PP2A2_PARTE
ID PP2A2_PARTE Reviewed; 315 AA.
AC A0CNL9;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Serine/threonine-protein phosphatase PP2A catalytic subunit 2;
DE Short=PPN 2;
DE EC=3.1.3.16;
GN Name=Ppn2; ORFNames=GSPATT00008828001;
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=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; CT868119; CAK72386.1; -; Genomic_DNA.
DR RefSeq; XP_001439783.1; XM_001439746.1.
DR AlphaFoldDB; A0CNL9; -.
DR SMR; A0CNL9; -.
DR STRING; 5888.CAK72386; -.
DR EnsemblProtists; CAK72386; CAK72386; GSPATT00008828001.
DR GeneID; 5025568; -.
DR KEGG; ptm:GSPATT00008828001; -.
DR eggNOG; KOG0371; Eukaryota.
DR HOGENOM; CLU_004962_8_1_1; -.
DR InParanoid; A0CNL9; -.
DR OMA; MECKALT; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; 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:0000082; P:G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; SSF56300; 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 2"
FT /id="PRO_0000307835"
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; 36176 MW; 5D2073F13028956E CRC64;
MASLNKLSSN EIGNIDRQIA KLRQGQILTE QEVKSLCIKA KEILQDEPNI IQVRAPLTIC
GDIHGQFHDL IELFQIGGNL PDTNYLFLGD YVDRGSQSVE TFSLMLSLKV RYKDRIVLLR
GNHENREINK IYGFYDECFR KYGNEIVWKQ FTEVFGYLPL SAIVEQQIFC AHGGLSPAME
SVDQIKQLNR VQDIPHEGLM CDLLWSDPEE TKNGWGISPR GAGWTWGCDI TEKFLHSNKL
KQIARAHQLV MEGIQKVHNQ KTITIFSAPN YCYRCGNQAC IVEVDEQLKM NQTQFEPAPR
ENEPHTTRRV PDYFL
