PP2A_MEDSA
ID PP2A_MEDSA Reviewed; 313 AA.
AC Q06009;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Serine/threonine-protein phosphatase PP2A catalytic subunit;
DE EC=3.1.3.16;
GN Name=PP2A;
OS Medicago sativa (Alfalfa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3879;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8393512; DOI=10.1007/bf00276891;
RA Pirck M., Pay A., Heberle-Bors E., Hirt H.;
RT "Isolation and characterization of a phosphoprotein phosphatase type 2A
RT gene from alfalfa.";
RL Mol. Gen. Genet. 240:126-131(1993).
CC -!- FUNCTION: May play a role in cell cycle regulation.
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 -!- TISSUE SPECIFICITY: Predominantly expressed in stems, moderate in
CC roots, nodes, leaves and flower buds.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2A subfamily.
CC {ECO:0000305}.
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DR EMBL; X70399; CAA49849.1; -; mRNA.
DR PIR; S35502; S35502.
DR AlphaFoldDB; Q06009; -.
DR SMR; Q06009; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
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 Cell cycle; Hydrolase; Manganese; Metal-binding; Protein phosphatase.
FT CHAIN 1..313
FT /note="Serine/threonine-protein phosphatase PP2A catalytic
FT subunit"
FT /id="PRO_0000058860"
FT ACT_SITE 122
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 313 AA; 35711 MW; 08230261A0110431 CRC64;
MGANSMIADV THDLNEQISQ LMQCKPLSEQ QVKELCEKAK EILMDESNVQ PVKSPVTICG
DIHGQFHDLA ELFRIGGKCP DTNYLFMGDY VDRGYYSVET VTLLVALKVR YPQRITILRG
NHESRQITQV YGFYDECLRK YGSANVWKIF TDLFDFFPLT ALVESEIFCL HGGLSPSIET
LDNIRNFDRV QEVPHEGPMC DLLWSDPDDR CGWGISPRGA GYTFGQDISE QFNHTNSLKL
IARAHQLVMD GFNWAHEQKV VTIFSAPNYC YRCGNMASIL EVDDCKGHTF IQFEPAPRRG
EPDVTRRTPD YFL