PPME1_YEAST
ID PPME1_YEAST Reviewed; 400 AA.
AC P38796; D3DL25;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Protein phosphatase methylesterase 1;
DE Short=PME-1;
DE EC=3.1.1.89;
DE AltName: Full=Yms2;
GN Name=PPE1; OrderedLocusNames=YHR075C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP PROTEIN SEQUENCE OF 36-44.
RC STRAIN=S288c / DC-5A;
RX PubMed=9151978; DOI=10.1111/j.1432-1033.1997.t01-2-00449.x;
RA Kitakawa M., Graack H.-R., Grohmann L., Goldschmidt-Reisin S., Herfurth E.,
RA Wittmann-Liebold B., Nishimura T., Isono K.;
RT "Identification and characterization of the genes for mitochondrial
RT ribosomal proteins of Saccharomyces cerevisiae.";
RL Eur. J. Biochem. 245:449-456(1997).
RN [4]
RP FUNCTION.
RX PubMed=11060018; DOI=10.1093/emboj/19.21.5672;
RA Wu J., Tolstykh T., Lee J., Boyd K., Stock J.B., Broach J.R.;
RT "Carboxyl methylation of the phosphoprotein phosphatase 2A catalytic
RT subunit promotes its functional association with regulatory subunits in
RT vivo.";
RL EMBO J. 19:5672-5681(2000).
RN [5]
RP FUNCTION.
RX PubMed=15022016; DOI=10.1007/s00294-004-0497-5;
RA Bogomolnaya L.M., Pathak R., Cham R., Guo J., Surovtseva Y.V., Jaeckel L.,
RA Polymenis M.;
RT "A new enrichment approach identifies genes that alter cell cycle
RT progression in Saccharomyces cerevisiae.";
RL Curr. Genet. 45:350-359(2004).
RN [6]
RP IDENTIFICATION AS A SERINE HYDROLASE, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=14645503; DOI=10.1074/mcp.m300082-mcp200;
RA Baxter S.M., Rosenblum J.S., Knutson S., Nelson M.R., Montimurro J.S.,
RA Di Gennaro J.A., Speir J.A., Burbaum J.J., Fetrow J.S.;
RT "Synergistic computational and experimental proteomics approaches for more
RT accurate detection of active serine hydrolases in yeast.";
RL Mol. Cell. Proteomics 3:209-225(2004).
RN [7]
RP FUNCTION, AND INTERACTION WITH PPG1; PPH21; PPH22; PPH3 AND SIT4.
RX PubMed=15447631; DOI=10.1042/bj20040887;
RA Van Hoof C., Martens E., Longin S., Jordens J., Stevens I., Janssens V.,
RA Goris J.;
RT "Specific interactions of PP2A and PP2A-like phosphatases with the yeast
RT PTPA homologues, Ypa1 and Ypa2.";
RL Biochem. J. 386:93-102(2005).
RN [8]
RP SHOWS THAT PPE1 IS NOT A CONSTITUENT OF THE MITOCHONDRIAL RIBOSOMAL SMALL
RP COMPLEX.
RX PubMed=28154081; DOI=10.1126/science.aal2415;
RA Desai N., Brown A., Amunts A., Ramakrishnan V.;
RT "The structure of the yeast mitochondrial ribosome.";
RL Science 355:528-531(2017).
CC -!- FUNCTION: Demethylates proteins that have been reversibly
CC carboxymethylated. Demethylates the phosphatase PP2A catalytic subunits
CC PPH21 and PPH22. Forms inactive complexes (PP2Ai) with phosphatase
CC PP2A-like catalytic subunits. Involved in the regulation of cell cycle
CC progression at START. {ECO:0000269|PubMed:11060018,
CC ECO:0000269|PubMed:15022016, ECO:0000269|PubMed:15447631}.
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: Interacts with and inactivates the phosphatase PP2A-like
CC catalytic subunits PPG1, PPH21, PPH22, PPH3 AND SIT4.
CC {ECO:0000269|PubMed:15447631}.
CC -!- INTERACTION:
CC P38796; P23594: PPH21; NbExp=5; IntAct=EBI-13775, EBI-12745;
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a mitochondrial ribosomal protein
CC (PubMed:9151978), but has not been identified in the structure of the
CC yeast mitoribosome (PubMed:28154081). {ECO:0000305|PubMed:28154081,
CC ECO:0000305|PubMed:9151978}.
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DR EMBL; U10556; AAB68892.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06769.1; -; Genomic_DNA.
DR PIR; S46814; S46814.
DR RefSeq; NP_011942.1; NM_001179205.1.
DR AlphaFoldDB; P38796; -.
DR SMR; P38796; -.
DR BioGRID; 36509; 176.
DR DIP; DIP-1943N; -.
DR IntAct; P38796; 4.
DR MINT; P38796; -.
DR STRING; 4932.YHR075C; -.
DR ESTHER; yeast-ppme1; PPase_methylesterase_euk.
DR MaxQB; P38796; -.
DR PaxDb; P38796; -.
DR PRIDE; P38796; -.
DR EnsemblFungi; YHR075C_mRNA; YHR075C; YHR075C.
DR GeneID; 856474; -.
DR KEGG; sce:YHR075C; -.
DR SGD; S000001117; PPE1.
DR VEuPathDB; FungiDB:YHR075C; -.
DR eggNOG; KOG2564; Eukaryota.
DR GeneTree; ENSGT00390000004396; -.
DR HOGENOM; CLU_024818_3_0_1; -.
DR InParanoid; P38796; -.
DR OMA; WHIRSRT; -.
DR BioCyc; YEAST:YHR075C-MON; -.
DR PRO; PR:P38796; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38796; protein.
DR GO; GO:0005763; C:mitochondrial small ribosomal subunit; IDA:SGD.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IMP:SGD.
DR GO; GO:0051723; F:protein methylesterase activity; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR GO; GO:1990577; P:C-terminal protein demethylation; IMP:SGD.
DR GO; GO:0032543; P:mitochondrial translation; IC:SGD.
DR GO; GO:0006482; P:protein demethylation; IBA:GO_Central.
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; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF022950; PPase_methylesterase_euk; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Reference proteome; Serine esterase.
FT CHAIN 1..400
FT /note="Protein phosphatase methylesterase 1"
FT /id="PRO_0000030588"
FT DOMAIN 114..365
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT REGION 32..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 205
FT /evidence="ECO:0000250"
FT ACT_SITE 233
FT /evidence="ECO:0000250"
FT ACT_SITE 359
FT /evidence="ECO:0000250"
FT CONFLICT 36
FT /note="G -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="L -> P (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="S -> K (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 400 AA; 44888 MW; AD00BEA4FB7795EE CRC64;
MSDDLRRKIA LSQFERAKNV LDATFQEAYE DDENDGDALG SLPSFNGQSN RNRKYTGKTG
STTDRISSKE KSSLPTWSDF FDNKELVSLP DRDLDVNTYY TLPTSLLSNT TSIPIFIFHH
GAGSSGLSFA NLAKELNTKL EGRCGCFAFD ARGHAETKFK KADAPICFDR DSFIKDFVSL
LNYWFKSKIS QEPLQKVSVI LIGHSLGGSI CTFAYPKLST ELQKKILGIT MLDIVEEAAI
MALNKVEHFL QNTPNVFESI NDAVDWHVQH ALSRLRSSAE IAIPALFAPL KSGKVVRITN
LKTFSPFWDT WFTDLSHSFV GLPVSKLLIL AGNENLDKEL IVGQMQGKYQ LVVFQDSGHF
IQEDSPIKTA ITLIDFWKRN DSRNVVIKTN WGQHKTVQNT
