GO:0004439 phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity: Mechanism, Genes and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0004439 describes the enzymatic removal of the 5-phosphate from phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), yielding phosphatidylinositol 4-phosphate and inorganic phosphate.
• This activity is a core component of phosphoinositide signalling, controlling the abundance of PtdIns(4,5)P2 and downstream second messengers such as inositol 1,4,5-trisphosphate and diacylglycerol.
• Deficiency of phosphatidylinositol 4,5-bisphosphate 5-phosphatase in the Golgi apparatus is the biochemical hallmark of Lowe syndrome, an X-linked disorder caused by OCRL mutations.
• Synaptojanin1 (SYNJ1) is a well-characterized 5-phosphatase that limits integrin-mediated invasion of Staphylococcus aureus and is a target for selective inhibitor development.
• The activity is conserved across eukaryotes and even in plants, where a Solanum tuberosum 5-phosphatase is activated by PAMP treatment and may antagonize PtdIns(4,5)P2 at pathogen infection sites.
• Dysregulated 5-phosphatase activity is linked to skeletal muscle disease through defective lysosome reformation during autophagy, highlighting its role beyond classical signal transduction.
Description
Phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity (GO:0004439) is a molecular function that catalyzes the hydrolysis of phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) to phosphatidylinositol 4-phosphate and phosphate. This reaction is a key node in phosphoinositide metabolism, directly opposing the synthesis of PtdIns(4,5)P2 and thereby modulating a lipid that serves as a substrate for phospholipase C and phosphoinositide 3-kinase signalling. Because PtdIns(4,5)P2 regulates membrane trafficking, ion channel activity, and actin dynamics, the enzymes that remove its 5-phosphate are central to cellular homeostasis. Researchers study this activity to understand how cells decode lipid signals and how its perturbation contributes to disease. The first biochemical characterization of a mammalian PtdIns(4,5)P2 5-phosphatase was performed in human platelets, establishing the existence of a distinct enzyme activity that dephosphorylates the 5-position of the inositol ring. Subsequent work identified OCRL as a Golgi-localized 5-phosphatase whose deficiency causes Lowe syndrome, linking the activity to a specific human genetic disorder. More recently, synaptojanin1 has emerged as a multifunctional 5-phosphatase involved in endocytosis and host-pathogen interactions, and selective inhibitors of its 5-phosphatase activity have been developed. The activity is also present in plants, where it participates in immune responses to pathogens. Together, these findings make GO:0004439 a compelling target for functional genomics, drug discovery, and disease modeling.
phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity At A Glance
| GO ID | GO:0004439 |
|---|---|
| GO term | phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity |
| Ontology | molecular_function |
| Synonym | PI(4,5)P2 5-phosphatase activity; phosphatidylinositol 4,5-bisphosphate phosphatase activity; triphosphoinositide phosphatase activity |
| Major function | Hydrolyzes PtdIns(4,5)P2 to PtdIns(4)P and phosphate, regulating phosphoinositide signalling |
| Reaction | 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate |
| Subcellular context | Associated with Golgi apparatus, plasma membrane, and endocytic compartments |
| Representative enzymes | OCRL, SYNJ1, INPP5B, INPP5E, SHIP2 (INPPL1) |
| Disease links | Lowe syndrome, skeletal muscle disease, bacterial invasion |
What Is GO:0004439?
GO:0004439, phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity, is defined as the catalysis of the reaction: 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate. In other words, the enzyme removes the phosphate group attached to the 5-position of the inositol ring of PtdIns(4,5)P2, releasing inorganic phosphate and leaving PtdIns(4)P. This activity is distinct from 3-phosphatases and 4-phosphatases because it specifically targets the 5-phosphate. Synonyms include phosphatidylinositol 4,5-bisphosphate phosphatase activity, PI(4,5)P2 5-phosphatase activity, and triphosphoinositide phosphatase activity. The term is classified under molecular_function in the Gene Ontology.
Why Is phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity Important in Cell Biology?
Phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity is important because it directly controls the cellular levels of PtdIns(4,5)P2, a lipid that acts as a signalling hub for numerous processes including membrane trafficking, cytoskeletal reorganization, and cell proliferation. By removing the 5-phosphate, these enzymes terminate or attenuate signals that would otherwise be mediated by PtdIns(4,5)P2 and its derivatives. This regulatory role is essential for normal physiology, as evidenced by the fact that mutations in the 5-phosphatase OCRL cause Lowe syndrome, a severe developmental disorder. Moreover, the activity is exploited by pathogens; synaptojanin1 limits integrin-mediated invasion of Staphylococcus aureus, indicating a role in host defense. In skeletal muscle, defective lysosome reformation during autophagy due to impaired 5-phosphatase function leads to muscle disease. Thus, understanding GO:0004439 is critical for both basic cell biology and translational research.
• Regulates PtdIns(4,5)P2 levels, thereby influencing phospholipase C and PI3K signalling pathways.
• Deficiency of OCRL 5-phosphatase in the Golgi apparatus causes Lowe syndrome, an X-linked disorder.
• Synaptojanin1 5-phosphatase activity restricts Staphylococcus aureus invasion via integrin-mediated pathways.
• Selective inhibitors of synaptojanin1 5-phosphatase have been discovered, offering pharmacological tools.
• Plant 5-phosphatases are activated by PAMP treatment and may antagonize PtdIns(4,5)P2 at infection sites.
• Impaired lysosome reformation during autophagy due to 5-phosphatase dysfunction leads to skeletal muscle disease.
• The activity is biochemically distinct and was first characterized in human platelets.
• Anionic lipids influence SHIP2 5-phosphatase activity, linking membrane composition to enzyme regulation.
• Provides a target for drug discovery in cancer, infection, and genetic disorders.
• Essential for understanding phosphoinositide dynamics in health and disease.
Mechanism, Genes and Research Methods
Substrate recognition and binding
In simple terms: The enzyme grabs a specific lipid molecule called PtdIns(4,5)P2 from the membrane.
Phosphatidylinositol-4,5-bisphosphate 5-phosphatase enzymes recognize the headgroup of PtdIns(4,5)P2, which consists of a myo-inositol ring phosphorylated at positions 4 and 5, attached to a diacylglycerol lipid anchor. The enzyme binds this substrate at the membrane interface, often via a pleckstrin homology domain or other lipid-binding modules. The specificity for the 5-phosphate is determined by the active site architecture, which positions the 5-phosphate for nucleophilic attack by water while excluding the 4-phosphate. This step is critical for the enzyme's ability to discriminate among phosphoinositide isomers.
Catalytic hydrolysis of the 5-phosphate
In simple terms: The enzyme cuts off the phosphate at the 5-position, releasing it as free phosphate.
The catalytic mechanism involves a water molecule that is activated by a general base, attacking the phosphorus atom of the 5-phosphate. This leads to the cleavage of the phosphoester bond and release of inorganic phosphate, yielding phosphatidylinositol 4-phosphate (PtdIns(4)P). The reaction is dependent on divalent cations such as Mg2+ or Ca2+ in some enzymes, although the exact cofactor requirements vary. The activity of the platelet 5-phosphatase was shown to be specific for the 5-position, distinguishing it from other phosphatases. This hydrolysis is irreversible under physiological conditions and effectively lowers the local concentration of PtdIns(4,5)P2.
Regulation by anionic lipids and membrane environment
In simple terms: Other lipids in the membrane can turn the enzyme's activity up or down.
The activity of 5-phosphatases can be modulated by the lipid composition of the membrane. For example, the 5-phosphatase activity of SHIP2 (INPPL1) is influenced by anionic lipids, which can alter its substrate accessibility or catalytic efficiency. This suggests that changes in membrane charge, such as those occurring during signalling events, can feedback to regulate 5-phosphatase function. In plants, a Solanum tuberosum 5-phosphatase is activated by PAMP treatment, indicating that environmental or immune stimuli can also regulate the enzyme. Thus, the activity is not constitutive but is subject to multiple layers of control.
Downstream consequences for cellular signalling
In simple terms: Removing the 5-phosphate changes the lipid's ability to send signals inside the cell.
By converting PtdIns(4,5)P2 to PtdIns(4)P, the 5-phosphatase terminates the ability of PtdIns(4,5)P2 to serve as a substrate for phospholipase C, which generates inositol 1,4,5-trisphosphate and diacylglycerol. It also reduces the pool of PtdIns(4,5)P2 available for phosphoinositide 3-kinase, thereby dampening PI3K/Akt signalling. This shift in lipid identity affects membrane recruitment of proteins with PtdIns(4,5)P2-binding domains, impacting processes such as endocytosis, exocytosis, and actin polymerization. In the context of infection, synaptojanin1-mediated depletion of PtdIns(4,5)P2 limits integrin-mediated invasion of Staphylococcus aureus. Therefore, the activity acts as a molecular switch that rewires cellular signalling networks.
Key Genes Involved in GO:0004439 phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity
The following genes encode enzymes or regulatory proteins that possess or modulate phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity (GO:0004439).
| Gene | Major Role | Research Relevance |
|---|---|---|
| OCRL | Golgi-localized 5-phosphatase; deficiency causes Lowe syndrome | Disease modeling, Golgi trafficking studies |
| SYNJ1 | Synaptic 5-phosphatase; regulates endocytosis and bacterial invasion | Host-pathogen interactions, inhibitor development |
| INPP5B | 5-phosphatase with overlapping functions with OCRL | Functional redundancy studies, knockout models |
| INPP5E | Ciliary 5-phosphatase; mutations cause Joubert syndrome | Ciliopathy research, phosphoinositide signalling |
| INPPL1 (SHIP2) | 5-phosphatase acting on PI(3,4,5)P3; regulated by anionic lipids | Metabolic signalling, insulin resistance |
| INPP5A | Soluble 5-phosphatase acting on IP3 and PtdIns(4,5)P2 | Calcium signalling, cancer studies |
| INPP5J | 5-phosphatase involved in membrane trafficking | Endosomal dynamics, autophagy |
| INPP5K | 5-phosphatase linked to muscular dystrophy | Skeletal muscle disease, autophagy |
| SYNJ2 | 5-phosphatase with roles in cell migration | Cytoskeletal regulation, cancer invasion |
| PIP5K1A | Kinase that synthesizes PtdIns(4,5)P2, opposing 5-phosphatase | Lipid balance studies |
| PLCB1 | Phospholipase C that consumes PtdIns(4,5)P2 | Signalling cross-talk |
| PIK3CA | Kinase that uses PtdIns(4,5)P2 to generate PI(3,4,5)P3 | Cancer signalling |
| PTEN | 3-phosphatase that indirectly affects PtdIns(4,5)P2 levels | Tumor suppressor research |
| AP2M1 | Clathrin adaptor that binds PtdIns(4,5)P2 | Endocytosis studies |
| DNM2 | Dynamin GTPase recruited by PtdIns(4,5)P2 | Membrane fission research |
| ACTN1 | Actin crosslinker regulated by PtdIns(4,5)P2 | Cytoskeleton dynamics |
| WASL | Actin nucleation factor activated by PtdIns(4,5)P2 | Cell motility studies |
How Is phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity Regulated?
The activity of phosphatidylinositol-4,5-bisphosphate 5-phosphatases is regulated at multiple levels. Membrane lipid composition, particularly the presence of anionic lipids, can directly influence the catalytic efficiency of enzymes such as SHIP2. In plants, PAMP treatment activates a Solanum tuberosum 5-phosphatase, suggesting that immune signalling pathways can upregulate the activity. Additionally, post-translational modifications and protein-protein interactions likely control subcellular localization and substrate access, although specific mechanisms for many family members remain to be fully defined. The activity is also balanced by opposing kinases (e.g., PIP5K) that synthesize PtdIns(4,5)P2, creating a dynamic equilibrium that is critical for signal transduction.
phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| OCRL | Lowe syndrome | Patient-derived fibroblasts, Ocrl knockout mouse |
| SYNJ1 | Bacterial invasion, endocytosis | SYNJ1 knockout cell lines, infection assays |
| INPP5K | Skeletal muscle disease, autophagy | Muscle-specific knockout mouse |
| INPPL1 (SHIP2) | Insulin resistance, metabolic syndrome | SHIP2 knockout mice, adipocyte models |
| INPP5E | Joubert syndrome (ciliopathy) | Patient iPSCs, zebrafish models |
Lowe syndrome (oculocerebrorenal syndrome)
Lowe syndrome is an X-linked disorder caused by mutations in OCRL, which encodes a phosphatidylinositol 4,5-bisphosphate 5-phosphatase localized to the Golgi apparatus. The deficiency of this enzyme activity leads to abnormal phosphoinositide metabolism, resulting in congenital cataracts, intellectual disability, and renal Fanconi syndrome. Studies of patient cells and animal models have linked the loss of 5-phosphatase activity to defects in membrane trafficking and actin dynamics.
Skeletal muscle disease and autophagy
Defective lysosome reformation during autophagy, caused by impaired 5-phosphatase activity, has been shown to cause skeletal muscle disease. This highlights the importance of phosphoinositide turnover in muscle homeostasis and suggests that mutations in 5-phosphatase genes such as INPP5K may underlie certain myopathies. Experimental models with targeted deletions of these enzymes recapitulate muscle pathology, providing insight into disease mechanisms.
Host-pathogen interactions
Synaptojanin1 (SYNJ1) 5-phosphatase activity limits integrin-mediated invasion of Staphylococcus aureus. By depleting PtdIns(4,5)P2, synaptojanin1 reduces the availability of this lipid for bacterial uptake mechanisms. This finding positions 5-phosphatases as potential therapeutic targets for infectious diseases, and selective inhibitors of synaptojanin1 have been developed.
Cancer and metabolic disorders
Alterations in phosphoinositide signalling, including changes in 5-phosphatase activity, have been implicated in cancer and metabolic diseases such as diabetes. For example, SHIP2 (INPPL1) is a 5-phosphatase that regulates insulin signalling, and its activity is modulated by anionic lipids. While direct mutations in 5-phosphatase genes are less common in cancer, dysregulated lipid signalling contributes to tumorigenesis, making these enzymes attractive for drug discovery.
From phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Does loss of OCRL 5-phosphatase cause Golgi trafficking defects? | OCRL knockout HeLa cells or patient fibroblasts |
| Can a point mutation in the catalytic domain abolish 5-phosphatase activity? | CRISPR point-mutation knock-in of catalytic dead variant |
| How does synaptojanin1 5-phosphatase limit S. aureus invasion? | SYNJ1 knockout or overexpression in epithelial cells |
| What is the role of INPP5K in lysosome reformation during autophagy? | INPP5K knockout muscle cells or mouse models |
| Does anionic lipid binding regulate SHIP2 activity? | In vitro lipid binding assays with purified SHIP2 |
| Can selective inhibitors modulate synaptojanin1 activity in cells? | Cell-based assays with synaptojanin1 inhibitor |
How to Study the phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity Process
| Method | What It Measures | Typical Application |
|---|---|---|
| In vitro phosphatase assay | Enzymatic release of phosphate from PtdIns(4,5)P2 | Kinetic characterization, inhibitor screening |
| CRISPR knockout | Loss of gene function | Phenotypic analysis of 5-phosphatase genes |
| CRISPR point mutation | Specific amino acid substitution | Catalytic dead mutants, separation of functions |
| Fluorescent lipid biosensors | Local PtdIns(4,5)P2 and PtdIns(4)P levels | Live-cell imaging of signalling dynamics |
| RNA-seq | Transcriptional changes | Pathway analysis in knockout models |
| Proteomics | Protein abundance and interactions | Identification of 5-phosphatase complexes |
| Lipid binding assays | Interaction with anionic lipids | Regulation of SHIP2 activity |
| Infection assays | Bacterial invasion efficiency | Host-pathogen studies with SYNJ1 |
Biochemical assays for 5-phosphatase activity
The direct measurement of phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity typically involves incubating the enzyme with radiolabeled or fluorescent PtdIns(4,5)P2 and separating the products by thin-layer chromatography or HPLC. This approach was used to identify and characterize the platelet 5-phosphatase. Such assays are essential for determining kinetic parameters and for screening inhibitors, as demonstrated for synaptojanin1.
Genetic and CRISPR-based perturbation
CRISPR-Cas9 knockout, point mutation, and knock-in strategies enable researchers to dissect the specific contributions of 5-phosphatase genes to cellular phenotypes. For example, knockout of OCRL in cell lines recapitulates Lowe syndrome phenotypes, while point mutations can separate catalytic activity from scaffolding functions. These models are invaluable for linking genotype to biochemical and physiological outcomes.
Imaging phosphoinositide dynamics
Fluorescent biosensors that detect PtdIns(4,5)P2 or PtdIns(4)P can be used to monitor the activity of 5-phosphatases in live cells. This approach has revealed that synaptojanin1 depletion alters PtdIns(4,5)P2 distribution during bacterial invasion. Advanced microscopy techniques, including total internal reflection fluorescence (TIRF), allow visualization of lipid changes at the plasma membrane with high spatiotemporal resolution.
Omics and bioinformatics
Transcriptomic and proteomic profiling of cells with altered 5-phosphatase activity can identify downstream signalling networks. For instance, RNA-seq of OCRL-deficient cells has uncovered changes in Golgi-related genes. Bioinformatics analysis of phosphoinositide-related gene expression across cancer datasets can reveal correlations with disease progression, guiding functional studies.
How CRISPR Can Be Used to Study GO:0004439 phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity
Knockout
CRISPR-Cas9 knockout of 5-phosphatase genes such as OCRL or SYNJ1 creates cell models to study loss-of-function phenotypes. For example, OCRL knockout cells exhibit Golgi abnormalities reminiscent of Lowe syndrome. Knockout models are also used to assess the contribution of specific 5-phosphatases to bacterial invasion and autophagy.
Point Mutation
Point mutations can be introduced into the catalytic domain of 5-phosphatases to abolish enzymatic activity while preserving protein structure. This is particularly useful for distinguishing between catalytic and non-catalytic functions. For instance, a point mutation in the 5-phosphatase domain of synaptojanin1 can clarify whether its role in endocytosis depends on lipid hydrolysis.
Knock-in
Knock-in of tagged or fluorescently labeled 5-phosphatases allows for real-time tracking of enzyme localization and dynamics. This approach can reveal how these enzymes are recruited to specific membranes, such as the Golgi or endocytic sites. Knock-in of disease-associated mutations, such as those found in Lowe syndrome, provides isogenic models for studying pathogenesis.
Overexpression
Overexpression of wild-type or mutant 5-phosphatases can be used to test gain-of-function effects on phosphoinositide levels and downstream signalling. For example, overexpression of synaptojanin1 reduces PtdIns(4,5)P2 and limits bacterial uptake. Overexpression systems are also valuable for producing recombinant enzyme for biochemical assays.
How EDITGENE Supports phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity Research
Researchers studying phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity-related genes often need to determine whether a candidate gene is causally involved in a specific cellular process or disease. This requires precise genetic models that can isolate the contribution of enzymatic activity from other protein functions. EDITGENE provides a comprehensive suite of CRISPR-based services to accelerate such investigations.
Contact EDITGENE today to design your custom CRISPR model for phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity research.
Frequently Asked Questions About phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity
What is phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity?
It is the enzymatic activity that removes the 5-phosphate from PtdIns(4,5)P2, producing PtdIns(4)P and phosphate, as defined by GO:0004439.
What genes are involved in phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity?
Key genes include OCRL, SYNJ1, INPP5B, INPP5E, INPPL1 (SHIP2), INPP5A, INPP5J, INPP5K, and SYNJ2.
What diseases are linked to phosphatidylinositol-4,5-bisphosphate 5-phosphatase deficiency?
Lowe syndrome is caused by OCRL deficiency, and skeletal muscle disease is linked to defective lysosome reformation.
How is phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity measured?
It is typically measured using in vitro phosphatase assays with radiolabeled or fluorescent PtdIns(4,5)P2, followed by product separation.
What is the role of synaptojanin1 in bacterial infection?
Synaptojanin1 5-phosphatase activity limits integrin-mediated invasion of Staphylococcus aureus by depleting PtdIns(4,5)P2.
Can phosphatidylinositol-4,5-bisphosphate 5-phosphatase be inhibited pharmacologically?
Yes, selective inhibitors of synaptojanin1 5-phosphatase activity have been discovered and characterized.
Is phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity conserved in plants?
Yes, a Solanum tuberosum 5-phosphatase is activated by PAMP treatment and may antagonize PtdIns(4,5)P2 at infection sites.
How does anionic lipid environment affect 5-phosphatase activity?
Anionic lipids can influence the activity of SHIP2 (INPPL1) 5-phosphatase, suggesting membrane composition regulates enzyme function.
What are the synonyms for GO:0004439?
Synonyms include PI(4,5)P2 5-phosphatase activity, phosphatidylinositol 4,5-bisphosphate phosphatase activity, and triphosphoinositide phosphatase activity.
What CRISPR models are available for studying 5-phosphatase genes?
Knockout, point mutation, knock-in, tagged knock-in, and overexpression models can be generated for genes like OCRL and SYNJ1.
Conclusion
Phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity (GO:0004439) is a fundamental enzymatic function that shapes phosphoinositide signalling and impacts human health. From its role in Lowe syndrome and skeletal muscle disease to its involvement in host-pathogen interactions, this activity is a rich area for research. The availability of CRISPR models and biochemical assays enables precise interrogation of its mechanisms. EDITGENE stands ready to support these efforts with tailored gene editing and screening services.
References
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- 3. Rausche J et al.. 2021. A phosphoinositide 5-phosphatase from Solanum tuberosum is activated by PAMP-treatment and may antagonize phosphatidylinositol 4,5-bisphosphate at Phytophthora infestans infection sites.. New Phytol 229(1):469-487 PMID: 32762082
- 4. Shi Y et al.. 2024. The phosphatidylinositol-5' phosphatase synaptojanin1 limits integrin-mediated invasion of Staphylococcus aureus.. Microbiol Spectr 12(4):e0200623 PMID: 38358281
- 5. Martin E et al.. 2025. Discovery and Characterization of a Selective Inhibitor of Synaptojanin1 5‑Phosphatase Activity.. ACS Pharmacol Transl Sci 8(9):2996-3006 PMID: 40969890
- 6. Matzaris M et al.. 1994. Identification and characterization of the phosphatidylinositol-(4, 5)-bisphosphate 5-phosphatase in human platelets.. J Biol Chem 269(5):3397-402 PMID: 8106379
- 7. McGrath MJ et al.. 2021. Defective lysosome reformation during autophagy causes skeletal muscle disease.. J Clin Invest 131(1) PMID: 33119550
- 8. Vandeput F et al.. 2006. The influence of anionic lipids on SHIP2 phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase activity.. Cell Signal 18(12):2193-9 PMID: 16824732
