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Protein

Phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1

Gene

Ptpmt1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Lipid phosphatase which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG). PGP is an essential intermediate in the biosynthetic pathway of cardiolipin, a mitochondrial-specific phospholipid regulating the membrane integrity and activities of the organelle. 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. Has probably a preference for proteins phosphorylated on Ser and/or Thr residues compared to proteins phosphorylated on Tyr residues. Probably involved in regulation of insulin secretion in pancreatic beta cells (By similarity).By similarity2 Publications

Catalytic activityi

Phosphatidylglycerophosphate + H2O = phosphatidylglycerol + phosphate.
Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation
[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Pathwayi: phosphatidylglycerol biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes phosphatidylglycerol from CDP-diacylglycerol.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, mitochondrial (Pgs1)
  2. Phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1 (Ptpmt1)
This subpathway is part of the pathway phosphatidylglycerol biosynthesis, which is itself part of Phospholipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes phosphatidylglycerol from CDP-diacylglycerol, the pathway phosphatidylglycerol biosynthesis and in Phospholipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei132Phosphocysteine intermediatePROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

  • cardiolipin biosynthetic process Source: UniProtKB
  • phosphatidylglycerol biosynthetic process Source: Reactome
  • phosphatidylinositol metabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

ReactomeiR-MMU-1483148. Synthesis of PG.
UniPathwayiUPA00084; UER00504.

Chemistry databases

SwissLipidsiSLP:000000643.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1 (EC:3.1.3.27)
Alternative name(s):
PTEN-like phosphatase
Phosphoinositide lipid phosphatase
Protein-tyrosine phosphatase mitochondrial 1 (EC:3.1.3.16, EC:3.1.3.48)
Gene namesi
Name:Ptpmt1
Synonyms:Plip
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1913711. Ptpmt1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial inner membrane Source: MGI
  • mitochondrion Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Disruption phenotypei

Mice die prior to E8.5.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi73E → A: Fails to dephosphorylate PGP in vitro. 1 Publication1
Mutagenesisi76E → A: Fails to dephosphorylate PGP in vitro. 1 Publication1
Mutagenesisi101D → A: Fails to dephosphorylate PGP in vitro. 1 Publication1
Mutagenesisi132C → S: Does not affect level of Akt phosphorylation; Fails to dephosphorylate PGP in vitro. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 31MitochondrionSequence analysisAdd BLAST31
ChainiPRO_000002542432 – 193Phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1Add BLAST162

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei85N6-succinyllysineCombined sources1

Proteomic databases

EPDiQ66GT5.
MaxQBiQ66GT5.
PaxDbiQ66GT5.
PeptideAtlasiQ66GT5.
PRIDEiQ66GT5.

PTM databases

iPTMnetiQ66GT5.
PhosphoSitePlusiQ66GT5.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

CleanExiMM_PTPMT1.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000077036.

Structurei

Secondary structure

1193
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi38 – 40Combined sources3
Beta strandi42 – 49Combined sources8
Helixi53 – 55Combined sources3
Helixi56 – 62Combined sources7
Beta strandi65 – 72Combined sources8
Turni75 – 79Combined sources5
Helixi84 – 89Combined sources6
Beta strandi93 – 97Combined sources5
Turni101 – 103Combined sources3
Helixi108 – 124Combined sources17
Beta strandi127 – 137Combined sources11
Helixi138 – 151Combined sources14
Helixi155 – 165Combined sources11
Helixi173 – 190Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3RGOX-ray1.93A37-193[»]
3RGQX-ray2.05A36-191[»]
ProteinModelPortaliQ66GT5.
SMRiQ66GT5.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ66GT5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini109 – 177Tyrosine-protein phosphataseAdd BLAST69

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1719. Eukaryota.
ENOG4111IMR. LUCA.
HOVERGENiHBG079822.
InParanoidiQ66GT5.
KOiK14165.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR000340. Dual-sp_phosphatase_cat-dom.
IPR024950. DUSP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR016130. Tyr_Pase_AS.
IPR000387. TYR_PHOSPHATASE_dom.
IPR020422. TYR_PHOSPHATASE_DUAL_dom.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00782. DSPc. 1 hit.
[Graphical view]
SMARTiSM00195. DSPc. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q66GT5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASAWLEAG LARVLFYPTL LYTVFRGRVR GPAHRDWYHR IDHTVLLGAL
60 70 80 90 100
PLKNMTRRLV LDENVRGVIT MNEEYETRFL CNTSKEWKKA GVEQLRLSTV
110 120 130 140 150
DMTGVPTLAN LHKGVQFALK YQALGQCVYV HCKAGRSRSA TMVAAYLIQV
160 170 180 190
HNWSPEEAIE AIAKIRSHIS IRPSQLEVLK EFHKEITARA AKN
Length:193
Mass (Da):21,943
Last modified:October 11, 2004 - v1
Checksum:i740D39798855D439
GO

Sequence cautioni

The sequence AAH26750 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAB28400 differs from that shown. Reason: Frameshift at position 36.Curated
The sequence BAB29504 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK012674 mRNA. Translation: BAB28400.1. Frameshift.
AK014691 mRNA. Translation: BAB29504.1. Different initiation.
BC026750 mRNA. Translation: AAH26750.1. Different initiation.
BK005540 mRNA. Translation: DAA05585.1.
RefSeqiNP_079852.1. NM_025576.2.
UniGeneiMm.23926.

Genome annotation databases

GeneIDi66461.
KEGGimmu:66461.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK012674 mRNA. Translation: BAB28400.1. Frameshift.
AK014691 mRNA. Translation: BAB29504.1. Different initiation.
BC026750 mRNA. Translation: AAH26750.1. Different initiation.
BK005540 mRNA. Translation: DAA05585.1.
RefSeqiNP_079852.1. NM_025576.2.
UniGeneiMm.23926.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3RGOX-ray1.93A37-193[»]
3RGQX-ray2.05A36-191[»]
ProteinModelPortaliQ66GT5.
SMRiQ66GT5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000077036.

Chemistry databases

SwissLipidsiSLP:000000643.

PTM databases

iPTMnetiQ66GT5.
PhosphoSitePlusiQ66GT5.

Proteomic databases

EPDiQ66GT5.
MaxQBiQ66GT5.
PaxDbiQ66GT5.
PeptideAtlasiQ66GT5.
PRIDEiQ66GT5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi66461.
KEGGimmu:66461.

Organism-specific databases

CTDi114971.
MGIiMGI:1913711. Ptpmt1.

Phylogenomic databases

eggNOGiKOG1719. Eukaryota.
ENOG4111IMR. LUCA.
HOVERGENiHBG079822.
InParanoidiQ66GT5.
KOiK14165.

Enzyme and pathway databases

UniPathwayiUPA00084; UER00504.
ReactomeiR-MMU-1483148. Synthesis of PG.

Miscellaneous databases

EvolutionaryTraceiQ66GT5.
PROiQ66GT5.
SOURCEiSearch...

Gene expression databases

CleanExiMM_PTPMT1.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR000340. Dual-sp_phosphatase_cat-dom.
IPR024950. DUSP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR016130. Tyr_Pase_AS.
IPR000387. TYR_PHOSPHATASE_dom.
IPR020422. TYR_PHOSPHATASE_DUAL_dom.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00782. DSPc. 1 hit.
[Graphical view]
SMARTiSM00195. DSPc. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPTPM1_MOUSE
AccessioniPrimary (citable) accession number: Q66GT5
Secondary accession number(s): Q9CSJ8, Q9D622
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: October 11, 2004
Last modified: November 2, 2016
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Was originally (PubMed:15247229) thought to have phosphatidylinositol 5-phosphatase activity, however, it was later shown (PubMed:16039589) that it is probably not the case in vivo.2 Publications

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.