ID   PPME1_PONAB             Reviewed;         386 AA.
AC   Q5R4F9;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Protein phosphatase methylesterase 1;
DE            Short=PME-1;
DE            EC=3.1.1.89;
GN   Name=PPME1; Synonyms=PME1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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   -!- 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}.
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DR   EMBL; CR861290; CAH93357.1; -; mRNA.
DR   RefSeq; NP_001126977.1; NM_001133505.1.
DR   AlphaFoldDB; Q5R4F9; -.
DR   SMR; Q5R4F9; -.
DR   STRING; 9601.ENSPPYP00000004196; -.
DR   ESTHER; ponab-ppme1; PPase_methylesterase_euk.
DR   GeneID; 100173996; -.
DR   KEGG; pon:100173996; -.
DR   CTD; 51400; -.
DR   eggNOG; KOG2564; Eukaryota.
DR   InParanoid; Q5R4F9; -.
DR   OrthoDB; 911863at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0051722; F:protein C-terminal methylesterase activity; ISS:UniProtKB.
DR   GO; GO:0051721; F:protein phosphatase 2A binding; ISS:UniProtKB.
DR   GO; GO:0006482; P:protein demethylation; ISS: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.
DR   PROSITE; PS00120; LIPASE_SER; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Methylation; Phosphoprotein; Reference proteome;
KW   Serine esterase.
FT   CHAIN           1..386
FT                   /note="Protein phosphatase methylesterase 1"
FT                   /id="PRO_0000090392"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          254..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"
FT   MOD_RES         42
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y570"
SQ   SEQUENCE   386 AA;  42257 MW;  D9203FEACA52B426 CRC64;
     MSALEKSMHL GRLPSRPPLP GSGGSQSGAK MRMGPGRKRD FSPVPWSQYF ESMEDVEVEN
     ETGKDTFRVY KSGSEGPVLL LLHGGGHSAL SWAVFTAAII SRVQCRIVAL DLRSHGETKV
     KNPEDLSAET MAKDVGNVVE AMYGDLPPPI MLIGHSMGGA IAVHTASSNL VPSLLGLCMI
     GVVEGTAMDA LNSMQNFLRG RPKTFKSLEN AIEWSVKSGQ IRNLESARVS MVGQVKQCEG
     ITSPEGSKSI VEGIIEEEEE DEEGSESISK RKKEDDMETK KDHPYTWRIE LAKTEKYWDG
     WFRGLSNLFL SCPIPKLLLL AGVDRLDKDL TIGQMQGKFQ MQVLPQCGHA VHEDAPDKVA
     EAVATFLIRH RFAEPIGGFQ CVFPGC