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Protein

Inositol monophosphatase 1

Gene

IMPA1

Organism
Bos taurus (Bovine)
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, glucose-1-phosphate, glucose-6-phosphate, fructose-1-phosphate, beta-glycerophosphate, and 2'-AMP as substrates (By similarity). Is equally active with myo-inositol monophosphate and D-galactose 1-phosphate.By similarity1 Publication

Catalytic activityi

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

Cofactori

Mg2+1 Publication1 Publication

Enzyme regulationi

Activity with myo-inositol monophosphate and D-galactose 1-phosphate is inhibited by Li+, Ca2+ and Mn2+, but also by Mg2+ at concentrations above 3 mM.1 Publication

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 3 (IMPAD1), Inositol monophosphatase 1 (IMPA1)
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 – 701SubstrateBy similarity
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

  • inositol monophosphate 1-phosphatase activity Source: GO_Central
  • inositol monophosphate 3-phosphatase activity Source: UniProtKB-EC
  • inositol monophosphate 4-phosphatase activity Source: UniProtKB-EC
  • inositol monophosphate phosphatase activity Source: UniProtKB
  • lithium ion binding Source: UniProtKB
  • magnesium ion binding Source: UniProtKB
  • manganese ion binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Lithium, Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAi3.1.3.25. 908.
ReactomeiR-BTA-1855183. Synthesis of IP2, IP, and Ins in the cytosol.
SABIO-RKP20456.
UniPathwayiUPA00823; UER00788.

Names & Taxonomyi

Protein namesi
Recommended name:
Inositol monophosphatase 1 (EC:3.1.3.251 Publication)
Short name:
IMP 1
Short name:
IMPase 1
Alternative name(s):
D-galactose 1-phosphate phosphatase1 Publication (EC:3.1.3.941 Publication)
Inositol-1(or 4)-monophosphatase 1
Lithium-sensitive myo-inositol monophosphatase A1
Gene namesi
Name:IMPA1
Synonyms:IMPA
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 14

Subcellular locationi

  • Cytoplasm By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL4505.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 277277Inositol monophosphatase 1PRO_0000142512Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei168 – 1681PhosphothreonineBy similarity

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP20456.
PRIDEiP20456.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000015548.

Chemistry

BindingDBiP20456.

Structurei

Secondary structure

1
277
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 2825Combined sources
Beta strandi33 – 353Combined sources
Beta strandi42 – 443Combined 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 – 1914Combined sources
Helixi196 – 2049Combined sources
Beta strandi207 – 2159Combined sources
Helixi218 – 23013Combined sources
Beta strandi234 – 2363Combined sources
Beta strandi240 – 2423Combined sources
Beta strandi247 – 2559Combined sources
Helixi256 – 26510Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BJIX-ray1.30A/B1-277[»]
ProteinModelPortaliP20456.
SMRiP20456. Positions 3-276.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20456.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni92 – 954Substrate bindingBy similarity
Regioni194 – 1963Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the inositol monophosphatase family.Curated

Phylogenomic databases

eggNOGiKOG2951. Eukaryota.
COG0483. LUCA.
GeneTreeiENSGT00390000014699.
HOGENOMiHOG000282238.
HOVERGENiHBG052123.
InParanoidiP20456.
KOiK01092.
OMAiKIEFGIV.
OrthoDBiEOG7RJPS8.
TreeFamiTF313194.

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.

P20456-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADPWQECMD YAVTLAGQAG EVVREALKNE MNIMVKSSPA DLVTATDQKV
60 70 80 90 100
EKMLITSIKE KYPSHSFIGE ESVAAGEKSI LTDNPTWIID PIDGTTNFVH
110 120 130 140 150
GFPFVAVSIG FVVNKKMEFG IVYSCLEDKM YTGRKGKGAF CNGQKLQVSH
160 170 180 190 200
QEDITKSLLV TELGSSRTPE TVRIILSNIE RLLCLPIHGI RGVGTAALNM
210 220 230 240 250
CLVAAGAADA YYEMGIHCWD VAGAGIIVTE AGGVLLDVTG GPFDLMSRRV
260 270
IASSNKTLAE RIAKEIQIIP LQRDDED
Length:277
Mass (Da):30,056
Last modified:February 1, 1991 - v1
Checksum:i773DDB0291AC5977
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05394 mRNA. Translation: AAA30589.1.
BC118411 mRNA. Translation: AAI18412.1.
PIRiA35223.
RefSeqiNP_776786.1. NM_174361.4.
XP_005215709.1. XM_005215652.3.
XP_015330015.1. XM_015474529.1.
XP_015330016.1. XM_015474530.1.
UniGeneiBt.424.

Genome annotation databases

EnsembliENSBTAT00000015548; ENSBTAP00000015548; ENSBTAG00000011709.
GeneIDi281865.
KEGGibta:281865.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05394 mRNA. Translation: AAA30589.1.
BC118411 mRNA. Translation: AAI18412.1.
PIRiA35223.
RefSeqiNP_776786.1. NM_174361.4.
XP_005215709.1. XM_005215652.3.
XP_015330015.1. XM_015474529.1.
XP_015330016.1. XM_015474530.1.
UniGeneiBt.424.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BJIX-ray1.30A/B1-277[»]
ProteinModelPortaliP20456.
SMRiP20456. Positions 3-276.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000015548.

Chemistry

BindingDBiP20456.
ChEMBLiCHEMBL4505.

Proteomic databases

PaxDbiP20456.
PRIDEiP20456.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000015548; ENSBTAP00000015548; ENSBTAG00000011709.
GeneIDi281865.
KEGGibta:281865.

Organism-specific databases

CTDi3612.

Phylogenomic databases

eggNOGiKOG2951. Eukaryota.
COG0483. LUCA.
GeneTreeiENSGT00390000014699.
HOGENOMiHOG000282238.
HOVERGENiHBG052123.
InParanoidiP20456.
KOiK01092.
OMAiKIEFGIV.
OrthoDBiEOG7RJPS8.
TreeFamiTF313194.

Enzyme and pathway databases

UniPathwayiUPA00823; UER00788.
BRENDAi3.1.3.25. 908.
ReactomeiR-BTA-1855183. Synthesis of IP2, IP, and Ins in the cytosol.
SABIO-RKP20456.

Miscellaneous databases

EvolutionaryTraceiP20456.

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

« Hide 'large scale' publications
  1. "Cloning and expression of bovine brain inositol monophosphatase."
    Diehl R.E., Whiting P., Potter J., Gee N., Ragan C.I., Linemeyer D., Schoepfer R., Bennett C., Dixon R.A.F.
    J. Biol. Chem. 265:5946-5949(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Brain.
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Fetal pons.
  3. "Brain inositol monophosphatase identified as a galactose 1-phosphatase."
    Parthasarathy R., Parthasarathy L., Vadnal R.
    Brain Res. 778:99-106(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, SUBUNIT.
  4. "High-resolution structure of myo-inositol monophosphatase, the putative target of lithium therapy."
    Gill R., Mohammed F., Badyal R., Coates L., Erskine P., Thompson D., Cooper J., Gore M., Wood S.
    Acta Crystallogr. D 61:545-555(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS, COFACTOR, SUBUNIT.

Entry informationi

Entry nameiIMPA1_BOVIN
AccessioniPrimary (citable) accession number: P20456
Secondary accession number(s): Q17QE4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: July 6, 2016
This is version 135 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, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.