PPME1_MOUSE
ID PPME1_MOUSE Reviewed; 386 AA.
AC Q8BVQ5; Q3U392; Q3UJX8; Q3UKE0; Q8K311; Q91YR8; Q9CSP7;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 5.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Protein phosphatase methylesterase 1;
DE Short=PME-1;
DE EC=3.1.1.89;
GN Name=Ppme1; Synonyms=Pme1;
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, and NOD; TISSUE=Dendritic cell, Embryo, and Placenta;
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=Mammary gland;
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 PARTIAL PROTEIN SEQUENCE, AND TISSUE SPECIFICITY.
RX PubMed=10318862; DOI=10.1074/jbc.274.20.14382;
RA Ogris E., Du X., Nelson K.C., Mak E.K., Yu X.X., Lane W.S., Pallas D.C.;
RT "A protein phosphatase methylesterase (PME-1) is one of several novel
RT proteins stably associating with two inactive mutants of protein
RT phosphatase 2A.";
RL J. Biol. Chem. 274:14382-14391(1999).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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 [5]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-16, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Demethylates proteins that have been reversibly
CC carboxymethylated. Demethylates PPP2CB (in vitro) and PPP2CA. Binding
CC to PPP2CA displaces the manganese ion and inactivates the enzyme (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[phosphatase 2A protein]-C-terminal L-leucine methyl ester +
CC H2O = [phosphatase 2A protein]-C-terminal L-leucine + H(+) +
CC methanol; Xref=Rhea:RHEA:48548, Rhea:RHEA-COMP:12134, Rhea:RHEA-
CC COMP:12135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790,
CC ChEBI:CHEBI:90516, ChEBI:CHEBI:90517; EC=3.1.1.89;
CC -!- SUBUNIT: Binds PPP2CA and PPP2CB. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in testis and brain.
CC {ECO:0000269|PubMed:10318862}.
CC -!- PTM: Phosphorylated by SIK1 following increases in intracellular
CC sodium, leading to dissociation from the protein phosphatase 2A (PP2A)
CC complex and subsequent dephosphorylation of sodium/potassium-
CC transporting ATPase ATP1A1. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE32896.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK012256; BAB28122.1; -; mRNA.
DR EMBL; AK146051; BAE26861.1; -; mRNA.
DR EMBL; AK146268; BAE27027.1; -; mRNA.
DR EMBL; AK154876; BAE32896.1; ALT_INIT; mRNA.
DR EMBL; BC014867; AAH14867.1; -; mRNA.
DR EMBL; BC029064; AAH29064.1; -; mRNA.
DR CCDS; CCDS40036.1; -.
DR RefSeq; NP_082568.1; NM_028292.2.
DR AlphaFoldDB; Q8BVQ5; -.
DR SMR; Q8BVQ5; -.
DR BioGRID; 215457; 27.
DR DIP; DIP-46211N; -.
DR IntAct; Q8BVQ5; 3.
DR MINT; Q8BVQ5; -.
DR STRING; 10090.ENSMUSP00000032963; -.
DR BindingDB; Q8BVQ5; -.
DR ChEMBL; CHEMBL2189138; -.
DR ESTHER; mouse-PPME1; PPase_methylesterase_euk.
DR iPTMnet; Q8BVQ5; -.
DR PhosphoSitePlus; Q8BVQ5; -.
DR SwissPalm; Q8BVQ5; -.
DR EPD; Q8BVQ5; -.
DR jPOST; Q8BVQ5; -.
DR MaxQB; Q8BVQ5; -.
DR PaxDb; Q8BVQ5; -.
DR PeptideAtlas; Q8BVQ5; -.
DR PRIDE; Q8BVQ5; -.
DR ProteomicsDB; 291719; -.
DR Antibodypedia; 3870; 338 antibodies from 32 providers.
DR DNASU; 72590; -.
DR Ensembl; ENSMUST00000032963; ENSMUSP00000032963; ENSMUSG00000030718.
DR GeneID; 72590; -.
DR KEGG; mmu:72590; -.
DR UCSC; uc009imu.1; mouse.
DR CTD; 51400; -.
DR MGI; MGI:1919840; Ppme1.
DR VEuPathDB; HostDB:ENSMUSG00000030718; -.
DR eggNOG; KOG2564; Eukaryota.
DR GeneTree; ENSGT00390000004396; -.
DR HOGENOM; CLU_024818_0_1_1; -.
DR InParanoid; Q8BVQ5; -.
DR OMA; WHIRSRT; -.
DR OrthoDB; 911863at2759; -.
DR PhylomeDB; Q8BVQ5; -.
DR TreeFam; TF314697; -.
DR BRENDA; 3.1.1.89; 3474.
DR Reactome; R-MMU-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR BioGRID-ORCS; 72590; 11 hits in 76 CRISPR screens.
DR ChiTaRS; Ppme1; mouse.
DR PRO; PR:Q8BVQ5; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BVQ5; protein.
DR Bgee; ENSMUSG00000030718; Expressed in primary motor cortex and 275 other tissues.
DR ExpressionAtlas; Q8BVQ5; baseline and differential.
DR Genevisible; Q8BVQ5; MM.
DR GO; GO:0106222; F:lncRNA binding; IDA:MGI.
DR GO; GO:0051722; F:protein C-terminal methylesterase activity; ISS:HGNC-UCL.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0051723; F:protein methylesterase activity; IBA:GO_Central.
DR GO; GO:0051721; F:protein phosphatase 2A binding; ISS:HGNC-UCL.
DR GO; GO:0019903; F:protein phosphatase binding; ISS:HGNC-UCL.
DR GO; GO:0006482; P:protein demethylation; ISS:HGNC-UCL.
DR GO; GO:0006468; P:protein phosphorylation; IMP:MGI.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR000639; Epox_hydrolase-like.
DR InterPro; IPR016812; PPase_methylesterase_euk.
DR PANTHER; PTHR14189; PTHR14189; 1.
DR Pfam; PF12697; Abhydrolase_6; 1.
DR PIRSF; PIRSF022950; PPase_methylesterase_euk; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR PRINTS; PR00412; EPOXHYDRLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Methylation; Phosphoprotein;
KW Reference proteome; Serine esterase.
FT CHAIN 1..386
FT /note="Protein phosphatase methylesterase 1"
FT /id="PRO_0000090391"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 156
FT /evidence="ECO:0000250"
FT ACT_SITE 181
FT /evidence="ECO:0000250"
FT ACT_SITE 349
FT /evidence="ECO:0000250"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y570"
FT MOD_RES 16
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 16
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y570"
FT CONFLICT 17
FT /note="P -> T (in Ref. 1; BAE27027)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="G -> D (in Ref. 2; AAH29064)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="H -> R (in Ref. 1; BAE27027)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 386 AA; 42256 MW; 2BD07B588299DB6D CRC64;
MSALEKSMHL GRLPSRPPLP GSGGSQSGAK MRMGPGRKRD FTPVPWSQYF ESMEDVEVEN
ETGKDTFRVY KSGSEGPVLL LLHGGGHSAL SWAVFTAAII SRVQCRIVAL DLRGHGETKV
KNSEDLSAET MAKDVGNVVE AMYGDLPPPV MLIGHSMGGA IAVHTAAANL VPSLLGLCMI
DVVEGTAMDA LNSMQNFLRG RPKTFKSLEN AIEWSVKSGQ IRNLESARVS MVGQVKQCEG
ITSPEGSKSI VEGIIEEEEE DEEGSESVNK RKKEDDMETK KDHPYTWRIE LAKTEKYWDG
WFRGLSNLFL SCPIPKLLLL AGVDRLDKDL TIGQMQGKFQ MQVLPQCGHA VHEDAPDKVA
EAVATFLIRH RFAEPIGGFQ CVFPGC
