ID PTPM1_DROME Reviewed; 200 AA. AC Q86BN8; Q8SZ90; Q9VCI6; DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 153. DE RecName: Full=Phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1; DE EC=3.1.3.27; DE AltName: Full=PTEN-like phosphatase {ECO:0000303|PubMed:15247229}; DE AltName: Full=PTEN-like protein; DE AltName: Full=Protein-tyrosine phosphatase mitochondrial 1-like protein; DE EC=3.1.3.16; DE EC=3.1.3.48; DE Flags: Precursor; GN Name=PTPMT1 {ECO:0000312|FlyBase:FBgn0039111}; GN Synonyms=Plip {ECO:0000303|PubMed:15247229}; GN ORFNames=CG10371 {ECO:0000312|FlyBase:FBgn0039111}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C., RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., RA Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING. RC STRAIN=Berkeley; RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic RT review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B). RC STRAIN=Berkeley; TISSUE=Embryo; RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., RA Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [4] RP LACK OF ACTIVITY TOWARD AKT, AND TISSUE SPECIFICITY. 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). CC -!- FUNCTION: Lipid phosphatase that may mediate dephosphorylation of CC mitochondrial proteins (By similarity). Protein phosphatase that may CC mediate dephosphorylation of mitochondrial proteins (By similarity). CC Does not dephosphorylate Akt. {ECO:0000250}. 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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33752; CC Evidence={ECO:0000305}; 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 -!- 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 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 -!- 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=2; CC Name=B; CC IsoId=Q86BN8-1; Sequence=Displayed; CC Name=A; CC IsoId=Q86BN8-2; Sequence=VSP_015010; CC -!- TISSUE SPECIFICITY: Highly enriched in testis. CC {ECO:0000269|PubMed:15247229}. CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- CC receptor class dual specificity subfamily. {ECO:0000305}. 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; AE014297; AAF56179.1; -; Genomic_DNA. DR EMBL; AE014297; AAN13956.2; -; Genomic_DNA. DR EMBL; AY071042; AAL48664.1; -; mRNA. DR RefSeq; NP_651180.3; NM_142923.3. [Q86BN8-1] DR RefSeq; NP_732901.1; NM_170090.2. [Q86BN8-2] DR AlphaFoldDB; Q86BN8; -. DR SMR; Q86BN8; -. DR BioGRID; 67745; 4. DR STRING; 7227.FBpp0083844; -. DR PaxDb; 7227-FBpp0083844; -. DR DNASU; 42807; -. DR EnsemblMetazoa; FBtr0084453; FBpp0083844; FBgn0039111. [Q86BN8-1] DR EnsemblMetazoa; FBtr0084454; FBpp0083845; FBgn0039111. [Q86BN8-2] DR GeneID; 42807; -. DR KEGG; dme:Dmel_CG10371; -. DR AGR; FB:FBgn0039111; -. DR CTD; 114971; -. DR FlyBase; FBgn0039111; PTPMT1. DR VEuPathDB; VectorBase:FBgn0039111; -. DR eggNOG; KOG1719; Eukaryota. DR GeneTree; ENSGT00390000014065; -. DR InParanoid; Q86BN8; -. DR OMA; NAHWRTV; -. DR OrthoDB; 1046951at2759; -. DR PhylomeDB; Q86BN8; -. DR UniPathway; UPA00084; UER00504. DR BioGRID-ORCS; 42807; 0 hits in 3 CRISPR screens. DR GenomeRNAi; 42807; -. DR PRO; PR:Q86BN8; -. DR Proteomes; UP000000803; Chromosome 3R. DR Bgee; FBgn0039111; Expressed in seminal fluid secreting gland and 32 other cell types or tissues. DR ExpressionAtlas; Q86BN8; baseline and differential. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; ISS:FlyBase. DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0008962; F:phosphatidylglycerophosphatase activity; IBA:GO_Central. DR GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; ISS:FlyBase. 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:0016311; P:dephosphorylation; ISS:FlyBase. DR GO; GO:0035002; P:liquid clearance, open tracheal system; IMP:FlyBase. DR GO; GO:0006655; P:phosphatidylglycerol biosynthetic process; IEA:UniProtKB-UniPathway. 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. DR Genevisible; Q86BN8; DM. PE 2: Evidence at transcript 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..28 FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN 29..200 FT /note="Phosphatidylglycerophosphatase and protein-tyrosine FT phosphatase 1" FT /id="PRO_0000025426" FT DOMAIN 31..197 FT /note="Tyrosine-protein phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" FT ACT_SITE 141 FT /note="Phosphocysteine intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" FT VAR_SEQ 1..6 FT /note="Missing (in isoform A)" FT /evidence="ECO:0000305" FT /id="VSP_015010" FT CONFLICT 186 FT /note="D -> G (in Ref. 3; AAL48664)" FT /evidence="ECO:0000305" SQ SEQUENCE 200 AA; 23156 MW; E7B4B6A69CB1CFCD CRC64; MEMSAAMFAR VSFYPTLLYN VLMEKASARN WYDRIDEHVI LGALPFRSQA NDLIEKENMK AVVSMNEDYE LTAFSNNTEK WRKLGIEFLQ LATTDIFESP NQEKLFRGVE FINKFLPLKQ RIGGLSSSYQ PENVGSVYVH CKAGRTRSAT LVGCYLMMKN GWTPDQAVDH MRKCRPHILL HTKQWDALRL FYTNNVETKS //