PTPM1_DROME
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 03-AUG-2022, entry version 148.
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; Q86BN8; -.
DR PRIDE; Q86BN8; -.
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 CTD; 114971; -.
DR FlyBase; FBgn0039111; PTPMT1.
DR VEuPathDB; VectorBase:FBgn0039111; -.
DR eggNOG; KOG1719; Eukaryota.
DR GeneTree; ENSGT00390000014065; -.
DR InParanoid; Q86BN8; -.
DR OMA; KISSRRW; -.
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 tissues.
DR ExpressionAtlas; Q86BN8; baseline and differential.
DR Genevisible; Q86BN8; DM.
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 GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
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 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
