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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)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

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 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

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

Belongs to the inositol monophosphatase family.Curated

Phylogenomic databases

eggNOGiKOG2951. Eukaryota.
COG0483. LUCA.
GeneTreeiENSGT00390000014699.
HOGENOMiHOG000282238.
HOVERGENiHBG052123.
InParanoidiP20456.
KOiK01092.
OMAiMWEAVKV.
OrthoDBiEOG091G0D21.
TreeFamiTF313194.

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.

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.

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_015330016.1. XM_015474530.1.
UniGeneiBt.424.

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...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000015548.

Chemistry databases

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.
OMAiMWEAVKV.
OrthoDBiEOG091G0D21.
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.

Gene expression databases

BgeeiENSBTAG00000011709.

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_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: November 30, 2016
This is version 139 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.