Q9Z2L6 · MINP1_MOUSE
- ProteinMultiple inositol polyphosphate phosphatase 1
- GeneMinpp1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids481 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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 + phosphateThis reaction proceeds in the forward direction.
- 1D-myo-inositol hexakisphosphate + H2O = 1D-myo-inositol 1,2,3,5,6-pentakisphosphate + phosphateThis reaction proceeds in the forward direction.
- 1D-myo-inositol 1,2,3,5,6-pentakisphosphate + H2O = 1D-myo-inositol 1,2,3,6-tetrakisphosphate + phosphateThis reaction proceeds in the forward direction.
- 1D-myo-inositol 1,2,3,6-tetrakisphosphate + H2O = 1D-myo-inositol 1,2,3-trisphosphate + phosphateThis reaction proceeds in the forward direction.
- 1D-myo-inositol 1,2,3-trisphosphate + H2O = 1D-myo-inositol 2,3-bisphosphate + phosphateThis reaction proceeds in the forward direction.
- 1D-myo-inositol 2,3-bisphosphate + H2O = 1D-myo-inositol 2-phosphate + phosphateThis reaction proceeds in the forward direction.
- 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + H2O = 1D-myo-inositol 1,4,5,6-tetrakisphosphate + phosphateThis reaction proceeds in the forward direction.
- 1D-myo-inositol 1,4,5,6-tetrakisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + phosphateThis reaction proceeds in the forward direction.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 89 | |||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum lumen | |
Cellular Component | extracellular space | |
Cellular Component | plasma membrane | |
Molecular Function | 3-phytase activity | |
Molecular Function | 4-phytase activity | |
Molecular Function | acid phosphatase activity | |
Molecular Function | bisphosphoglycerate 3-phosphatase activity | |
Molecular Function | inositol bisphosphate phosphatase activity | |
Molecular Function | inositol hexakisphosphate 2-phosphatase activity | |
Molecular Function | inositol pentakisphosphate phosphatase activity | |
Molecular Function | inositol phosphate phosphatase activity | |
Molecular Function | inositol trisphosphate phosphatase activity | |
Molecular Function | inositol-1,3,4,5,6-pentakisphosphate 3-phosphatase activity | |
Molecular Function | inositol-1,4,5,6-tetrakisphosphate 6-phosphatase activity | |
Molecular Function | inositol-hexakisphosphate phosphatase activity | |
Biological Process | intracellular monoatomic cation homeostasis |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMultiple inositol polyphosphate phosphatase 1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9Z2L6
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Also associated with the plasma membrane in erythrocytes.
Keywords
- Cellular component
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).
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 89 | Loss of phosphatase inositol phosphate phosphatase activity. | ||||
Sequence: H → A |
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.
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-30 | |||||
Sequence: MLRGARSHLPASVAPAAVLAAALLSSFARC | ||||||
Chain | PRO_0000019583 | 31-481 | Multiple inositol polyphosphate phosphatase 1 | |||
Sequence: SLPGRGDPVASVLSPYFGTKTRYEDANPWLLVDPVAPRRDPELLAGTCTPVQLVALIRHGTRYPTTKQIRKLKQLQGLLQTRESRDGGSQVAAALAEWPLWYGDWMDGQLVEKGRQDMRQLALRLAALFPDLFSRENYDRLRLITSSKHRCVDSSAAFLQGLWQHYHPGLPPPDVSDMECGPPRINDKLMRFFDHCEKFLTDVERNETALYHVEAFKTGPEMQKVLKKVAATLQVPMNSLNADLIQVAFFTCSFDLAIKGVHSPWCDVFDVDDARVLEYLNDLKQYWKRSYGYTINSRSSCNLFQDIFLHLDKAVEQKQRSQPVSSPVILQFGHAETLLPLLSLMGYFKDKEPLTAYNFEEQVNRKFRSGHIVPYASNLIFVLYHCDNAQSPEEQFQIQLLLNEKVLPLAHSQRPVGLYEELKTHYRDILQSCQTSKECSPPKANITSDEL | ||||||
Glycosylation | 236 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 475 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
N-glycosylated.
Keywords
- PTM
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
Structure
Family & Domains
Features
Showing features for motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 478-481 | Prevents secretion from ER | ||||
Sequence: SDEL |
Sequence similarities
Belongs to the histidine acid phosphatase family. MINPP1 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length481
- Mass (Da)54,537
- Last updated2011-07-27 v3
- Checksum7CE78356B11F4606
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 211 | in Ref. 4; AAH21437 | ||||
Sequence: G → D | ||||||
Sequence conflict | 257 | in Ref. 4; AAH21437 | ||||
Sequence: K → Q | ||||||
Sequence conflict | 267 | in Ref. 4; AAH21437 | ||||
Sequence: M → V |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |