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   27-MAR-2024, entry version 85.
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   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   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:SF12; SERINE_THREONINE-PROTEIN PHOSPHATASE PP2A; 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..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
//