PP2A1_ORYSI
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 03-AUG-2022, entry version 83.
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}.
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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 PRIDE; A2YEB4; -.
DR EnsemblPlants; BGIOSGA023128-TA; BGIOSGA023128-PA; BGIOSGA023128.
DR Gramene; BGIOSGA023128-TA; BGIOSGA023128-PA; BGIOSGA023128.
DR HOGENOM; CLU_004962_8_1_1; -.
DR OMA; YSLECAT; -.
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 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 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
