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 24-JAN-2024, entry version 114. DE RecName: Full=Phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1 {ECO:0000305}; DE EC=3.1.3.27 {ECO:0000250|UniProtKB:Q66GT5}; DE AltName: Full=Protein-tyrosine phosphatase mitochondrial 1; DE EC=3.1.3.16 {ECO:0000305|PubMed:16039589}; DE EC=3.1.3.48 {ECO:0000255|PROSITE-ProRule:PRU10044}; DE Flags: Precursor; GN Name=Ptpmt1 {ECO:0000312|RGD:1589783}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC 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., Smith D., RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., RA Zdobnov E., 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., Schmidt J., RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., RA Lazar J., 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., Webber C., RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., RA Mockrin S., Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into mammalian RT evolution."; RL Nature 428:493-521(2004). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. 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., Worby C.A., RA 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) (By CC similarity). PGP is an essential intermediate in the biosynthetic CC pathway of cardiolipin, a mitochondrial-specific phospholipid CC regulating the membrane integrity and activities of the organelle (By CC similarity). Has also been shown to display phosphatase activity toward CC phosphoprotein substrates, specifically mediates dephosphorylation of CC mitochondrial proteins, thereby playing an essential role in ATP CC production (PubMed:16039589). Has probably a preference for proteins CC phosphorylated on Ser and/or Thr residues compared to proteins CC phosphorylated on Tyr residues (PubMed:16039589). Probably involved in CC regulation of insulin secretion in pancreatic beta cells CC (PubMed:16039589). May prevent intrinsic apoptosis, probably by CC regulating mitochondrial membrane integrity (By similarity). CC {ECO:0000250|UniProtKB:Q66GT5, ECO:0000250|UniProtKB:Q8WUK0, CC ECO:0000269|PubMed:16039589}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA- CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU10044}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10685; CC Evidence={ECO:0000305}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:83421; EC=3.1.3.16; CC Evidence={ECO:0000305|PubMed:16039589}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20630; CC Evidence={ECO:0000305}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:61977; EC=3.1.3.16; CC Evidence={ECO:0000305|PubMed:16039589}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47005; CC Evidence={ECO:0000305}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + CC H2O = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + phosphate; CC Xref=Rhea:RHEA:33751, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:60110, ChEBI:CHEBI:64716; EC=3.1.3.27; CC Evidence={ECO:0000250|UniProtKB:Q66GT5}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33752; CC Evidence={ECO:0000305}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol- CC 3'-phosphate) + H2O = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho- CC (1'-sn-glycerol) + phosphate; Xref=Rhea:RHEA:42304, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:75163, CC ChEBI:CHEBI:78907; Evidence={ECO:0000250|UniProtKB:Q66GT5}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42305; CC Evidence={ECO:0000250|UniProtKB:Q66GT5}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-5- CC phosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo- CC inositol) + phosphate; Xref=Rhea:RHEA:42308, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:65221, ChEBI:CHEBI:78911; CC Evidence={ECO:0000250|UniProtKB:Q66GT5}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42309; CC Evidence={ECO:0000250|UniProtKB:Q66GT5}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1-acyl-2-hexanoyl-sn-glycero-3-phospho-(1D-myo-inositol-5- CC phosphate) + H2O = a 1-acyl-2-hexanoyl-sn-glycero-3-phospho-(1D-myo- CC inositol) + phosphate; Xref=Rhea:RHEA:42320, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:78930, ChEBI:CHEBI:78931; CC Evidence={ECO:0000250|UniProtKB:Q66GT5}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42321; CC Evidence={ECO:0000250|UniProtKB:Q66GT5}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2-dibutyryl-sn-glycero-3-phospho-(1D-myo-inositol-5- CC phosphate) + H2O = 1,2-dibutyryl-sn-glycero-3-phospho-(1D-myo- CC inositol) + phosphate; Xref=Rhea:RHEA:42584, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:82605, ChEBI:CHEBI:82606; CC Evidence={ECO:0000250|UniProtKB:Q66GT5}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42585; CC Evidence={ECO:0000250|UniProtKB:Q66GT5}; CC -!- PATHWAY: Phospholipid metabolism; phosphatidylglycerol biosynthesis; CC phosphatidylglycerol from CDP-diacylglycerol: step 2/2. CC {ECO:0000250|UniProtKB:Q66GT5}. CC -!- SUBUNIT: Interacts with STYXL1; the interaction inhibits PTPMT1 CC catalytic activity. {ECO:0000250|UniProtKB:Q8WUK0}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000269|PubMed:16039589}; Peripheral membrane protein CC {ECO:0000269|PubMed:16039589}; Matrix side CC {ECO:0000269|PubMed:16039589}. CC -!- TISSUE SPECIFICITY: Expressed in liver and in pancreatic beta cells. CC {ECO:0000269|PubMed:16039589}. CC -!- MISCELLANEOUS: Its absence in pancreatic insulinoma cell line INS-1 CC 832/13 alters the mitochondrial phosphoprotein profile and markedly CC enhances both ATP production and insulin secretion, suggesting that it CC may serve as a drug target for the treatment of type II diabetes. CC {ECO:0000269|PubMed:16039589}. CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- CC receptor class dual specificity subfamily. {ECO:0000305}. CC -!- CAUTION: Does not have phosphatidylinositol 5-phosphatase activity. CC {ECO:0000305|PubMed:16039589}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AABR03026072; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AABR03030907; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AABR03026441; -; NOT_ANNOTATED_CDS; mRNA. DR AlphaFoldDB; P0C089; -. DR SMR; P0C089; -. DR STRING; 10116.ENSRNOP00000013584; -. DR PhosphoSitePlus; P0C089; -. DR jPOST; P0C089; -. DR PaxDb; 10116-ENSRNOP00000013584; -. DR PeptideAtlas; P0C089; -. DR UCSC; RGD:1589783; rat. DR AGR; RGD:1589783; -. DR RGD; 1589783; Ptpmt1. DR eggNOG; KOG1719; Eukaryota. DR InParanoid; P0C089; -. DR PhylomeDB; P0C089; -. DR UniPathway; UPA00084; UER00504. DR PRO; PR:P0C089; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:RGD. DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central. DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0008962; F:phosphatidylglycerophosphatase activity; ISS:UniProtKB. DR GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; ISO:RGD. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro. DR GO; GO:0032049; P:cardiolipin biosynthetic process; ISS:UniProtKB. DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro. DR GO; GO:0061179; P:negative regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:RGD. DR GO; GO:2001242; P:regulation of intrinsic apoptotic signaling pathway; ISO:RGD. DR CDD; cd14524; PTPMT1; 1. DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1. DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom. DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like. DR InterPro; IPR042165; PTPMT1. DR InterPro; IPR044596; PTPMT1-like. DR InterPro; IPR016130; Tyr_Pase_AS. DR InterPro; IPR000387; Tyr_Pase_dom. DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom. DR PANTHER; PTHR46712; PHOSPHATIDYLGLYCEROPHOSPHATASE AND PROTEIN-TYROSINE PHOSPHATASE 1; 1. DR PANTHER; PTHR46712:SF1; PHOSPHATIDYLGLYCEROPHOSPHATASE AND PROTEIN-TYROSINE PHOSPHATASE 1; 1. DR Pfam; PF00782; DSPc; 1. DR SMART; SM00195; DSPc; 1. DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1. DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1. DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1. DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1. PE 1: Evidence at protein level; KW Hydrolase; Lipid biosynthesis; Lipid metabolism; Membrane; Mitochondrion; KW Mitochondrion inner membrane; Phospholipid biosynthesis; KW Phospholipid metabolism; Protein phosphatase; Reference proteome; KW Transit peptide. FT TRANSIT 1..31 FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN 32..193 FT /note="Phosphatidylglycerophosphatase and protein-tyrosine FT phosphatase 1" FT /id="PRO_0000025425" FT DOMAIN 37..188 FT /note="Tyrosine-protein phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" FT ACT_SITE 132 FT /note="Phosphocysteine intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" FT MOD_RES 85 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q66GT5" 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 //