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Database: UniProt
Entry: P0C089
LinkDB: P0C089
Original site: P0C089 
ID   PTPM1_RAT               Reviewed;         193 AA.
AC   P0C089;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 1.
DT   01-OCT-2014, entry version 72.
DE   RecName: Full=Phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1;
DE            EC=3.1.3.27;
DE   AltName: Full=Protein-tyrosine phosphatase mitochondrial 1;
DE            EC=3.1.3.16;
DE            EC=3.1.3.48;
DE   Flags: Precursor;
GN   Name=Ptpmt1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
RA   Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
RA   Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
RA   Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
RA   Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
RA   Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
RA   Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
RA   Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
RA   Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
RA   D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
RA   Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
RA   Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
RA   Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
RA   Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
RA   Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
RA   Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
RA   Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
RA   Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
RA   Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
RA   Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
RA   Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
RA   Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
RA   Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
RA   Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
RA   Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
RA   Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
RA   Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
RA   Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
RA   Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
RA   Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
RA   Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
RA   Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
RA   Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
RA   Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
RA   Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into
RT   mammalian evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   FUNCTION.
RX   PubMed=16039589; DOI=10.1016/j.molcel.2005.06.008;
RA   Pagliarini D.J., Wiley S.E., Kimple M.E., Dixon J.R., Kelly P.,
RA   Worby C.A., Casey P.J., Dixon J.E.;
RT   "Involvement of a mitochondrial phosphatase in the regulation of ATP
RT   production and insulin secretion in pancreatic beta cells.";
RL   Mol. Cell 19:197-207(2005).
CC   -!- FUNCTION: Lipid phosphatase which dephosphorylates
CC       phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG).
CC       PGP is an essential intermediate in the biosynthetic pathway of
CC       cardiolipin, a mitochondrial-specific phospholipid regulating the
CC       membrane integrity and activities of the organelle (By
CC       similarity). Has also been shown to display phosphatase activity
CC       toward phosphoprotein substrates, specifically mediates
CC       dephosphorylation of mitochondrial proteins, thereby playing an
CC       essential role in ATP production. Has probably a preference for
CC       proteins phosphorylated on Ser and/or Thr residues compared to
CC       proteins phosphorylated on Tyr residues. Probably involved in
CC       regulation of insulin secretion in pancreatic beta cells.
CC       {ECO:0000250, ECO:0000269|PubMed:16039589}.
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate. {ECO:0000255|PROSITE-ProRule:PRU10044}.
CC   -!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O
CC       = [a protein]-serine/threonine + phosphate.
CC   -!- CATALYTIC ACTIVITY: Phosphatidylglycerophosphate + H(2)O =
CC       phosphatidylglycerol + phosphate.
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylglycerol
CC       biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step
CC       2/2.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}.
CC       Note=Associated with the inner membrane. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Its absence in pancreatic insulinoma cell line INS-
CC       1 832/13 alters the mitochondrial phosphoprotein profile and
CC       markedly enhances both ATP production and insulin secretion,
CC       suggesting that it may serve as a drug target for the treatment of
CC       type II diabetes.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Non-receptor class dual specificity subfamily. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
CC       {ECO:0000305}.
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DR   EMBL; AABR03026072; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AABR03030907; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AABR03026441; -; NOT_ANNOTATED_CDS; mRNA.
DR   UniGene; Rn.108023; -.
DR   ProteinModelPortal; P0C089; -.
DR   STRING; 10116.ENSRNOP00000013584; -.
DR   PaxDb; P0C089; -.
DR   PRIDE; P0C089; -.
DR   UCSC; RGD:1589783; rat.
DR   RGD; 1589783; Ptpmt1.
DR   eggNOG; NOG146651; -.
DR   HOGENOM; HOG000220855; -.
DR   HOVERGEN; HBG079822; -.
DR   InParanoid; P0C089; -.
DR   PhylomeDB; P0C089; -.
DR   Reactome; REACT_199140; Synthesis of PG.
DR   UniPathway; UPA00084; UER00504.
DR   PRO; PR:P0C089; -.
DR   Genevestigator; P0C089; -.
DR   GO; GO:0031305; C:integral component of mitochondrial inner membrane; IDA:RGD.
DR   GO; GO:0008962; F:phosphatidylglycerophosphatase activity; ISS:UniProtKB.
DR   GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IBA:RefGenome.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IBA:RefGenome.
DR   GO; GO:0032049; P:cardiolipin biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0046855; P:inositol phosphate dephosphorylation; IBA:RefGenome.
DR   GO; GO:0006470; P:protein dephosphorylation; IBA:RefGenome.
DR   Gene3D; 3.90.190.10; -; 1.
DR   InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR   InterPro; IPR024950; DUSP.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000387; Tyr/Dual-sp_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   PANTHER; PTHR10159; PTHR10159; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   SUPFAM; SSF52799; SSF52799; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Hydrolase; Lipid biosynthesis; Lipid metabolism;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Phospholipid biosynthesis; Phospholipid metabolism;
KW   Protein phosphatase; Reference proteome; Transit peptide.
FT   TRANSIT       1     31       Mitochondrion. {ECO:0000255}.
FT   CHAIN        32    193       Phosphatidylglycerophosphatase and
FT                                protein-tyrosine phosphatase 1.
FT                                /FTId=PRO_0000025425.
FT   DOMAIN      109    177       Tyrosine-protein phosphatase.
FT   ACT_SITE    132    132       Phosphocysteine intermediate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10044}.
FT   MOD_RES      85     85       N6-succinyllysine. {ECO:0000250}.
SQ   SEQUENCE   193 AA;  21886 MW;  04529D5BFD801A90 CRC64;
     MAASAWLEAG LARVLFYPTL LYTVFRGRVG GPAHRDWYHR IDHTVLLGAL PLRSMTRRLV
     LDENVRGVIT MNEEYETRFL CNTSKEWKNV GVEQLRLSTV DMTGVPTLAN LHRGVQFALK
     YQSLGQCVYV HCKAGRSRSA TMVAAYLIQV HNWSPEEAIE AIAKIRSHIS IRPSQLEILK
     EFHKEIAARA AKN
//
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