PTPM1_HUMAN
ID PTPM1_HUMAN Reviewed; 201 AA.
AC Q8WUK0; E9PAT8; Q7Z557; Q96CR2; Q9BXV8;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1 {ECO:0000305};
DE EC=3.1.3.27 {ECO:0000269|PubMed:24709986};
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|HGNC:HGNC:26965}; Synonyms=MOSP, PLIP;
GN ORFNames=PNAS-129;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Lin L., Ke R., Li H., Zhou G., Shen C., Yu R., Zhong G., Xiao W., Li M.,
RA Yang S.;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Cervix, Kidney, and Kidney adenocarcinoma;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 68-201 (ISOFORM 2).
RC TISSUE=Promyelocytic leukemia;
RA Yu W.-Q., Sun B.-Z., Chai Y.-B., Zhu F., Liu X.-S., Li Z., Lu F., Yan W.,
RA Yang H., Zhao Z.-L.;
RT "Human acute promyelocytic leukemia cell line NB4's
RT apoptosis/differentiation related genes.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH STYXL1, IDENTIFICATION BY
RP MASS SPECTROMETRY, AND MUTAGENESIS OF CYS-132.
RX PubMed=24709986; DOI=10.1371/journal.pone.0093896;
RA Niemi N.M., Sacoman J.L., Westrate L.M., Gaither L.A., Lanning N.J.,
RA Martin K.R., MacKeigan J.P.;
RT "The pseudophosphatase MK-STYX physically and genetically interacts with
RT the mitochondrial phosphatase PTPMT1.";
RL PLoS ONE 9:E93896-E93896(2014).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
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 (By similarity). Has probably a preference for proteins
CC phosphorylated on Ser and/or Thr residues compared to proteins
CC phosphorylated on Tyr residues (By similarity). Probably involved in
CC regulation of insulin secretion in pancreatic beta cells (By
CC similarity). May prevent intrinsic apoptosis, probably by regulating
CC mitochondrial membrane integrity (PubMed:24709986).
CC {ECO:0000250|UniProtKB:P0C089, ECO:0000250|UniProtKB:Q66GT5,
CC ECO:0000269|PubMed:24709986}.
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:24709986};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33752;
CC Evidence={ECO:0000305|PubMed:24709986};
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: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:0000269|PubMed:24709986}.
CC -!- INTERACTION:
CC Q8WUK0; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-7199479, EBI-10173507;
CC Q8WUK0; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-7199479, EBI-3867333;
CC Q8WUK0; P28799: GRN; NbExp=3; IntAct=EBI-7199479, EBI-747754;
CC Q8WUK0; Q15323: KRT31; NbExp=6; IntAct=EBI-7199479, EBI-948001;
CC Q8WUK0; O76011: KRT34; NbExp=3; IntAct=EBI-7199479, EBI-1047093;
CC Q8WUK0; Q6A162: KRT40; NbExp=3; IntAct=EBI-7199479, EBI-10171697;
CC Q8WUK0; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-7199479, EBI-11749135;
CC Q8WUK0; P60409: KRTAP10-7; NbExp=6; IntAct=EBI-7199479, EBI-10172290;
CC Q8WUK0; P60410: KRTAP10-8; NbExp=6; IntAct=EBI-7199479, EBI-10171774;
CC Q8WUK0; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-7199479, EBI-10172052;
CC Q8WUK0; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-7199479, EBI-11953334;
CC Q8WUK0; P0C7H8: KRTAP2-3; NbExp=3; IntAct=EBI-7199479, EBI-10196781;
CC Q8WUK0; Q9BYR8: KRTAP3-1; NbExp=3; IntAct=EBI-7199479, EBI-9996449;
CC Q8WUK0; Q9BQ66: KRTAP4-12; NbExp=3; IntAct=EBI-7199479, EBI-739863;
CC Q8WUK0; Q6L8G8: KRTAP5-7; NbExp=3; IntAct=EBI-7199479, EBI-11987425;
CC Q8WUK0; P26371: KRTAP5-9; NbExp=6; IntAct=EBI-7199479, EBI-3958099;
CC Q8WUK0; Q9BYQ4: KRTAP9-2; NbExp=6; IntAct=EBI-7199479, EBI-1044640;
CC Q8WUK0; Q9BYQ3: KRTAP9-3; NbExp=3; IntAct=EBI-7199479, EBI-1043191;
CC Q8WUK0; Q5TA81: LCE2C; NbExp=3; IntAct=EBI-7199479, EBI-11973993;
CC Q8WUK0; Q99750: MDFI; NbExp=7; IntAct=EBI-7199479, EBI-724076;
CC Q8WUK0; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-7199479, EBI-742948;
CC Q8WUK0; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-7199479, EBI-945833;
CC Q8WUK0; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-7199479, EBI-22310682;
CC Q8WUK0; O76081-6: RGS20; NbExp=6; IntAct=EBI-7199479, EBI-10178530;
CC Q8WUK0; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-7199479, EBI-747107;
CC Q8WUK0; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-7199479, EBI-8638294;
CC Q8WUK0; P14373: TRIM27; NbExp=3; IntAct=EBI-7199479, EBI-719493;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P0C089}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P0C089}; Matrix side
CC {ECO:0000250|UniProtKB:P0C089}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8WUK0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WUK0-2; Sequence=VSP_015009;
CC Name=3;
CC IsoId=Q8WUK0-3; Sequence=VSP_045030, VSP_045031;
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
CC -!- CAUTION: Was originally erroneously termed DUSP23. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH14048.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAK07545.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY333987; AAP94732.1; -; mRNA.
DR EMBL; AC090559; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104942; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014048; AAH14048.1; ALT_INIT; mRNA.
DR EMBL; BC020242; AAH20242.1; -; mRNA.
DR EMBL; BC073798; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AF277187; AAK07545.1; ALT_INIT; mRNA.
DR CCDS; CCDS41643.1; -. [Q8WUK0-1]
DR CCDS; CCDS44593.1; -. [Q8WUK0-3]
DR RefSeq; NP_001137456.1; NM_001143984.1. [Q8WUK0-3]
DR RefSeq; NP_783859.1; NM_175732.2. [Q8WUK0-1]
DR AlphaFoldDB; Q8WUK0; -.
DR SMR; Q8WUK0; -.
DR BioGRID; 125402; 182.
DR IntAct; Q8WUK0; 134.
DR MINT; Q8WUK0; -.
DR STRING; 9606.ENSP00000325958; -.
DR BindingDB; Q8WUK0; -.
DR ChEMBL; CHEMBL2052033; -.
DR DEPOD; PTPMT1; -.
DR GlyGen; Q8WUK0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8WUK0; -.
DR PhosphoSitePlus; Q8WUK0; -.
DR SwissPalm; Q8WUK0; -.
DR BioMuta; PTPMT1; -.
DR DMDM; 73621420; -.
DR EPD; Q8WUK0; -.
DR jPOST; Q8WUK0; -.
DR MassIVE; Q8WUK0; -.
DR MaxQB; Q8WUK0; -.
DR PaxDb; Q8WUK0; -.
DR PeptideAtlas; Q8WUK0; -.
DR PRIDE; Q8WUK0; -.
DR ProteomicsDB; 19078; -.
DR ProteomicsDB; 74692; -. [Q8WUK0-1]
DR ProteomicsDB; 74693; -. [Q8WUK0-2]
DR Antibodypedia; 6453; 176 antibodies from 28 providers.
DR DNASU; 114971; -.
DR Ensembl; ENST00000326656.12; ENSP00000325882.8; ENSG00000110536.14. [Q8WUK0-2]
DR Ensembl; ENST00000326674.10; ENSP00000325958.9; ENSG00000110536.14. [Q8WUK0-1]
DR Ensembl; ENST00000426530.2; ENSP00000410272.2; ENSG00000110536.14. [Q8WUK0-3]
DR Ensembl; ENST00000643547.1; ENSP00000494387.1; ENSG00000285206.2. [Q8WUK0-2]
DR Ensembl; ENST00000646905.1; ENSP00000495288.1; ENSG00000285206.2. [Q8WUK0-3]
DR Ensembl; ENST00000647378.2; ENSP00000496417.1; ENSG00000285206.2. [Q8WUK0-1]
DR GeneID; 114971; -.
DR KEGG; hsa:114971; -.
DR MANE-Select; ENST00000326674.10; ENSP00000325958.9; NM_175732.3; NP_783859.1.
DR UCSC; uc001nfs.5; human. [Q8WUK0-1]
DR CTD; 114971; -.
DR DisGeNET; 114971; -.
DR GeneCards; PTPMT1; -.
DR HGNC; HGNC:26965; PTPMT1.
DR HPA; ENSG00000110536; Low tissue specificity.
DR MIM; 609538; gene.
DR neXtProt; NX_Q8WUK0; -.
DR OpenTargets; ENSG00000110536; -.
DR PharmGKB; PA142671115; -.
DR VEuPathDB; HostDB:ENSG00000110536; -.
DR eggNOG; KOG1719; Eukaryota.
DR GeneTree; ENSGT00390000014065; -.
DR HOGENOM; CLU_047330_0_0_1; -.
DR InParanoid; Q8WUK0; -.
DR OMA; KISSRRW; -.
DR OrthoDB; 1386941at2759; -.
DR PhylomeDB; Q8WUK0; -.
DR TreeFam; TF319745; -.
DR BioCyc; MetaCyc:HS03319-MON; -.
DR PathwayCommons; Q8WUK0; -.
DR Reactome; R-HSA-1483148; Synthesis of PG.
DR SignaLink; Q8WUK0; -.
DR SIGNOR; Q8WUK0; -.
DR UniPathway; UPA00084; UER00504.
DR BioGRID-ORCS; 114971; 464 hits in 1097 CRISPR screens.
DR ChiTaRS; PTPMT1; human.
DR GenomeRNAi; 114971; -.
DR Pharos; Q8WUK0; Tchem.
DR PRO; PR:Q8WUK0; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q8WUK0; protein.
DR Bgee; ENSG00000110536; Expressed in left testis and 95 other tissues.
DR ExpressionAtlas; Q8WUK0; baseline and differential.
DR Genevisible; Q8WUK0; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
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; IBA:GO_Central.
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:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:2001242; P:regulation of intrinsic apoptotic signaling pathway; IGI:UniProtKB.
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 Alternative splicing; Hydrolase; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Protein phosphatase;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 28..201
FT /note="Phosphatidylglycerophosphatase and protein-tyrosine
FT phosphatase 1"
FT /id="PRO_0000025423"
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 VAR_SEQ 59..151
FT /note="LVQDENVRGVITMNEEYETRFLCNSSQEWKRLGVEQLRLSTVDMTGIPTLDN
FT LQKGVQFALKYQSLGQCVYVHCKAGRSRSATMVAAYLIQVH -> VSRAGEPGPLPRPR
FT RSVPVGPLGSPPSLLSHLFASAAGTGRERARGDHHERGVRDEVPVQLFTGAQMESRGGC
FT KSHRQDPVIHPHQAWPAGCS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045030"
FT VAR_SEQ 85..148
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4"
FT /id="VSP_015009"
FT VAR_SEQ 152..201
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045031"
FT MUTAGEN 132
FT /note="C->S: Probable loss of catalytic activity. Does not
FT affect interaction with STYXL1."
FT /evidence="ECO:0000269|PubMed:24709986"
SQ SEQUENCE 201 AA; 22844 MW; 88A4CC76EEFD0835 CRC64;
MAATALLEAG LARVLFYPTL LYTLFRGKVP GRAHRDWYHR IDPTVLLGAL PLRSLTRQLV
QDENVRGVIT MNEEYETRFL CNSSQEWKRL GVEQLRLSTV DMTGIPTLDN LQKGVQFALK
YQSLGQCVYV HCKAGRSRSA TMVAAYLIQV HKWSPEEAVR AIAKIRSYIH IRPGQLDVLK
EFHKQITARA TKDGTFVISK T
