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Protein

Inositol monophosphatase 1

Gene

IMPA1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: -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-1-monophosphatase (IMPA1), Inositol-1-monophosphatase (IMPA2), 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)DescriptionActionsGraphical viewLength
Metal bindingi70Magnesium 1; catalytic1 Publication1
Binding sitei70SubstrateBy similarity1
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

  • 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
  • protein homodimerization activity Source: Ensembl

GO - Biological processi

Keywordsi

Molecular functionHydrolase
LigandLithium, 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-RKiP20456
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

Organism-specific databases

VGNCiVGNC:30184 IMPA1

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL4505

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001425121 – 277Inositol monophosphatase 1Add BLAST277

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei168PhosphothreonineBy similarity1

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP20456
PRIDEiP20456

Expressioni

Gene expression databases

BgeeiENSBTAG00000011709

Interactioni

Subunit structurei

Homodimer.2 Publications

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000015548

Chemistry databases

BindingDBiP20456

Structurei

Secondary structure

1277
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 28Combined sources25
Beta strandi33 – 35Combined sources3
Beta strandi42 – 44Combined sources3
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 – 191Combined sources4
Helixi196 – 204Combined sources9
Beta strandi207 – 215Combined sources9
Helixi218 – 230Combined sources13
Beta strandi234 – 236Combined sources3
Beta strandi240 – 242Combined sources3
Beta strandi247 – 255Combined sources9
Helixi256 – 265Combined sources10

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP20456

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni92 – 95Substrate bindingBy similarity4
Regioni194 – 196Substrate bindingBy similarity3

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2951 Eukaryota
COG0483 LUCA
GeneTreeiENSGT00390000014699
HOGENOMiHOG000282238
HOVERGENiHBG052123
InParanoidiP20456
KOiK01092
OMAiNNYAEFC
OrthoDBiEOG091G0D21
TreeFamiTF313194

Family and domain databases

CDDicd01639 IMPase, 1 hit
InterProiView protein in InterPro
IPR033942 IMPase
IPR020583 Inositol_monoP_metal-BS
IPR020552 Inositol_monoPase_Li-sen
IPR000760 Inositol_monophosphatase-like
IPR020550 Inositol_monophosphatase_CS
PfamiView protein in Pfam
PF00459 Inositol_P, 1 hit
PRINTSiPR00377 IMPHPHTASES
PR00378 LIIMPHPHTASE
PROSITEiView protein in PROSITE
PS00629 IMP_1, 1 hit
PS00630 IMP_2, 1 hit

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_015330016.1, XM_015474530.1
UniGeneiBt.424

Genome annotation databases

EnsembliENSBTAT00000015548; ENSBTAP00000015548; ENSBTAG00000011709
GeneIDi281865
KEGGibta:281865

Similar proteinsi

Entry informationi

Entry nameiIMPA1_BOVIN
AccessioniPrimary (citable) accession number: P20456
Secondary accession number(s): Q17QE4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: March 28, 2018
This is version 147 of the entry and version 1 of the sequence. See 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
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Main funding by: National Institutes of Health