ID PP2A5_ARATH Reviewed; 307 AA. AC O04951; Q1EC63; Q42544; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 27-MAR-2024, entry version 164. DE RecName: Full=Serine/threonine-protein phosphatase PP2A-5 catalytic subunit; DE EC=3.1.3.16; DE AltName: Full=Protein phosphatase 2A isoform 5; GN Name=PP2A5 {ECO:0000303|PubMed:17368080}; OrderedLocusNames=At1g69960; GN ORFNames=F20P5.30, T17F3.1; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Columbia; RA Stamey R.T., Rundle S.J.; RT "Characterization of a novel isoform of a type 2A serine/threonine protein RT phosphatase from Arabidopsis thaliana."; RL (er) Plant Gene Register PGR95-116(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=11130712; DOI=10.1038/35048500; RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L., RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., RA Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."; RL Nature 408:816-820(2000). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RX PubMed=27862469; DOI=10.1111/tpj.13415; RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S., RA Town C.D.; RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference RT genome."; RL Plant J. 89:789-804(2017). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.; RT "Arabidopsis ORF clones."; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K., RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., RA Shinozaki K.; RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. RN [6] RP INTERACTION WITH PP2AA1. RX PubMed=10091592; DOI=10.1046/j.1432-1327.1999.00154.x; RA Haynes J.G., Hartung A.J., Hendershot J.D. III, Passingham R.S., RA Rundle S.J.; RT "Molecular characterization of the B' regulatory subunit gene family of RT Arabidopsis protein phosphatase 2A."; RL Eur. J. Biochem. 260:127-136(1999). RN [7] RP INTERACTION WITH CHIP. RX PubMed=16640601; DOI=10.1111/j.1365-313x.2006.02730.x; RA Luo J., Shen G., Yan J., He C., Zhang H.; RT "AtCHIP functions as an E3 ubiquitin ligase of protein phosphatase 2A RT subunits and alters plant response to abscisic acid treatment."; RL Plant J. 46:649-657(2006). RN [8] RP GENE FAMILY, AND NOMENCLATURE. RX PubMed=17368080; DOI=10.1016/j.tplants.2007.03.003; RA Farkas I., Dombradi V., Miskei M., Szabados L., Koncz C.; RT "Arabidopsis PPP family of serine/threonine phosphatases."; RL Trends Plant Sci. 12:169-176(2007). RN [9] RP INTERACTION WITH TAF12B. RC STRAIN=cv. Wassilewskija; RX PubMed=17526916; DOI=10.1093/jxb/erm080; RA Robles L.M., Wampole J.S., Christians M.J., Larsen P.B.; RT "Arabidopsis enhanced ethylene response 4 encodes an EIN3-interacting TFIID RT transcription factor required for proper ethylene response, including ERF1 RT induction."; RL J. Exp. Bot. 58:2627-2639(2007). RN [10] RP FUNCTION, INTERACTION WITH B'THETA, AND SUBCELLULAR LOCATION. RX PubMed=25489022; DOI=10.1104/pp.114.254409; RA Kataya A.R., Heidari B., Hagen L., Kommedal R., Slupphaug G., Lillo C.; RT "Protein phosphatase 2A holoenzyme is targeted to peroxisomes by RT piggybacking and positively affects peroxisomal beta-oxidation."; RL Plant Physiol. 167:493-506(2015). RN [11] RP FUNCTION, INTERACTION WITH CLC-A; CLC-B; CLC-C AND CLC-G, INDUCTION BY SALT RP STRESS, AND DISRUPTION PHENOTYPE. RX PubMed=27676158; DOI=10.1111/pce.12837; RA Hu R., Zhu Y., Wei J., Chen J., Shi H., Shen G., Zhang H.; RT "Overexpression of PP2A-C5 that encodes the catalytic subunit 5 of protein RT phosphatase 2A in Arabidopsis confers better root and shoot development RT under salt conditions."; RL Plant Cell Environ. 40:150-164(2017). RN [12] RP METHYLATION AT LEU-307. RX PubMed=28741704; DOI=10.1111/pce.13038; RA Creighton M.T., Kolton A., Kataya A.R.A., Maple-Groedem J., Averkina I.O., RA Heidari B., Lillo C.; RT "Methylation of protein phosphatase 2A-influence of regulators and RT environmental stress factors."; RL Plant Cell Environ. 40:2347-2358(2017). CC -!- FUNCTION: Associates with the serine/threonine-protein phosphatase PP2A CC regulatory subunits A and B' to positively regulates beta-oxidation of CC fatty acids and protoauxins in peroxisomes by dephosphorylating CC peroxisomal beta-oxidation-related proteins (PubMed:25489022). Involved CC in the positive regulation of salt stress responses. May function by CC increasing chloride channel activities on vacuolar membranes CC (PubMed:27676158). {ECO:0000269|PubMed:25489022, CC ECO:0000269|PubMed:27676158}. 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 -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, composed CC of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant CC regulatory subunit (subunit A), that associates with a variety of CC regulatory subunits such as subunits B (the R2/B/PR55/B55, CC R3/B''/PR72/PR130/PR59 and R5/B'/B56 families). Also interacts with CC CHIP and TAF12B. Interacts with B'THETA (PubMed:25489022). Interacts CC with CLC-A, CLC-B, CLC-C and CLC-G (PubMed:27676158). CC {ECO:0000250|UniProtKB:P62714, ECO:0000269|PubMed:10091592, CC ECO:0000269|PubMed:16640601, ECO:0000269|PubMed:17526916, CC ECO:0000269|PubMed:25489022, ECO:0000269|PubMed:27676158}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:25489022}. CC Peroxisome {ECO:0000269|PubMed:25489022}. Note=Interacts with B'THETA CC in the cytosol and peroxisomal import occurs by a piggybacking CC transport. {ECO:0000269|PubMed:25489022}. CC -!- INDUCTION: Induced by salt stress. {ECO:0000269|PubMed:27676158}. CC -!- PTM: Reversibly methyl esterified on Leu-307 by leucine carboxyl CC methyltransferase 1 (LCMT1) and pectin methylesterase 1 (PME1). CC Carboxyl methylation influences the affinity of the catalytic subunit CC for the different regulatory subunits, thereby modulating the PP2A CC holoenzyme's substrate specificity, enzyme activity and cellular CC localization. {ECO:0000305|PubMed:28741704}. CC -!- PTM: Phosphorylation of either threonine (by autophosphorylation- CC activated protein kinase) or tyrosine results in inactivation of the CC phosphatase. Auto-dephosphorylation has been suggested as a mechanism CC for reactivation. {ECO:0000250|UniProtKB:P67774}. CC -!- PTM: Ubiquitinated. CHIP-mediated ubiquitination enhances phosphatase CC activity after an abiotic stress such as low temperature or darkness CC (By similarity). {ECO:0000250}. CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth CC conditions, but mutant plants are hypersensitive to salt stress. CC {ECO:0000269|PubMed:27676158}. CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2A subfamily. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U39568; AAC49668.1; -; mRNA. DR EMBL; AC002062; AAB61116.1; -; Genomic_DNA. DR EMBL; AC010675; AAG52565.1; -; Genomic_DNA. DR EMBL; CP002684; AEE35002.1; -; Genomic_DNA. DR EMBL; BT025871; ABF85773.1; -; mRNA. DR EMBL; AK227054; BAE99114.1; -; mRNA. DR PIR; B96722; B96722. DR RefSeq; NP_177154.1; NM_105665.3. DR AlphaFoldDB; O04951; -. DR SMR; O04951; -. DR BioGRID; 28554; 17. DR IntAct; O04951; 1. DR STRING; 3702.O04951; -. DR PaxDb; 3702-AT1G69960-1; -. DR ProteomicsDB; 249116; -. DR EnsemblPlants; AT1G69960.1; AT1G69960.1; AT1G69960. DR GeneID; 843333; -. DR Gramene; AT1G69960.1; AT1G69960.1; AT1G69960. DR KEGG; ath:AT1G69960; -. DR Araport; AT1G69960; -. DR TAIR; AT1G69960; PP2A. DR eggNOG; KOG0371; Eukaryota. DR HOGENOM; CLU_004962_8_1_1; -. DR InParanoid; O04951; -. DR OMA; SECKPLS; -. DR OrthoDB; 19833at2759; -. DR PhylomeDB; O04951; -. DR PRO; PR:O04951; -. DR Proteomes; UP000006548; Chromosome 1. DR ExpressionAtlas; O04951; baseline and differential. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0005777; C:peroxisome; 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 GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISS:TAIR. DR GO; GO:2000012; P:regulation of auxin polar transport; IMP:TAIR. 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:SF59; 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. DR Genevisible; O04951; AT. PE 1: Evidence at protein level; KW Cytoplasm; Hydrolase; Manganese; Metal-binding; Methylation; Peroxisome; KW Phosphoprotein; Protein phosphatase; Reference proteome; Stress response; KW Ubl conjugation. FT CHAIN 1..307 FT /note="Serine/threonine-protein phosphatase PP2A-5 FT catalytic subunit" FT /id="PRO_0000058856" 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|UniProtKB:P67775" FT BINDING 57 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P67775" FT BINDING 83 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P67775" FT BINDING 83 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P67775" FT BINDING 115 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P67775" FT BINDING 165 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P67775" FT BINDING 239 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P67775" FT MOD_RES 307 FT /note="Leucine methyl ester" FT /evidence="ECO:0000305|PubMed:28741704" SQ SEQUENCE 307 AA; 35042 MW; D00149EA0E20C82F CRC64; MPPATGDIDR QIEQLMECKA LSETEVKMLC EHAKTILVEE YNVQPVKCPV TVCGDIHGQF YDLIELFRIG GSSPDTNYLF MGDYVDRGYY SVETVSLLVA LKVRYRDRLT ILRGNHESRQ ITQVYGFYDE CLRKYGNANV WKHFTDLFDY LPLTALIESQ VFCLHGGLSP SLDTLDNIRS LDRIQEVPHE GPMCDLLWSD PDDRCGWGIS PRGAGYTFGQ DIATQFNHTN GLSLISRAHQ LVMEGFNWCQ EKNVVTVFSA PNYCYRCGNM AAILEIGENM DQNFLQFDPA PRQVEPETTR KTPDYFL //