PPME1_RAT
ID PPME1_RAT Reviewed; 386 AA.
AC Q4FZT2;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 2.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Protein phosphatase methylesterase 1;
DE Short=PME-1;
DE EC=3.1.1.89;
GN Name=Ppme1; Synonyms=Pme1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 290-386.
RC TISSUE=Thymus;
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 PHOSPHORYLATION BY SIK1, AND FUNCTION.
RX PubMed=17939993; DOI=10.1073/pnas.0706838104;
RA Sjostrom M., Stenstrom K., Eneling K., Zwiller J., Katz A.I., Takemori H.,
RA Bertorello A.M.;
RT "SIK1 is part of a cell sodium-sensing network that regulates active sodium
RT transport through a calcium-dependent process.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:16922-16927(2007).
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, ECO:0000269|PubMed:17939993}.
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 -!- 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:0000269|PubMed:17939993}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR EMBL; BC099160; AAH99160.1; -; mRNA.
DR RefSeq; NP_001178767.1; NM_001191838.1.
DR AlphaFoldDB; Q4FZT2; -.
DR SMR; Q4FZT2; -.
DR STRING; 10116.ENSRNOP00000023649; -.
DR iPTMnet; Q4FZT2; -.
DR PhosphoSitePlus; Q4FZT2; -.
DR jPOST; Q4FZT2; -.
DR PaxDb; Q4FZT2; -.
DR PRIDE; Q4FZT2; -.
DR Ensembl; ENSRNOT00000023648; ENSRNOP00000023649; ENSRNOG00000017227.
DR GeneID; 361613; -.
DR KEGG; rno:361613; -.
DR UCSC; RGD:1309683; rat.
DR CTD; 51400; -.
DR RGD; 1309683; Ppme1.
DR eggNOG; KOG2564; Eukaryota.
DR GeneTree; ENSGT00390000004396; -.
DR HOGENOM; CLU_024818_0_1_1; -.
DR InParanoid; Q4FZT2; -.
DR OMA; WHIRSRT; -.
DR OrthoDB; 911863at2759; -.
DR TreeFam; TF314697; -.
DR Reactome; R-RNO-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR PRO; PR:Q4FZT2; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000017227; Expressed in frontal cortex and 20 other tissues.
DR Genevisible; Q4FZT2; RN.
DR GO; GO:0106222; F:lncRNA binding; ISO:RGD.
DR GO; GO:0051722; F:protein C-terminal methylesterase activity; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0051723; F:protein methylesterase activity; IBA:GO_Central.
DR GO; GO:0051721; F:protein phosphatase 2A binding; ISO:RGD.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:RGD.
DR GO; GO:0019888; F:protein phosphatase regulator activity; TAS:UniProtKB.
DR GO; GO:0006482; P:protein demethylation; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR GO; GO:0002028; P:regulation of sodium ion transport; TAS:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
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 SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Methylation; Phosphoprotein; Reference proteome;
KW Serine esterase.
FT CHAIN 1..386
FT /note="Protein phosphatase methylesterase 1"
FT /id="PRO_0000413635"
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 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:0000250|UniProtKB:Q8BVQ5"
FT MOD_RES 16
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y570"
SQ SEQUENCE 386 AA; 42316 MW; 2D176042469C9E29 CRC64;
MSALEKSMHL GRLPSRPPLP GSGGSQSGAK MRMGPGRKRD FTPVPWSQYF ESMEDVEVEN
ETGKDTFRVY KSGSEGPVLL LLHGGGHSAL SWAVFTAAII SRVQCRIVAL DLRSHGETKV
KNSEDLSAET MAKDVGNVVE AMYGDLPPPV MLIGHSMGGA IAVHTAAANL VPSLLGLCMI
DVVEGTAMDA LNSMQNFLRG RPKTFKSLEN AIEWSVKSGQ IRNLESARVS MVGQVKQCEG
ITSPESSKSI VEGIIEEEEE DEEGSESVNK RKKEDDMETK KDHPYTWRIE LAKTEKYWDG
WFRGLSNLFL SCPIPKLLLL AGVDRLDKDL TIGQMQGKFQ MQVLPQCGHA VHEDAPDKVA
EAVATFLIRH RFAEPIGGFQ CVFPGC
