ID   PTPM1_MOUSE             Reviewed;         193 AA.
AC   Q66GT5; Q9CSJ8; Q9D622;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 139.
DE   RecName: Full=Phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1 {ECO:0000305};
DE            EC=3.1.3.27 {ECO:0000269|PubMed:21641550, ECO:0000269|PubMed:21730175};
DE   AltName: Full=PTEN-like phosphatase;
DE   AltName: Full=Phosphoinositide lipid phosphatase;
DE   AltName: Full=Protein-tyrosine phosphatase mitochondrial 1;
DE            EC=3.1.3.16 {ECO:0000250|UniProtKB:P0C089};
DE            EC=3.1.3.48 {ECO:0000255|PROSITE-ProRule:PRU10044};
DE   Flags: Precursor;
GN   Name=Ptpmt1 {ECO:0000312|MGI:MGI:1913711}; Synonyms=Plip;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION, TISSUE SPECIFICITY, MUTAGENESIS OF CYS-132, AND CATALYTIC
RP   ACTIVITY.
RX   PubMed=15247229; DOI=10.1074/jbc.m404959200;
RA   Pagliarini D.J., Worby C.A., Dixon J.E.;
RT   "A PTEN-like phosphatase with a novel substrate specificity.";
RL   J. Biol. Chem. 279:38590-38596(2004).
RN   [4]
RP   SUBCELLULAR LOCATION, AND MUTAGENESIS OF 2-ALA--THR-19 AND 2-ALA--TRP-37.
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).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and
RC   Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
RP   FUNCTION AS PHOSPHATIDYLGLYCEROPHOSPHATASE, CATALYTIC ACTIVITY, PATHWAY,
RP   DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-132.
RX   PubMed=21641550; DOI=10.1016/j.cmet.2011.04.007;
RA   Zhang J., Guan Z., Murphy A.N., Wiley S.E., Perkins G.A., Worby C.A.,
RA   Engel J.L., Heacock P., Nguyen O.K., Wang J.H., Raetz C.R., Dowhan W.,
RA   Dixon J.E.;
RT   "Mitochondrial phosphatase PTPMT1 is essential for cardiolipin
RT   biosynthesis.";
RL   Cell Metab. 13:690-700(2011).
RN   [7]
RP   SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-85, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 37-193 IN COMPLEX WITH
RP   PHOSPHATIDYLINOSITOL 5-PHOSPHATE, CATALYTIC ACTIVITY, AND MUTAGENESIS OF
RP   GLU-73; GLU-76; ASP-101 AND CYS-132.
RX   PubMed=21730175; DOI=10.1073/pnas.1109290108;
RA   Xiao J., Engel J.L., Zhang J., Chen M.J., Manning G., Dixon J.E.;
RT   "Structural and functional analysis of PTPMT1, a phosphatase required for
RT   cardiolipin synthesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:11860-11865(2011).
CC   -!- FUNCTION: Lipid phosphatase which dephosphorylates
CC       phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG)
CC       (PubMed:21641550, PubMed:21730175). PGP is an essential intermediate in
CC       the biosynthetic pathway of cardiolipin, a mitochondrial-specific
CC       phospholipid regulating the membrane integrity and activities of the
CC       organelle (PubMed:21641550). Has also been shown to display phosphatase
CC       activity toward phosphoprotein substrates, specifically mediates
CC       dephosphorylation of mitochondrial proteins, thereby playing an
CC       essential role in ATP production (By similarity). Has probably a
CC       preference for proteins phosphorylated on Ser and/or Thr residues
CC       compared to proteins phosphorylated on Tyr residues (By similarity).
CC       Probably involved in regulation of insulin secretion in pancreatic beta
CC       cells (By similarity). May prevent intrinsic apoptosis, probably by
CC       regulating mitochondrial membrane integrity (By similarity).
CC       {ECO:0000250|UniProtKB:P0C089, ECO:0000250|UniProtKB:Q8WUK0,
CC       ECO:0000269|PubMed:16039589, ECO:0000269|PubMed:21641550}.
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:0000269|PubMed:21641550, ECO:0000269|PubMed:21730175};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33752;
CC         Evidence={ECO:0000269|PubMed:21641550, ECO:0000269|PubMed:21730175};
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:0000250|UniProtKB:P0C089};
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:0000250|UniProtKB:P0C089};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47005;
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:0000269|PubMed:21730175};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42305;
CC         Evidence={ECO:0000269|PubMed:21730175};
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:0000269|PubMed:15247229};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42309;
CC         Evidence={ECO:0000269|PubMed:15247229};
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:0000269|PubMed:15247229};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42321;
CC         Evidence={ECO:0000269|PubMed:15247229};
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:0000269|PubMed:15247229};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42585;
CC         Evidence={ECO:0000269|PubMed:15247229};
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylglycerol biosynthesis;
CC       phosphatidylglycerol from CDP-diacylglycerol: step 2/2.
CC       {ECO:0000269|PubMed:21641550}.
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:0000250|UniProtKB:P0C089}; Matrix side
CC       {ECO:0000250|UniProtKB:P0C089}.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in testis. Expressed at
CC       lower level in heart, brain, spleen, lung, liver, skeletal muscle,
CC       kidney, bone marrow, eye, lymph node, smooth muscle, prostate, thymus,
CC       stomach and uterus. {ECO:0000269|PubMed:15247229}.
CC   -!- DISRUPTION PHENOTYPE: Mice die prior to E8.5.
CC       {ECO:0000269|PubMed:21641550}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class dual specificity subfamily. {ECO:0000305}.
CC   -!- CAUTION: Was originally (PubMed:15247229) thought to have
CC       phosphatidylinositol 5-phosphatase activity, however, it was later
CC       shown (PubMed:16039589) that it is probably not the case in vivo.
CC       {ECO:0000305|PubMed:15247229, ECO:0000305|PubMed:16039589}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH26750.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB28400.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAB29504.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK012674; BAB28400.1; ALT_FRAME; mRNA.
DR   EMBL; AK014691; BAB29504.1; ALT_INIT; mRNA.
DR   EMBL; BC026750; AAH26750.1; ALT_INIT; mRNA.
DR   EMBL; BK005540; DAA05585.1; -; mRNA.
DR   RefSeq; NP_079852.1; NM_025576.2.
DR   PDB; 3RGO; X-ray; 1.93 A; A=37-193.
DR   PDB; 3RGQ; X-ray; 2.05 A; A=36-191.
DR   PDBsum; 3RGO; -.
DR   PDBsum; 3RGQ; -.
DR   AlphaFoldDB; Q66GT5; -.
DR   SMR; Q66GT5; -.
DR   BioGRID; 211491; 2.
DR   STRING; 10090.ENSMUSP00000159164; -.
DR   SwissLipids; SLP:000000643; -.
DR   iPTMnet; Q66GT5; -.
DR   PhosphoSitePlus; Q66GT5; -.
DR   EPD; Q66GT5; -.
DR   MaxQB; Q66GT5; -.
DR   PeptideAtlas; Q66GT5; -.
DR   ProteomicsDB; 302012; -.
DR   Pumba; Q66GT5; -.
DR   Antibodypedia; 6453; 197 antibodies from 28 providers.
DR   DNASU; 66461; -.
DR   Ensembl; ENSMUST00000111461.13; ENSMUSP00000159390.2; ENSMUSG00000063235.19.
DR   GeneID; 66461; -.
DR   KEGG; mmu:66461; -.
DR   AGR; MGI:1913711; -.
DR   CTD; 114971; -.
DR   MGI; MGI:1913711; Ptpmt1.
DR   GeneTree; ENSGT00390000014065; -.
DR   InParanoid; Q66GT5; -.
DR   OMA; NAHWRTV; -.
DR   OrthoDB; 1046951at2759; -.
DR   UniPathway; UPA00084; UER00504.
DR   BioGRID-ORCS; 66461; 7 hits in 20 CRISPR screens.
DR   ChiTaRS; Ptpmt1; mouse.
DR   EvolutionaryTrace; Q66GT5; -.
DR   PRO; PR:Q66GT5; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q66GT5; Protein.
DR   Bgee; ENSMUSG00000063235; Expressed in heart left ventricle and 73 other cell types or tissues.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:MGI.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008962; F:phosphatidylglycerophosphatase activity; IMP:UniProtKB.
DR   GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IDA:MGI.
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; IMP: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; ISO:MGI.
DR   GO; GO:0046488; P:phosphatidylinositol metabolic process; IC:MGI.
DR   GO; GO:2001242; P:regulation of intrinsic apoptotic signaling pathway; ISO:MGI.
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   3D-structure; Hydrolase; Lipid biosynthesis; Lipid metabolism; Membrane;
KW   Mitochondrion; 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_0000025424"
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:0007744|PubMed:23806337"
FT   MUTAGEN         2..37
FT                   /note="Missing: Loss of mitochondrion localization."
FT                   /evidence="ECO:0000269|PubMed:16039589"
FT   MUTAGEN         2..19
FT                   /note="Missing: Does not affect mitochondrion
FT                   localization."
FT                   /evidence="ECO:0000269|PubMed:16039589"
FT   MUTAGEN         73
FT                   /note="E->A: Fails to dephosphorylate PGP in vitro."
FT                   /evidence="ECO:0000269|PubMed:21730175"
FT   MUTAGEN         76
FT                   /note="E->A: Fails to dephosphorylate PGP in vitro."
FT                   /evidence="ECO:0000269|PubMed:21730175"
FT   MUTAGEN         101
FT                   /note="D->A: Fails to dephosphorylate PGP in vitro."
FT                   /evidence="ECO:0000269|PubMed:21730175"
FT   MUTAGEN         132
FT                   /note="C->S: Fails to dephosphorylate PGP in vitro. Does
FT                   not affect level of Akt phosphorylation."
FT                   /evidence="ECO:0000269|PubMed:15247229,
FT                   ECO:0000269|PubMed:21641550, ECO:0000269|PubMed:21730175"
FT   STRAND          38..40
FT                   /evidence="ECO:0007829|PDB:3RGO"
FT   STRAND          42..49
FT                   /evidence="ECO:0007829|PDB:3RGO"
FT   HELIX           53..55
FT                   /evidence="ECO:0007829|PDB:3RGO"
FT   HELIX           56..62
FT                   /evidence="ECO:0007829|PDB:3RGO"
FT   STRAND          65..72
FT                   /evidence="ECO:0007829|PDB:3RGO"
FT   TURN            75..79
FT                   /evidence="ECO:0007829|PDB:3RGO"
FT   HELIX           84..89
FT                   /evidence="ECO:0007829|PDB:3RGO"
FT   STRAND          93..97
FT                   /evidence="ECO:0007829|PDB:3RGO"
FT   TURN            101..103
FT                   /evidence="ECO:0007829|PDB:3RGO"
FT   HELIX           108..124
FT                   /evidence="ECO:0007829|PDB:3RGO"
FT   STRAND          127..137
FT                   /evidence="ECO:0007829|PDB:3RGO"
FT   HELIX           138..151
FT                   /evidence="ECO:0007829|PDB:3RGO"
FT   HELIX           155..165
FT                   /evidence="ECO:0007829|PDB:3RGO"
FT   HELIX           173..190
FT                   /evidence="ECO:0007829|PDB:3RGO"
SQ   SEQUENCE   193 AA;  21943 MW;  740D39798855D439 CRC64;
     MAASAWLEAG LARVLFYPTL LYTVFRGRVR GPAHRDWYHR IDHTVLLGAL PLKNMTRRLV
     LDENVRGVIT MNEEYETRFL CNTSKEWKKA GVEQLRLSTV DMTGVPTLAN LHKGVQFALK
     YQALGQCVYV HCKAGRSRSA TMVAAYLIQV HNWSPEEAIE AIAKIRSHIS IRPSQLEVLK
     EFHKEITARA AKN
//