Q6BFF6 PP2A3_PARTE Serine/threonine-protein phosphatase PP2A catalytic subunit 3 PPN 3 3.1.3.16 Ppn3 GSPATT00000061001 PTMB.417c Paramecium tetraurelia Eukaryota Sar Alveolata Ciliophora Intramacronucleata Oligohymenophorea Peniculida Parameciidae Paramecium NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] Stock d4-2 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] Stock d4-2 O-phospho-L-seryl-[protein] + H2O = L-seryl-[protein] + phosphate O-phospho-L-threonyl-[protein] + H2O = L-threonyl-[protein] + phosphate Mn(2+) Binds 2 manganese ions per subunit. Reversibly methyl esterified on Leu-315 by leucine carboxyl methyltransferase 1 (PPM1) and protein phosphatase methylesterase 1 (PPE1). Carboxyl methylation influences the affinity of the catalytic subunit for the different regulatory subunits, thereby modulating the PP2A holoenzyme's substrate specificity, enzyme activity and cellular localization. Belongs to the PPP phosphatase family. PP-2A subfamily. Hydrolase Manganese Metal-binding Methylation Protein phosphatase Reference proteome Mn(2+) 1 Mn(2+) 1 Mn(2+) 1 Mn(2+) 2 Mn(2+) 2 Mn(2+) 2 Mn(2+) 2 MASLNKLSSNDIGNIDRQIAKLKQGQILTESEIKSLCIKAKEILSDEPNIIQVRAPLTICGDIHGQFHDLIELFQIGGNLPDTNYLFLGDYVDRGSQSVETFSLMLSLKVRYKDRIVLLRGNHENREINKVYGFYDECFRKYGNEIVWKQFTEVFGYLPLSAIVEQQIFCAHGGLSPAMESVDQIKQLNRVQDIPHEGLMCDLLWSDPEETKNGWGISPRGAGWTWGCDITEKFLHSNKLKQIARAHQLVMEGIQKVHNQKTITIFSAPNYCYRCGNQACIVEVDEQLRMNQTQFEPAPRENEPHTTRRVPDYFL Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms Distributed under the Creative Commons Attribution (CC BY 4.0) License