ID PP2A1_ORYSI Reviewed; 306 AA. AC A2YEB4; Q42981; Q5Z7K2; Q9ZSS3; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 20-MAR-2007, sequence version 1. DT 27-MAR-2024, entry version 88. DE RecName: Full=Serine/threonine-protein phosphatase PP2A-1 catalytic subunit; DE EC=3.1.3.16; GN Name=PP2A1; ORFNames=OsI_022657; OS Oryza sativa subsp. indica (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade; OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa. OX NCBI_TaxID=39946; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. IR36; TISSUE=Seed; RX PubMed=10080713; DOI=10.1023/a:1006152223183; RA Chang M., Wang B., Chen X., Wu R.; RT "Molecular characterization of catalytic-subunit cDNA sequences encoding RT protein phosphatases 1 and 2A and study of their roles in the gibberellin- RT dependent Osamy-c expression in rice."; RL Plant Mol. Biol. 39:105-115(1999). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. IR36; RX PubMed=12602862; DOI=10.1023/a:1022006023273; RA Yu R.M.K., Zhou Y., Xu Z.-F., Chye M.-L., Kong R.Y.; RT "Two genes encoding protein phosphatase 2A catalytic subunits are RT differentially expressed in rice."; RL Plant Mol. Biol. 51:295-311(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. 93-11; RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038; RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L., RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J., RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X., RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y., RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L., RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H., RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z., RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L., RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.; RT "The genomes of Oryza sativa: a history of duplications."; RL PLoS Biol. 3:266-281(2005). 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2A subfamily. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U49113; AAA91806.1; -; mRNA. DR EMBL; AF097182; AAC72838.1; -; Genomic_DNA. DR EMBL; CM000131; EAZ01425.1; -; Genomic_DNA. DR PIR; T03389; T03389. DR AlphaFoldDB; A2YEB4; -. DR SMR; A2YEB4; -. DR STRING; 39946.A2YEB4; -. DR EnsemblPlants; BGIOSGA023128-TA; BGIOSGA023128-PA; BGIOSGA023128. DR Gramene; BGIOSGA023128-TA; BGIOSGA023128-PA; BGIOSGA023128. DR HOGENOM; CLU_004962_8_1_1; -. DR OMA; MDDKTFT; -. DR Proteomes; UP000007015; Chromosome 6. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC. 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:SF69; SERINE_THREONINE-PROTEIN PHOSPHATASE PP2A-1 CATALYTIC SUBUNIT; 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 2: Evidence at transcript level; KW Cytoplasm; Hydrolase; Manganese; Metal-binding; Protein phosphatase; KW Reference proteome. FT CHAIN 1..306 FT /note="Serine/threonine-protein phosphatase PP2A-1 FT catalytic subunit" FT /id="PRO_0000301655" FT ACT_SITE 115 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 54 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 56 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 82 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 82 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 114 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 164 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 238 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT CONFLICT 47 FT /note="C -> S (in Ref. 1; AAA91806)" FT /evidence="ECO:0000305" FT CONFLICT 69 FT /note="G -> A (in Ref. 2; AAC72838)" FT /evidence="ECO:0000305" FT CONFLICT 106 FT /note="D -> E (in Ref. 1; AAA91806)" FT /evidence="ECO:0000305" FT CONFLICT 144 FT /note="T -> A (in Ref. 1; AAA91806)" FT /evidence="ECO:0000305" FT CONFLICT 217 FT /note="F -> N (in Ref. 1; AAA91806)" FT /evidence="ECO:0000305" FT CONFLICT 294 FT /note="E -> D (in Ref. 1; AAA91806)" FT /evidence="ECO:0000305" SQ SEQUENCE 306 AA; 35114 MW; F95722F8A638FF31 CRC64; MPSHADLDRQ ISQLRECKFL GEAEVRALCE QAKAILMEEW NVQPVRCPVT VCGDIHGQFY DLIELFRIGG DSPDTNYLFM GDYVDRGYYS VETVTLLVAL KVRYRDRITI LRGNHESRQI TQVYGFYDEC LRKYGNANVW KYFTDLFDYL PLTALVENQV FCLHGGLSPS LDTLDNIRAL DRIQEVPHEG PMCDLLWSDP DDRCGWGISP RGAGYTFGQD IAQQFNHTNG LTLISRAHQL VMEGFNWCQD KNVVTVFSAP NYCYRCGNMA AILEIGENMD QNFLQFDPAP RQIEPDTTRK TPDYFL //