PTPM1_RAT
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-AUG-2022, entry version 109.
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}.
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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 AlphaFoldDB; P0C089; -.
DR SMR; P0C089; -.
DR STRING; 10116.ENSRNOP00000013584; -.
DR jPOST; P0C089; -.
DR PaxDb; P0C089; -.
DR PeptideAtlas; P0C089; -.
DR PRIDE; P0C089; -.
DR UCSC; RGD:1589783; rat.
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:0031305; C:integral component of 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:0061179; P:negative regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:RGD.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:2001242; P:regulation of intrinsic apoptotic signaling pathway; ISO:RGD.
DR CDD; cd14524; PTPMT1; 1.
DR Gene3D; 3.90.190.10; -; 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; PTHR46712; 1.
DR Pfam; PF00782; DSPc; 1.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; SSF52799; 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
