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Protein

Inositol monophosphatase 1

Gene

Impa1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Responsible for the provision of inositol required for synthesis of phosphatidylinositol and polyphosphoinositides and has been implicated as the pharmacological target for lithium action in brain. Has broad substrate specificity and can use myo-inositol monophosphates, myo-inositol 1,3-diphosphate, myo-inositol 1,4-diphosphate, scyllo-inositol-phosphate, D-galactose 1-phosphate, glucose-1-phosphate, glucose-6-phosphate, fructose-1-phosphate, beta-glycerophosphate, and 2'-AMP as substrates.By similarity

Catalytic activityi

Myo-inositol phosphate + H2O = myo-inositol + phosphate.By similarity
Alpha-D-galactose 1-phosphate + H2O = D-galactose + phosphate.By similarity

Cofactori

Mg2+1 Publication

Enzyme regulationi

Inhibited by Li+, Ca2+ and Mn2+, but also by Mg2+ at concentrations above 3 mM.By similarity

Pathway:imyo-inositol biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes myo-inositol from D-glucose 6-phosphate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Inositol-3-phosphate synthase 1 (Isyna1)
  2. Inositol monophosphatase 1 (Impa1), Inositol monophosphatase 2 (Impa2), Inositol monophosphatase 3 (Impad1)
This subpathway is part of the pathway myo-inositol biosynthesis, which is itself part of Polyol metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes myo-inositol from D-glucose 6-phosphate, the pathway myo-inositol biosynthesis and in Polyol metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi70 – 701Magnesium 1; catalytic1 Publication
Binding sitei70 – 701SubstrateCurated
Metal bindingi90 – 901Magnesium 1; catalytic1 Publication
Metal bindingi90 – 901Magnesium 21 Publication
Metal bindingi92 – 921Magnesium 1; via carbonyl oxygen; catalytic1 Publication
Metal bindingi93 – 931Magnesium 21 Publication
Binding sitei213 – 2131SubstrateBy similarity
Metal bindingi220 – 2201Magnesium 21 Publication
Binding sitei220 – 2201SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Lithium, Magnesium, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00823; UER00788.

Names & Taxonomyi

Protein namesi
Recommended name:
Inositol monophosphatase 1 (EC:3.1.3.25By similarity)
Short name:
IMP 1
Short name:
IMPase 1
Alternative name(s):
D-galactose 1-phosphate phosphataseBy similarity (EC:3.1.3.94By similarity)
Inositol-1(or 4)-monophosphatase 1
Lithium-sensitive myo-inositol monophosphatase A1
Gene namesi
Name:Impa1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1933158. Impa1.

Subcellular locationi

  • Cytoplasm By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 277277Inositol monophosphatase 1PRO_0000142514Add
BLAST

Proteomic databases

MaxQBiO55023.
PaxDbiO55023.
PRIDEiO55023.

PTM databases

PhosphoSiteiO55023.

Expressioni

Tissue specificityi

Mostly expressed in brain, small intestine, testis, kidney, and spleen (at protein level).1 Publication

Inductioni

By lithium Li+ in hippocamp.1 Publication

Gene expression databases

CleanExiMM_IMPA1.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

IntActiO55023. 1 interaction.
STRINGi10090.ENSMUSP00000068174.

Structurei

Secondary structure

1
277
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 2623Combined sources
Beta strandi34 – 385Combined sources
Helixi45 – 6117Combined sources
Beta strandi65 – 695Combined sources
Helixi70 – 745Combined sources
Beta strandi86 – 938Combined sources
Helixi95 – 1006Combined sources
Beta strandi106 – 1138Combined sources
Beta strandi116 – 1249Combined sources
Turni125 – 1284Combined sources
Beta strandi129 – 1346Combined sources
Turni135 – 1373Combined sources
Beta strandi138 – 1414Combined sources
Helixi154 – 1563Combined sources
Beta strandi158 – 1603Combined sources
Helixi169 – 18315Combined sources
Turni184 – 1863Combined sources
Beta strandi188 – 1925Combined sources
Helixi196 – 2049Combined sources
Beta strandi207 – 2159Combined sources
Helixi218 – 23013Combined sources
Beta strandi234 – 2363Combined sources
Beta strandi240 – 2423Combined sources
Beta strandi247 – 2548Combined sources
Helixi256 – 26510Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4AS5X-ray2.43A/B/C/D1-277[»]
ProteinModelPortaliO55023.
SMRiO55023. Positions 3-276.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni90 – 956Substrate bindingCurated
Regioni194 – 1963Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the inositol monophosphatase family.Curated

Phylogenomic databases

eggNOGiCOG0483.
HOGENOMiHOG000282238.
HOVERGENiHBG052123.
InParanoidiO55023.
PhylomeDBiO55023.

Family and domain databases

InterProiIPR020583. Inositol_monoP_metal-BS.
IPR020552. Inositol_monoPase_Li-sen.
IPR000760. Inositol_monophosphatase.
IPR020550. Inositol_monophosphatase_CS.
[Graphical view]
PANTHERiPTHR20854. PTHR20854. 1 hit.
PfamiPF00459. Inositol_P. 1 hit.
[Graphical view]
PRINTSiPR00377. IMPHPHTASES.
PR00378. LIIMPHPHTASE.
PROSITEiPS00629. IMP_1. 1 hit.
PS00630. IMP_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O55023-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADPWQECMD YAVILARQAG EMIREALKNE MDVMIKSSPA DLVTVTDQKV
60 70 80 90 100
EKMLMSSIKE KYPCHSFIGE ESVAAGEKTV FTESPTWFID PIDGTTNFVH
110 120 130 140 150
RFPFVAVSIG FLVNKEMEFG IVYSCVEDKM YTGRKGKGAF CNGQKLQVSQ
160 170 180 190 200
QEDITKSLLV TELGSSRKPE TLRIVLSNME KLCSIPIHGI RSVGTAAVNM
210 220 230 240 250
CLVATGGADA YYEMGIHCWD MAGAGIIVTE AGGVLMDVTG GPFDLMSRRI
260 270
IAANSITLAK RIAKEIEIIP LQRDDES
Length:277
Mass (Da):30,436
Last modified:June 1, 1998 - v1
Checksum:iEDBDB7BD24748E9D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF042730 mRNA. Translation: AAB97469.1.
CCDSiCCDS17240.1.
UniGeneiMm.183042.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF042730 mRNA. Translation: AAB97469.1.
CCDSiCCDS17240.1.
UniGeneiMm.183042.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4AS5X-ray2.43A/B/C/D1-277[»]
ProteinModelPortaliO55023.
SMRiO55023. Positions 3-276.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO55023. 1 interaction.
STRINGi10090.ENSMUSP00000068174.

PTM databases

PhosphoSiteiO55023.

Proteomic databases

MaxQBiO55023.
PaxDbiO55023.
PRIDEiO55023.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:1933158. Impa1.

Phylogenomic databases

eggNOGiCOG0483.
HOGENOMiHOG000282238.
HOVERGENiHBG052123.
InParanoidiO55023.
PhylomeDBiO55023.

Enzyme and pathway databases

UniPathwayiUPA00823; UER00788.

Miscellaneous databases

ChiTaRSiImpa1. mouse.
PROiO55023.
SOURCEiSearch...

Gene expression databases

CleanExiMM_IMPA1.

Family and domain databases

InterProiIPR020583. Inositol_monoP_metal-BS.
IPR020552. Inositol_monoPase_Li-sen.
IPR000760. Inositol_monophosphatase.
IPR020550. Inositol_monophosphatase_CS.
[Graphical view]
PANTHERiPTHR20854. PTHR20854. 1 hit.
PfamiPF00459. Inositol_P. 1 hit.
[Graphical view]
PRINTSiPR00377. IMPHPHTASES.
PR00378. LIIMPHPHTASE.
PROSITEiPS00629. IMP_1. 1 hit.
PS00630. IMP_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Parthasarathy L., Parthasarathy R., Vadnal R.E.
    Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "The effect of lithium on expression of genes for inositol biosynthetic enzymes in mouse hippocampus; a comparison with the yeast model."
    Shamir A., Shaltiel G., Greenberg M.L., Belmaker R.H., Agam G.
    Brain Res. Mol. Brain Res. 115:104-110(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  3. "Spatial expression patterns and biochemical properties distinguish a second myo-inositol monophosphatase IMPA2 from IMPA1."
    Ohnishi T., Ohba H., Seo K.-C., Im J., Sato Y., Iwayama Y., Furuichi T., Chung S.-K., Yoshikawa T.
    J. Biol. Chem. 282:637-646(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  4. "Cloning, expression, purification, crystallization and X-ray analysis of inositol monophosphatase from Mus musculus and Homo sapiens."
    Singh N., Halliday A.C., Knight M., Lack N.A., Lowe E., Churchill G.C.
    Acta Crystallogr. F 68:1149-1152(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.43 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND PHOSPHATE, SUBUNIT, COFACTOR.

Entry informationi

Entry nameiIMPA1_MOUSE
AccessioniPrimary (citable) accession number: O55023
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 1, 1998
Last modified: June 24, 2015
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.