ID G1PJY0_MYOLU Unreviewed; 389 AA.
AC G1PJY0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Protein phosphatase methylesterase 1 {ECO:0000256|PIRNR:PIRNR022950};
DE Short=PME-1 {ECO:0000256|PIRNR:PIRNR022950};
DE EC=3.1.1.- {ECO:0000256|PIRNR:PIRNR022950};
GN Name=PPME1 {ECO:0000313|Ensembl:ENSMLUP00000011073.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000011073.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000011073.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000011073.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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.
CC {ECO:0000256|ARBA:ARBA00024698}.
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 Evidence={ECO:0000256|ARBA:ARBA00000906};
CC -!- SUBUNIT: Binds PPP2CA and PPP2CB. {ECO:0000256|ARBA:ARBA00011604}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily.
CC {ECO:0000256|ARBA:ARBA00008645, ECO:0000256|PIRNR:PIRNR022950}.
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DR EMBL; AAPE02040805; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02040806; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02040807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02040808; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02040809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1PJY0; -.
DR STRING; 59463.ENSMLUP00000011073; -.
DR Ensembl; ENSMLUT00000012154.2; ENSMLUP00000011073.2; ENSMLUG00000012151.2.
DR eggNOG; KOG2564; Eukaryota.
DR GeneTree; ENSGT00390000004396; -.
DR HOGENOM; CLU_024818_0_1_1; -.
DR InParanoid; G1PJY0; -.
DR OMA; EAHHTSM; -.
DR TreeFam; TF314697; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0106222; F:lncRNA binding; IEA:Ensembl.
DR GO; GO:0051722; F:protein C-terminal methylesterase activity; IEA:Ensembl.
DR GO; GO:0051721; F:protein phosphatase 2A binding; IEA:Ensembl.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 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:SF0; PROTEIN PHOSPHATASE METHYLESTERASE 1; 1.
DR PANTHER; PTHR14189; PROTEIN PHOSPHATASE METHYLESTERASE-1 RELATED; 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; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PIRNR:PIRNR022950};
KW Reference proteome {ECO:0000313|Proteomes:UP000001074};
KW Serine esterase {ECO:0000256|PIRNR:PIRNR022950}.
FT DOMAIN 79..365
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF12697"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 156
FT /evidence="ECO:0000256|PIRSR:PIRSR022950-1"
FT ACT_SITE 181
FT /evidence="ECO:0000256|PIRSR:PIRSR022950-1"
FT ACT_SITE 352
FT /evidence="ECO:0000256|PIRSR:PIRSR022950-1"
SQ SEQUENCE 389 AA; 42563 MW; 52320597AB545CAB CRC64;
MSALEKSMHL GRLPSRPPLP GNGGNQSGAK MRMGPGRKRD FSPVSWSQYF ESMEDVEVEN
ETGKDSFRVY KSGSEGPVLL LLHGGGHSAL SWAVFTAAII SRVQCRIVAL DLRGHGETKV
KNSEDLSAET MAKDVGNVIE AMYGDLPPPI MLIGHSMGGA IAVHTASSNL VPSLLGLCVI
DVVEGTAMDA LNSMQNFLRG RPKTFKSLEN AIEWSVKSGQ IRNLESARVS MVGQVKEKPR
CEGITSPEGS KSVVEGIIEE DEDDEEGSES VNKRKKEDDT ETKKDHPYTW RIELAKTEKY
WDGWFRGLSN LFLSCPIPKL LLLAGVDRLD KDLTIGQMQG KFQMQVLPQC GHAVHEDAPD
KVAEAVATFL IRNRFAESVG GFQCVFPGC
//
