"
FT BINDING 158
FT /ligand="1D-myo-inositol 1,4-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58282"
FT /evidence="ECO:0000250|UniProtKB:P21327"
FT BINDING 264
FT /ligand="1D-myo-inositol 1,4-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58282"
FT /evidence="ECO:0000250|UniProtKB:P21327"
FT BINDING 266
FT /ligand="1D-myo-inositol 1,4-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58282"
FT /evidence="ECO:0000250|UniProtKB:P21327"
FT BINDING 286
FT /ligand="1D-myo-inositol 1,4-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58282"
FT /evidence="ECO:0000250|UniProtKB:P21327"
FT BINDING 287
FT /ligand="1D-myo-inositol 1,4-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58282"
FT /evidence="ECO:0000250|UniProtKB:P21327"
FT BINDING 290
FT /ligand="1D-myo-inositol 1,4-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58282"
FT /evidence="ECO:0000250|UniProtKB:P21327"
FT BINDING 308
FT /ligand="1D-myo-inositol 1,4-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58282"
FT /evidence="ECO:0000250|UniProtKB:P21327"
FT BINDING 313
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P21327"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49441"
FT CONFLICT 10
FT /note="C -> R (in Ref. 1; AAA97574)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="V -> A (in Ref. 1; AAA97574)"
FT /evidence="ECO:0000305"
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
