PTPM1_MOUSE
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 03-AUG-2022, entry version 131.
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 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 SwissLipids; SLP:000000643; -.
DR iPTMnet; Q66GT5; -.
DR PhosphoSitePlus; Q66GT5; -.
DR EPD; Q66GT5; -.
DR MaxQB; Q66GT5; -.
DR PaxDb; Q66GT5; -.
DR PeptideAtlas; Q66GT5; -.
DR PRIDE; Q66GT5; -.
DR ProteomicsDB; 302012; -.
DR Antibodypedia; 6453; 176 antibodies from 28 providers.
DR DNASU; 66461; -.
DR Ensembl; ENSMUST00000111461; ENSMUSP00000159390; ENSMUSG00000063235.
DR GeneID; 66461; -.
DR KEGG; mmu:66461; -.
DR CTD; 114971; -.
DR MGI; MGI:1913711; Ptpmt1.
DR GeneTree; ENSGT00390000014065; -.
DR InParanoid; Q66GT5; -.
DR OMA; KISSRRW; -.
DR OrthoDB; 1386941at2759; -.
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 70 other tissues.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; ISO:MGI.
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: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:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:2001242; P:regulation of intrinsic apoptotic signaling pathway; ISO:MGI.
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 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
