Q9Z2L6 · MINP1_MOUSE

  • Protein
    Multiple inositol polyphosphate phosphatase 1
  • Gene
    Minpp1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Multiple inositol polyphosphate phosphatase that hydrolyzes 1D-myo-inositol 1,3,4,5,6-pentakisphosphate (InsP5[2OH]) and 1D-myo-inositol hexakisphosphate (InsP6) to a range of less phosphorylated inositol phosphates. This regulates the availability of these various small molecule second messengers and metal chelators which control many aspects of cell physiology (PubMed:10087200, PubMed:10938126).
Has a weak in vitro activity towards 1D-myo-inositol 1,4,5-trisphosphate which is unlikely to be physiologically relevant. By regulating intracellular inositol polyphosphates pools, which act as metal chelators, it may control the availability of intracellular calcium and iron, which are important for proper neuronal development and homeostasis (PubMed:33257696).
May have a dual substrate specificity, and function as a 2,3-bisphosphoglycerate 3-phosphatase hydrolyzing 2,3-bisphosphoglycerate to 2-phosphoglycerate. 2,3-bisphosphoglycerate (BPG) is formed as part of the Rapoport-Luebering glycolytic bypass and is a regulator of systemic oxygen homeostasis as the major allosteric effector of hemoglobin (By similarity).

Catalytic activity

  • 1D-myo-inositol hexakisphosphate + H2O = 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
    This reaction proceeds in the forward direction.
    EC:3.1.3.62 (UniProtKB | ENZYME | Rhea)
  • 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + H2O = 1D-myo-inositol 1,2,5,6-tetrakisphosphate + phosphate
    This reaction proceeds in the forward direction.
    EC:3.1.3.62 (UniProtKB | ENZYME | Rhea)
  • 1D-myo-inositol 1,2,5,6-tetrakisphosphate + H2O = 1D-myo-inositol 1,2,6-trisphosphate + phosphate
    This reaction proceeds in the forward direction.
    EC:3.1.3.62 (UniProtKB | ENZYME | Rhea)
  • 1D-myo-inositol 1,2,6-trisphosphate + H2O = 1D-myo-inositol 1,2-bisphosphate + phosphate
    This reaction proceeds in the forward direction.
    EC:3.1.3.62 (UniProtKB | ENZYME | Rhea)
  • 1D-myo-inositol 1,2-bisphosphate + H2O = 1D-myo-inositol 2-phosphate + phosphate
    This reaction proceeds in the forward direction.
    EC:3.1.3.62 (UniProtKB | ENZYME | Rhea)
  • 1D-myo-inositol hexakisphosphate + H2O = 1D-myo-inositol 1,2,3,5,6-pentakisphosphate + phosphate
    This reaction proceeds in the forward direction.
  • 1D-myo-inositol 1,2,3,5,6-pentakisphosphate + H2O = 1D-myo-inositol 1,2,3,6-tetrakisphosphate + phosphate
    This reaction proceeds in the forward direction.
  • 1D-myo-inositol 1,2,3,6-tetrakisphosphate + H2O = 1D-myo-inositol 1,2,3-trisphosphate + phosphate
    This reaction proceeds in the forward direction.
  • 1D-myo-inositol 1,2,3-trisphosphate + H2O = 1D-myo-inositol 2,3-bisphosphate + phosphate
    This reaction proceeds in the forward direction.
  • 1D-myo-inositol 2,3-bisphosphate + H2O = 1D-myo-inositol 2-phosphate + phosphate
    This reaction proceeds in the forward direction.
  • 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + H2O = 1D-myo-inositol 1,4,5,6-tetrakisphosphate + phosphate
    This reaction proceeds in the forward direction.
  • 1D-myo-inositol 1,4,5,6-tetrakisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + phosphate
    This reaction proceeds in the forward direction.
  • (2R)-2,3-bisphosphoglycerate + H2O = (2R)-2-phosphoglycerate + phosphate
    This reaction proceeds in the forward direction.
    EC:3.1.3.80 (UniProtKB | ENZYME | Rhea)

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site89

GO annotations

AspectTerm
Cellular Componentendoplasmic reticulum lumen
Cellular Componentextracellular space
Cellular Componentplasma membrane
Molecular Function3-phytase activity
Molecular Function4-phytase activity
Molecular Functionacid phosphatase activity
Molecular Functionbisphosphoglycerate 3-phosphatase activity
Molecular Functioninositol bisphosphate phosphatase activity
Molecular Functioninositol hexakisphosphate 2-phosphatase activity
Molecular Functioninositol pentakisphosphate phosphatase activity
Molecular Functioninositol phosphate phosphatase activity
Molecular Functioninositol trisphosphate phosphatase activity
Molecular Functioninositol-1,3,4,5,6-pentakisphosphate 3-phosphatase activity
Molecular Functioninositol-1,4,5,6-tetrakisphosphate 6-phosphatase activity
Molecular Functioninositol-hexakisphosphate phosphatase activity
Biological Processintracellular monoatomic cation homeostasis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Multiple inositol polyphosphate phosphatase 1
  • EC number
  • Alternative names
    • 2,3-bisphosphoglycerate 3-phosphatase
      (2,3-BPG phosphatase
      ) (EC:3.1.3.80
      ) . EC:3.1.3.80 (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      Minpp1
    • Synonyms
      Mipp
    • ORF names
      MNCb-1572

Organism names

  • Taxonomic identifier
  • Strains
    • 129
    • C57BL/6J
    • Czech II
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q9Z2L6
  • Secondary accessions
    • Q3UA76
    • Q8VDR0
    • Q9JJD5

Proteomes

Organism-specific databases

Subcellular Location

Secreted
Cell membrane
Note: Also associated with the plasma membrane in erythrocytes.

Keywords

Phenotypes & Variants

Disruption phenotype

Knockout mice are born at Mendelian ratio and are fertile. Although brain histology does not identify major differences in cerebellar or cerebral cortex architecture, a mild, but significant 10% decrease in the brain weight was identified associated with a reduced cortical thickness in homozygous mutant mice at postnatal day 21 (PubMed:33257696).
At 14.5 dpc, neural progenitors show a decrease of about one third in intracellular free Ca2+ levels compared to wild-type progenitors (PubMed:33257696).
Normal chondrocyte differentiation and bone development are observed (PubMed:10938126).

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis89Loss of phosphatase inositol phosphate phosphatase activity.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 12 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for signal, chain, glycosylation.

TypeIDPosition(s)Description
Signal1-30
ChainPRO_000001958331-481Multiple inositol polyphosphate phosphatase 1
Glycosylation236N-linked (GlcNAc...) asparagine
Glycosylation475N-linked (GlcNAc...) asparagine

Post-translational modification

N-glycosylated.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Widely expressed with highest levels in kidney, intestine, thymus and liver.

Developmental stage

Expressed in different stages of embryogenesis, from 7.5 dpc through 14.5 dpc. The highest levels of expression is found in the visceral endoderm at 7.5 dpc and 8.5 dpc and in the fetal liver at 12.5 dpc and 14.5 dpc.

Gene expression databases

    • ENSMUSG00000024896Expressed in fetal liver hematopoietic progenitor cell and 271 other cell types or tissues

Interaction

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for motif.

TypeIDPosition(s)Description
Motif478-481Prevents secretion from ER

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    481
  • Mass (Da)
    54,537
  • Last updated
    2011-07-27 v3
  • Checksum
    7CE78356B11F4606
MLRGARSHLPASVAPAAVLAAALLSSFARCSLPGRGDPVASVLSPYFGTKTRYEDANPWLLVDPVAPRRDPELLAGTCTPVQLVALIRHGTRYPTTKQIRKLKQLQGLLQTRESRDGGSQVAAALAEWPLWYGDWMDGQLVEKGRQDMRQLALRLAALFPDLFSRENYDRLRLITSSKHRCVDSSAAFLQGLWQHYHPGLPPPDVSDMECGPPRINDKLMRFFDHCEKFLTDVERNETALYHVEAFKTGPEMQKVLKKVAATLQVPMNSLNADLIQVAFFTCSFDLAIKGVHSPWCDVFDVDDARVLEYLNDLKQYWKRSYGYTINSRSSCNLFQDIFLHLDKAVEQKQRSQPVSSPVILQFGHAETLLPLLSLMGYFKDKEPLTAYNFEEQVNRKFRSGHIVPYASNLIFVLYHCDNAQSPEEQFQIQLLLNEKVLPLAHSQRPVGLYEELKTHYRDILQSCQTSKECSPPKANITSDEL

Sequence caution

The sequence BAA95058.1 differs from that shown. Reason: Frameshift

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict211in Ref. 4; AAH21437
Sequence conflict257in Ref. 4; AAH21437
Sequence conflict267in Ref. 4; AAH21437

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF046908
EMBL· GenBank· DDBJ
AAD02434.1
EMBL· GenBank· DDBJ
mRNA
AB041574
EMBL· GenBank· DDBJ
BAA95058.1
EMBL· GenBank· DDBJ
mRNA Frameshift
AK151486
EMBL· GenBank· DDBJ
BAE30439.1
EMBL· GenBank· DDBJ
mRNA
BC021437
EMBL· GenBank· DDBJ
AAH21437.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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