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P0C089

- PTPM1_RAT

UniProt

P0C089 - PTPM1_RAT

Protein

Phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1

Gene

Ptpmt1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 1 (16 Aug 2005)
      Previous versions | rss
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    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

    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

    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

    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

    MAASAWLEAG LARVLFYPTL LYTVFRGRVG GPAHRDWYHR IDHTVLLGAL    50
    PLRSMTRRLV LDENVRGVIT MNEEYETRFL CNTSKEWKNV GVEQLRLSTV 100
    DMTGVPTLAN LHRGVQFALK YQSLGQCVYV HCKAGRSRSA TMVAAYLIQV 150
    HNWSPEEAIE AIAKIRSHIS IRPSQLEILK EFHKEIAARA AKN 193
    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

    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

    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 1, 2014
    This is version 72 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