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Q66GT5 (PTPM1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Ptpmt1
Synonyms:Plip
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length193 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4 Ref.5

Catalytic activity

Phosphatidylglycerophosphate + H2O = phosphatidylglycerol + phosphate.

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Pathway

Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 2/2.

Subcellular location

Mitochondrion inner membrane. Note: Associated with the inner membrane. Ref.4

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. Ref.3

Disruption phenotype

Mice die prior to E8.5. Ref.5

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily.

Contains 1 tyrosine-protein phosphatase domain.

Caution

Was originally (Ref.3) thought to have phosphatidylinositol 5-phosphatase activity, however, it was later shown (Ref.4) that it is probably not the case in vivo.

Sequence caution

The sequence AAH26750.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAB28400.1 differs from that shown. Reason: Frameshift at position 36.

The sequence BAB29504.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3131Mitochondrion Potential
Chain32 – 193162Phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1
PRO_0000025424

Regions

Domain109 – 17769Tyrosine-protein phosphatase

Sites

Active site1321Phosphocysteine intermediate By similarity

Amino acid modifications

Modified residue851N6-succinyllysine Ref.6

Experimental info

Mutagenesis731E → A: Fails to dephosphorylate PGP in vitro. Ref.7
Mutagenesis761E → A: Fails to dephosphorylate PGP in vitro. Ref.7
Mutagenesis1011D → A: Fails to dephosphorylate PGP in vitro. Ref.7
Mutagenesis1321C → S: Does not affect level of Akt phosphorylation; Fails to dephosphorylate PGP in vitro. Ref.3 Ref.7

Secondary structure

........................... 193
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q66GT5 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 740D39798855D439

FASTA19321,943
        10         20         30         40         50         60 
MAASAWLEAG LARVLFYPTL LYTVFRGRVR GPAHRDWYHR IDHTVLLGAL PLKNMTRRLV 

        70         80         90        100        110        120 
LDENVRGVIT MNEEYETRFL CNTSKEWKKA GVEQLRLSTV DMTGVPTLAN LHKGVQFALK 

       130        140        150        160        170        180 
YQALGQCVYV HCKAGRSRSA TMVAAYLIQV HNWSPEEAIE AIAKIRSHIS IRPSQLEVLK 

       190 
EFHKEITARA AKN 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Head.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Liver.
[3]"A PTEN-like phosphatase with a novel substrate specificity."
Pagliarini D.J., Worby C.A., Dixon J.E.
J. Biol. Chem. 279:38590-38596(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION, TISSUE SPECIFICITY, MUTAGENESIS OF CYS-132.
[4]"Involvement of a mitochondrial phosphatase in the regulation of ATP production and insulin secretion in pancreatic beta cells."
Pagliarini D.J., Wiley S.E., Kimple M.E., Dixon J.R., Kelly P., Worby C.A., Casey P.J., Dixon J.E.
Mol. Cell 19:197-207(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS PROTEIN PHOSPHATASE, SUBCELLULAR LOCATION.
[5]"Mitochondrial phosphatase PTPMT1 is essential for cardiolipin biosynthesis."
Zhang J., Guan Z., Murphy A.N., Wiley S.E., Perkins G.A., Worby C.A., Engel J.L., Heacock P., Nguyen O.K., Wang J.H., Raetz C.R., Dowhan W., Dixon J.E.
Cell Metab. 13:690-700(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS PHOSPHATIDYLGLYCEROPHOSPHATASE, DISRUPTION PHENOTYPE.
[6]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-85, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[7]"Structural and functional analysis of PTPMT1, a phosphatase required for cardiolipin synthesis."
Xiao J., Engel J.L., Zhang J., Chen M.J., Manning G., Dixon J.E.
Proc. Natl. Acad. Sci. U.S.A. 108:11860-11865(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 37-193 IN COMPLEX WITH PHOSPHATIDYLINOSITOL 5-PHOSPHATE, MUTAGENESIS OF GLU-73; GLU-76; ASP-101 AND CYS-132.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_079852.1. NM_025576.2.
UniGeneMm.23926.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3RGOX-ray1.93A37-193[»]
3RGQX-ray2.05A36-191[»]
ProteinModelPortalQ66GT5.
SMRQ66GT5. Positions 37-193.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ66GT5.

Proteomic databases

MaxQBQ66GT5.
PaxDbQ66GT5.
PRIDEQ66GT5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID66461.
KEGGmmu:66461.

Organism-specific databases

CTD114971.
MGIMGI:1913711. Ptpmt1.

Phylogenomic databases

eggNOGNOG146651.
HOVERGENHBG079822.
InParanoidQ66GT5.
KOK14165.

Enzyme and pathway databases

ReactomeREACT_188937. Metabolism.
UniPathwayUPA00084; UER00504.

Gene expression databases

CleanExMM_PTPMT1.
GenevestigatorQ66GT5.

Family and domain databases

Gene3D3.90.190.10. 1 hit.
InterProIPR000340. Dual-sp_phosphatase_cat-dom.
IPR024950. DUSP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERPTHR10159. PTHR10159. 1 hit.
PfamPF00782. DSPc. 1 hit.
[Graphical view]
SUPFAMSSF52799. SSF52799. 1 hit.
PROSITEPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ66GT5.
NextBio321760.
PROQ66GT5.
SOURCESearch...

Entry information

Entry namePTPM1_MOUSE
AccessionPrimary (citable) accession number: Q66GT5
Secondary accession number(s): Q9CSJ8, Q9D622
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: October 11, 2004
Last modified: June 11, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot