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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

Pathwayi: myo-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)DescriptionActionsGraphical viewLength
Metal bindingi70Magnesium 1; catalytic1 Publication1
Binding sitei70SubstrateCurated1
Metal bindingi90Magnesium 1; catalytic1 Publication1
Metal bindingi90Magnesium 21 Publication1
Metal bindingi92Magnesium 1; via carbonyl oxygen; catalytic1 Publication1
Metal bindingi93Magnesium 21 Publication1
Binding sitei213SubstrateBy similarity1
Metal bindingi220Magnesium 21 Publication1
Binding sitei220SubstrateBy similarity1

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
Proteomesi
  • UP000000589 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)DescriptionActionsGraphical viewLength
ChainiPRO_00001425141 – 277Inositol monophosphatase 1Add BLAST277

Proteomic databases

EPDiO55023.
MaxQBiO55023.
PaxDbiO55023.
PeptideAtlasiO55023.
PRIDEiO55023.

PTM databases

iPTMnetiO55023.
PhosphoSitePlusiO55023.
SwissPalmiO55023.

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

GO - Molecular functioni

Protein-protein interaction databases

IntActiO55023. 2 interactors.
STRINGi10090.ENSMUSP00000068174.

Structurei

Secondary structure

1277
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 26Combined sources23
Beta strandi34 – 38Combined sources5
Helixi45 – 61Combined sources17
Beta strandi65 – 69Combined sources5
Helixi70 – 74Combined sources5
Beta strandi86 – 93Combined sources8
Helixi95 – 100Combined sources6
Beta strandi106 – 113Combined sources8
Beta strandi116 – 124Combined sources9
Turni125 – 128Combined sources4
Beta strandi129 – 134Combined sources6
Turni135 – 137Combined sources3
Beta strandi138 – 141Combined sources4
Helixi154 – 156Combined sources3
Beta strandi158 – 160Combined sources3
Helixi169 – 183Combined sources15
Turni184 – 186Combined sources3
Beta strandi188 – 192Combined sources5
Helixi196 – 204Combined sources9
Beta strandi207 – 215Combined sources9
Helixi218 – 230Combined sources13
Beta strandi234 – 236Combined sources3
Beta strandi240 – 242Combined sources3
Beta strandi247 – 254Combined sources8
Helixi256 – 265Combined sources10

3D structure databases

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

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni90 – 95Substrate bindingCurated6
Regioni194 – 196Substrate bindingBy similarity3

Sequence similaritiesi

Belongs to the inositol monophosphatase family.Curated

Phylogenomic databases

eggNOGiKOG2951. Eukaryota.
COG0483. LUCA.
HOGENOMiHOG000282238.
HOVERGENiHBG052123.
InParanoidiO55023.
PhylomeDBiO55023.

Family and domain databases

CDDicd01639. IMPase. 1 hit.
InterProiIPR033942. IMPase.
IPR020583. Inositol_monoP_metal-BS.
IPR020552. Inositol_monoPase_Li-sen.
IPR000760. Inositol_monophosphatase-like.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4AS5X-ray2.43A/B/C/D1-277[»]
ProteinModelPortaliO55023.
SMRiO55023.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO55023. 2 interactors.
STRINGi10090.ENSMUSP00000068174.

PTM databases

iPTMnetiO55023.
PhosphoSitePlusiO55023.
SwissPalmiO55023.

Proteomic databases

EPDiO55023.
MaxQBiO55023.
PaxDbiO55023.
PeptideAtlasiO55023.
PRIDEiO55023.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:1933158. Impa1.

Phylogenomic databases

eggNOGiKOG2951. Eukaryota.
COG0483. LUCA.
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

CDDicd01639. IMPase. 1 hit.
InterProiIPR033942. IMPase.
IPR020583. Inositol_monoP_metal-BS.
IPR020552. Inositol_monoPase_Li-sen.
IPR000760. Inositol_monophosphatase-like.
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...

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: November 30, 2016
This is version 129 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

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 one 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.