UniProt functional annotation for Q66GT5



	UniProt functional annotation for Q66GT5

UniProt code: Q66GT5.

Organism: Mus musculus (Mouse).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus.

Function: Lipid phosphatase which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG) (PubMed:21641550, PubMed:21730175). PGP is an essential intermediate in the biosynthetic pathway of cardiolipin, a mitochondrial-specific phospholipid regulating the membrane integrity and activities of the organelle (PubMed:21641550). Has also been shown to display phosphatase activity toward phosphoprotein substrates, specifically mediates dephosphorylation of mitochondrial proteins, thereby playing an essential role in ATP production (By similarity). Has probably a preference for proteins phosphorylated on Ser and/or Thr residues compared to proteins phosphorylated on Tyr residues (By similarity). Probably involved in regulation of insulin secretion in pancreatic beta cells (By similarity). May prevent intrinsic apoptosis, probably by regulating mitochondrial membrane integrity (By similarity). {ECO:0000250|UniProtKB:P0C089, ECO:0000250|UniProtKB:Q8WUK0, ECO:0000269|PubMed:16039589, ECO:0000269|PubMed:21641550}.

Catalytic activity: Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + H2O = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + phosphate; Xref=Rhea:RHEA:33751, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:60110, ChEBI:CHEBI:64716; EC=3.1.3.27; Evidence={ECO:0000269|PubMed:21641550, ECO:0000269|PubMed:21730175}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33752; Evidence={ECO:0000269|PubMed:21641550, ECO:0000269|PubMed:21730175};

Catalytic activity: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA- COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE- ProRule:PRU10044}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10685; Evidence={ECO:0000305};

Catalytic activity: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000250|UniProtKB:P0C089}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20630; Evidence={ECO:0000305};

Catalytic activity: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA- COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; Evidence={ECO:0000250|UniProtKB:P0C089}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47005; Evidence={ECO:0000305};

Catalytic activity: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol- 3'-phosphate) + H2O = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho- (1'-sn-glycerol) + phosphate; Xref=Rhea:RHEA:42304, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:75163, ChEBI:CHEBI:78907; Evidence={ECO:0000269|PubMed:21730175}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42305; Evidence={ECO:0000269|PubMed:21730175};

Catalytic activity: Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-5- phosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo- inositol) + phosphate; Xref=Rhea:RHEA:42308, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:65221, ChEBI:CHEBI:78911; Evidence={ECO:0000269|PubMed:15247229}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42309; Evidence={ECO:0000269|PubMed:15247229};

Catalytic activity: Reaction=a 1-acyl-2-hexanoyl-sn-glycero-3-phospho-(1D-myo-inositol-5- phosphate) + H2O = a 1-acyl-2-hexanoyl-sn-glycero-3-phospho-(1D-myo- inositol) + phosphate; Xref=Rhea:RHEA:42320, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:78930, ChEBI:CHEBI:78931; Evidence={ECO:0000269|PubMed:15247229}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42321; Evidence={ECO:0000269|PubMed:15247229};

Catalytic activity: Reaction=1,2-dibutyryl-sn-glycero-3-phospho-(1D-myo-inositol-5- phosphate) + H2O = 1,2-dibutyryl-sn-glycero-3-phospho-(1D-myo- inositol) + phosphate; Xref=Rhea:RHEA:42584, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:82605, ChEBI:CHEBI:82606; Evidence={ECO:0000269|PubMed:15247229}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42585; Evidence={ECO:0000269|PubMed:15247229};

Pathway: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 2/2. {ECO:0000269|PubMed:21641550}.

Subunit: Interacts with STYXL1; the interaction inhibits PTPMT1 catalytic activity. {ECO:0000250|UniProtKB:Q8WUK0}.

Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:16039589}; Peripheral membrane protein {ECO:0000250|UniProtKB:P0C089}; Matrix side {ECO:0000250|UniProtKB:P0C089}.

Tissue specificity: Predominantly expressed in testis. Expressed at lower level in heart, brain, spleen, lung, liver, skeletal muscle, kidney, bone marrow, eye, lymph node, smooth muscle, prostate, thymus, stomach and uterus. {ECO:0000269|PubMed:15247229}.

Disruption phenotype: Mice die prior to E8.5. {ECO:0000269|PubMed:21641550}.

Similarity: Belongs to the protein-tyrosine phosphatase family. Non- receptor class dual specificity subfamily. {ECO:0000305}.

Sequence caution: Sequence=AAH26750.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; Sequence=BAB28400.1; Type=Frameshift; Evidence={ECO:0000305}; Sequence=BAB29504.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.


Organism:		Mus musculus (Mouse).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus.



Function:		Lipid phosphatase which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG) (PubMed:21641550, PubMed:21730175). PGP is an essential intermediate in the biosynthetic pathway of cardiolipin, a mitochondrial-specific phospholipid regulating the membrane integrity and activities of the organelle (PubMed:21641550). Has also been shown to display phosphatase activity toward phosphoprotein substrates, specifically mediates dephosphorylation of mitochondrial proteins, thereby playing an essential role in ATP production (By similarity). Has probably a preference for proteins phosphorylated on Ser and/or Thr residues compared to proteins phosphorylated on Tyr residues (By similarity). Probably involved in regulation of insulin secretion in pancreatic beta cells (By similarity). May prevent intrinsic apoptosis, probably by regulating mitochondrial membrane integrity (By similarity). {ECO:0000250\|UniProtKB:P0C089, ECO:0000250\|UniProtKB:Q8WUK0, ECO:0000269\|PubMed:16039589, ECO:0000269\|PubMed:21641550}.


Catalytic activity:		Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + H2O = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + phosphate; Xref=Rhea:RHEA:33751, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:60110, ChEBI:CHEBI:64716; EC=3.1.3.27; Evidence={ECO:0000269\|PubMed:21641550, ECO:0000269\|PubMed:21730175}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33752; Evidence={ECO:0000269\|PubMed:21641550, ECO:0000269\|PubMed:21730175};
Catalytic activity:		Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA- COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255\|PROSITE- ProRule:PRU10044}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10685; Evidence={ECO:0000305};
Catalytic activity:		Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000250\|UniProtKB:P0C089}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20630; Evidence={ECO:0000305};
Catalytic activity:		Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA- COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; Evidence={ECO:0000250\|UniProtKB:P0C089}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47005; Evidence={ECO:0000305};
Catalytic activity:		Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol- 3'-phosphate) + H2O = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho- (1'-sn-glycerol) + phosphate; Xref=Rhea:RHEA:42304, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:75163, ChEBI:CHEBI:78907; Evidence={ECO:0000269\|PubMed:21730175}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42305; Evidence={ECO:0000269\|PubMed:21730175};
Catalytic activity:		Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-5- phosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo- inositol) + phosphate; Xref=Rhea:RHEA:42308, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:65221, ChEBI:CHEBI:78911; Evidence={ECO:0000269\|PubMed:15247229}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42309; Evidence={ECO:0000269\|PubMed:15247229};
Catalytic activity:		Reaction=a 1-acyl-2-hexanoyl-sn-glycero-3-phospho-(1D-myo-inositol-5- phosphate) + H2O = a 1-acyl-2-hexanoyl-sn-glycero-3-phospho-(1D-myo- inositol) + phosphate; Xref=Rhea:RHEA:42320, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:78930, ChEBI:CHEBI:78931; Evidence={ECO:0000269\|PubMed:15247229}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42321; Evidence={ECO:0000269\|PubMed:15247229};
Catalytic activity:		Reaction=1,2-dibutyryl-sn-glycero-3-phospho-(1D-myo-inositol-5- phosphate) + H2O = 1,2-dibutyryl-sn-glycero-3-phospho-(1D-myo- inositol) + phosphate; Xref=Rhea:RHEA:42584, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:82605, ChEBI:CHEBI:82606; Evidence={ECO:0000269\|PubMed:15247229}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42585; Evidence={ECO:0000269\|PubMed:15247229};
Pathway:		Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 2/2. {ECO:0000269\|PubMed:21641550}.
Subunit:		Interacts with STYXL1; the interaction inhibits PTPMT1 catalytic activity. {ECO:0000250\|UniProtKB:Q8WUK0}.
Subcellular location:		Mitochondrion inner membrane {ECO:0000269\|PubMed:16039589}; Peripheral membrane protein {ECO:0000250\|UniProtKB:P0C089}; Matrix side {ECO:0000250\|UniProtKB:P0C089}.
Tissue specificity:		Predominantly expressed in testis. Expressed at lower level in heart, brain, spleen, lung, liver, skeletal muscle, kidney, bone marrow, eye, lymph node, smooth muscle, prostate, thymus, stomach and uterus. {ECO:0000269\|PubMed:15247229}.
Disruption phenotype:		Mice die prior to E8.5. {ECO:0000269\|PubMed:21641550}.
Similarity:		Belongs to the protein-tyrosine phosphatase family. Non- receptor class dual specificity subfamily. {ECO:0000305}.
Sequence caution:		Sequence=AAH26750.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; Sequence=BAB28400.1; Type=Frameshift; Evidence={ECO:0000305}; Sequence=BAB29504.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};