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 03-APR-2013, entry version 59.
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 -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC tyrosine + phosphate.
CC -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC 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 (By
CC similarity). Note=Associated with the inner membrane (By
CC similarity).
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.
CC -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
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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 IPI; IPI00207732; -.
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 OrthoDB; EOG4WWRKR; -.
DR UniPathway; UPA00084; UER00504.
DR Genevestigator; P0C089; -.
DR GermOnline; ENSRNOG00000009723; Rattus norvegicus.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:RefGenome.
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: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:0035335; P:peptidyl-tyrosine dephosphorylation; IEA:GOC.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR024950; DUSP.
DR InterPro; IPR000387; Tyr/Dual-sp_Pase.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR PANTHER; PTHR10159; PTHR10159; 1.
DR Pfam; PF00782; DSPc; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; FALSE_NEG.
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 (Potential).
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 (By
FT similarity).
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
//
