ID   PP2A3_PARTE             Reviewed;         315 AA.
AC   Q6BFF6;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   RecName: Full=Serine/threonine-protein phosphatase PP2A catalytic subunit 3;
DE            Short=PPN 3;
DE            EC=3.1.3.16;
GN   Name=Ppn3; ORFNames=GSPATT00000061001, PTMB.417c;
OS   Paramecium tetraurelia.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX   NCBI_TaxID=5888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Stock d4-2;
RX   PubMed=15296759; DOI=10.1016/j.cub.2004.07.029;
RA   Zagulski M., Nowak J.K., Le Mouel A., Nowacki M., Migdalski A.,
RA   Gromadka R., Noel B., Blanc I., Dessen P., Wincker P., Keller A.-M.,
RA   Cohen J., Meyer E., Sperling L.;
RT   "High coding density on the largest Paramecium tetraurelia somatic
RT   chromosome.";
RL   Curr. Biol. 14:1397-1404(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Stock d4-2;
RX   PubMed=17086204; DOI=10.1038/nature05230;
RA   Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA   Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA   Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA   Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA   Le Mouel A., Lepere G., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA   Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA   Weissenbach J., Scarpelli C., Schaechter V., Sperling L., Meyer E.,
RA   Cohen J., Wincker P.;
RT   "Global trends of whole-genome duplications revealed by the ciliate
RT   Paramecium tetraurelia.";
RL   Nature 444:171-178(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC   -!- PTM: Reversibly methyl esterified on Leu-315 by leucine carboxyl
CC       methyltransferase 1 (PPM1) and protein phosphatase methylesterase 1
CC       (PPE1). Carboxyl methylation influences the affinity of the catalytic
CC       subunit for the different regulatory subunits, thereby modulating the
CC       PP2A holoenzyme's substrate specificity, enzyme activity and cellular
CC       localization.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2A subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CR548612; CAH03615.1; -; Genomic_DNA.
DR   EMBL; CT867985; CAK55626.1; -; Genomic_DNA.
DR   RefSeq; XP_001347241.1; XM_001347205.1.
DR   RefSeq; XP_001423024.1; XM_001422987.1.
DR   AlphaFoldDB; Q6BFF6; -.
DR   SMR; Q6BFF6; -.
DR   STRING; 5888.Q6BFF6; -.
DR   EnsemblProtists; CAK55626; CAK55626; GSPATT00000061001.
DR   GeneID; 5008828; -.
DR   GeneID; 79574108; -.
DR   KEGG; ptm:GSPATT00000061001; -.
DR   KEGG; ptm:PTMB.417c; -.
DR   eggNOG; KOG0371; Eukaryota.
DR   HOGENOM; CLU_004962_8_1_1; -.
DR   InParanoid; Q6BFF6; -.
DR   OMA; RYPERIF; -.
DR   Proteomes; UP000000600; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR   GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR   CDD; cd07415; MPP_PP2A_PP4_PP6; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR047129; PPA2-like.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   PANTHER; PTHR45619; SERINE/THREONINE-PROTEIN PHOSPHATASE PP2A-RELATED; 1.
DR   PANTHER; PTHR45619:SF12; SERINE_THREONINE-PROTEIN PHOSPHATASE PP2A; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Manganese; Metal-binding; Methylation; Protein phosphatase;
KW   Reference proteome.
FT   CHAIN           1..315
FT                   /note="Serine/threonine-protein phosphatase PP2A catalytic
FT                   subunit 3"
FT                   /id="PRO_0000307836"
FT   REGION          294..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        123
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         62
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         64
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         90
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         90
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         122
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         172
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         247
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         315
FT                   /note="Leucine methyl ester"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   315 AA;  36080 MW;  19AD3EAF9F1E392D CRC64;
     MASLNKLSSN DIGNIDRQIA KLKQGQILTE SEIKSLCIKA KEILSDEPNI IQVRAPLTIC
     GDIHGQFHDL IELFQIGGNL PDTNYLFLGD YVDRGSQSVE TFSLMLSLKV RYKDRIVLLR
     GNHENREINK VYGFYDECFR KYGNEIVWKQ FTEVFGYLPL SAIVEQQIFC AHGGLSPAME
     SVDQIKQLNR VQDIPHEGLM CDLLWSDPEE TKNGWGISPR GAGWTWGCDI TEKFLHSNKL
     KQIARAHQLV MEGIQKVHNQ KTITIFSAPN YCYRCGNQAC IVEVDEQLRM NQTQFEPAPR
     ENEPHTTRRV PDYFL
//