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P0C089

- PTPM1_RAT

UniProt

P0C089 - PTPM1_RAT

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Protein

Phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1

Gene

Ptpmt1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript 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 (By similarity). 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 similarity1 Publication

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei132 – 1321Phosphocysteine intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  1. phosphatidylglycerophosphatase activity Source: UniProtKB
  2. phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity Source: RefGenome
  3. protein tyrosine/serine/threonine phosphatase activity Source: RefGenome
  4. protein tyrosine phosphatase activity Source: UniProtKB-EC

GO - Biological processi

  1. cardiolipin biosynthetic process Source: UniProtKB
  2. inositol phosphate dephosphorylation Source: RefGenome
  3. protein dephosphorylation Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

ReactomeiREACT_199140. Synthesis of PG.
UniPathwayiUPA00084; UER00504.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1 (EC:3.1.3.27)
Alternative name(s):
Protein-tyrosine phosphatase mitochondrial 1 (EC:3.1.3.16, EC:3.1.3.48)
Gene namesi
Name:Ptpmt1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi1589783. Ptpmt1.

Subcellular locationi

Mitochondrion inner membrane By similarity
Note: Associated with the inner membrane.By similarity

GO - Cellular componenti

  1. integral component of mitochondrial inner membrane Source: RGD
  2. nucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3131MitochondrionSequence AnalysisAdd
BLAST
Chaini32 – 193162Phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1PRO_0000025425Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei85 – 851N6-succinyllysineBy similarity

Proteomic databases

PaxDbiP0C089.
PRIDEiP0C089.

Expressioni

Gene expression databases

ExpressionAtlasiP0C089. baseline.
GenevestigatoriP0C089.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000013584.

Structurei

3D structure databases

ProteinModelPortaliP0C089.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini109 – 17769Tyrosine-protein phosphataseAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiNOG146651.
HOGENOMiHOG000220855.
HOVERGENiHBG079822.
InParanoidiP0C089.
PhylomeDBiP0C089.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR000340. Dual-sp_phosphatase_cat-dom.
IPR024950. DUSP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00782. 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.

P0C089-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAASAWLEAG LARVLFYPTL LYTVFRGRVG GPAHRDWYHR IDHTVLLGAL
60 70 80 90 100
PLRSMTRRLV LDENVRGVIT MNEEYETRFL CNTSKEWKNV GVEQLRLSTV
110 120 130 140 150
DMTGVPTLAN LHRGVQFALK YQSLGQCVYV HCKAGRSRSA TMVAAYLIQV
160 170 180 190
HNWSPEEAIE AIAKIRSHIS IRPSQLEILK EFHKEIAARA AKN
Length:193
Mass (Da):21,886
Last modified:August 16, 2005 - v1
Checksum:i04529D5BFD801A90
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AABR03026072 mRNA. No translation available.
AABR03030907 mRNA. No translation available.
AABR03026441 mRNA. No translation available.
UniGeneiRn.108023.

Genome annotation databases

UCSCiRGD:1589783. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AABR03026072 mRNA. No translation available.
AABR03030907 mRNA. No translation available.
AABR03026441 mRNA. No translation available.
UniGenei Rn.108023.

3D structure databases

ProteinModelPortali P0C089.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000013584.

Proteomic databases

PaxDbi P0C089.
PRIDEi P0C089.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

UCSCi RGD:1589783. rat.

Organism-specific databases

RGDi 1589783. Ptpmt1.

Phylogenomic databases

eggNOGi NOG146651.
HOGENOMi HOG000220855.
HOVERGENi HBG079822.
InParanoidi P0C089.
PhylomeDBi P0C089.

Enzyme and pathway databases

UniPathwayi UPA00084 ; UER00504 .
Reactomei REACT_199140. Synthesis of PG.

Miscellaneous databases

PROi P0C089.

Gene expression databases

ExpressionAtlasi P0C089. baseline.
Genevestigatori P0C089.

Family and domain databases

Gene3Di 3.90.190.10. 1 hit.
InterProi IPR000340. Dual-sp_phosphatase_cat-dom.
IPR024950. DUSP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view ]
PANTHERi PTHR10159. PTHR10159. 1 hit.
Pfami PF00782. DSPc. 1 hit.
[Graphical view ]
SUPFAMi SSF52799. SSF52799. 1 hit.
PROSITEi PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "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.

Entry informationi

Entry nameiPTPM1_RAT
AccessioniPrimary (citable) accession number: P0C089
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: August 16, 2005
Last modified: October 29, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Its absence in pancreatic insulinoma cell line INS-1 832/13 alters the mitochondrial phosphoprotein profile and markedly enhances both ATP production and insulin secretion, suggesting that it may serve as a drug target for the treatment of type II diabetes.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3