ID   PP2A5_TOBAC             Reviewed;         314 AA.
AC   O04860;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=Serine/threonine-protein phosphatase PP2A-5 catalytic subunit;
DE            EC=3.1.3.16;
GN   Name=NPP5;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Xanthi;
RX   PubMed=9484443; DOI=10.1023/a:1005943805988;
RA   Suh M., Cho H., Kim Y., Liu J., Lee H.;
RT   "Multiple genes encoding serine/threonine protein phosphatases and their
RT   differential expression in Nicotiana tabacum.";
RL   Plant Mol. Biol. 36:315-322(1998).
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; Z93772; CAB07807.1; -; mRNA.
DR   PIR; T03600; T03600.
DR   RefSeq; NP_001312240.1; NM_001325311.1.
DR   AlphaFoldDB; O04860; -.
DR   SMR; O04860; -.
DR   STRING; 4097.O04860; -.
DR   PaxDb; 4097-O04860; -.
DR   GeneID; 107781246; -.
DR   KEGG; nta:107781246; -.
DR   OrthoDB; 19833at2759; -.
DR   Proteomes; UP000084051; Unplaced.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR   GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
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:SF17; SERINE_THREONINE-PROTEIN PHOSPHATASE PP2A-5 CATALYTIC SUBUNIT; 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..314
FT                   /note="Serine/threonine-protein phosphatase PP2A-5
FT                   catalytic subunit"
FT                   /id="PRO_0000058866"
FT   ACT_SITE        123
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         62
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         64
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         90
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         90
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         122
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         172
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         246
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   314 AA;  35640 MW;  77F8348771E078C3 CRC64;
     MSSSDLVAAS IQGNLDEQIS QLMQCKPLSE PDVRALCEKA KEILAEESNV QPVKSPVTIC
     GDIHGQFHDL AELFRIGGQC PDTNYLFMGD YVDRGYYSVE TVTLLVALKV RYPQRLTILR
     GNHESRQITQ VYGFYDECLR KYGNANVWKT FTDLFDYFPL TALVESEIFC LHGGLSPSIE
     TLDNVRSFDR VQEVPHEGAM CDLLWSDPDD CCGWGMSPRG AGYTFGQDIS EQFHQTNNLK
     LIARAHQLVM EGYNWSHEQK VVTIFSAPNY CYRCGNMASI LEVDDCRGHT FIQFDPAPRR
     GEPDVTRRTP DYFL
//