ID   PP2A_HEVBR              Reviewed;         306 AA.
AC   Q9ZSE4;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Serine/threonine-protein phosphatase PP2A catalytic subunit;
DE            EC=3.1.3.16;
GN   Name=PP2A;
OS   Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Micrandreae;
OC   Hevea.
OX   NCBI_TaxID=3981;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Shin D.H., Han K.-H.;
RT   "Isolation of a cDNA encoding a type 2A serine/threonine protein
RT   phosphatase (PP2A) from Hevea brasiliensis.";
RL   (er) Plant Gene Register PGR99-011(1999).
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   -!- TISSUE SPECIFICITY: Expressed at the same level in latex as in leaves.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2A subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF107464; AAD09953.1; -; mRNA.
DR   AlphaFoldDB; Q9ZSE4; -.
DR   SMR; Q9ZSE4; -.
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.
FT   CHAIN           1..306
FT                   /note="Serine/threonine-protein phosphatase PP2A catalytic
FT                   subunit"
FT                   /id="PRO_0000058859"
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"
SQ   SEQUENCE   306 AA;  34969 MW;  EFBE7F9DF4EB4A61 CRC64;
     MPSHGDLDRQ IEHLMECKPL PEARGQTLCD QARAILVEEW NVQPVKCPVT VCGDIHGQFY
     DLIELFRIGG NAPDTNYLFM GDYVDRGYYS VETVTLLVAL KVRYRDRITI LRGNHESRQI
     TQVYGFYDEC LRKYGNANVW KYFTDLFDYL PLTALIESQI FCLHGGLSPS LDTLDNIRAL
     DRIQEVPHEG PMCDLLWSDP DDRCGWGISP RGAGYTFGQD IAAQFNHTNG LTLISRAHQL
     VMEGYNWCQE KNVVTVFSAP NYCYRCGIMA AILEIGENMA QNFLQFDPAP RQIEPDTTRK
     TPDYFL