PP2A2_ORYSI
ID PP2A2_ORYSI Reviewed; 307 AA.
AC A2XN40; Q75HI9; Q9XF94;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Serine/threonine-protein phosphatase PP2A-2 catalytic subunit;
DE EC=3.1.3.16;
GN Name=PP2A2; ORFNames=OsI_013483;
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 [GENOMIC DNA].
RC STRAIN=cv. IR36;
RA Yu R.M.K., Kong R.Y.C.;
RT "Molecular cloning and characterization of protein phosphatase 2A catalytic
RT subunit genes from Oryza sativa.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Guang-Lu-Ai No.4;
RX PubMed=17522955; DOI=10.1007/s11103-007-9174-7;
RA Liu X., Lu T., Yu S., Li Y., Huang Y., Huang T., Zhang L., Zhu J., Zhao Q.,
RA Fan D., Mu J., Shangguan Y., Feng Q., Guan J., Ying K., Zhang Y., Lin Z.,
RA Sun Z., Qian Q., Lu Y., Han B.;
RT "A collection of 10,096 indica rice full-length cDNAs reveals highly
RT expressed sequence divergence between Oryza sativa indica and japonica
RT subspecies.";
RL Plant Mol. Biol. 65:403-415(2007).
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 -!- SEQUENCE CAUTION:
CC Sequence=EAY92250.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF134552; AAD22116.1; -; Genomic_DNA.
DR EMBL; CM000128; EAY92250.1; ALT_FRAME; Genomic_DNA.
DR EMBL; CT832173; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; A2XN40; -.
DR SMR; A2XN40; -.
DR STRING; 39946.A2XN40; -.
DR PRIDE; A2XN40; -.
DR BRENDA; 3.1.3.16; 4460.
DR Proteomes; UP000007015; Chromosome 3.
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..307
FT /note="Serine/threonine-protein phosphatase PP2A-2
FT catalytic subunit"
FT /id="PRO_0000301656"
FT ACT_SITE 116
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 55
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 57
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CONFLICT 42..43
FT /note="NV -> SG (in Ref. 3; CT832173)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="N -> D (in Ref. 3; CT832173)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="D -> E (in Ref. 3; CT832173)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="L -> R (in Ref. 3; CT832173)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 307 AA; 35243 MW; ABD1A94EDDFAC2EE CRC64;
MSSPHGGLDD QIERLMQCKP LPEPEVRALC EKAKEILMEE SNVQPVKSPV TICGDIHGQF
HDLAELFRIG GKCPDTNYLF MGDYVDRGYY SVETVTLLVA LKVRYPQRIT ILRGNHESRQ
ITQVYGFYDE CLRKYGNANV WKTFTDLFDY FPLTALVESE IFCLHGGLSP SIETLDNIRN
FDRVQEVPHE GPMCDLLWSD PDDRCGWGIS PRGAGYTFGQ DISEQFNHTN NLRLIARAHQ
LVMEGFNWAH EQKVVTIFSA PNYCYRCGNM ASILEVDDCR EHTFIQFEPA PRRGEPDVTR
RTPDYFL
