PP2A5_ARATH
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 03-AUG-2022, entry version 156.
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}.
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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.AT1G69960.1; -.
DR PaxDb; O04951; -.
DR PRIDE; O04951; -.
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; locus:2020598; AT1G69960.
DR eggNOG; KOG0371; Eukaryota.
DR HOGENOM; CLU_004962_8_1_1; -.
DR OMA; TEVKMLC; -.
DR OrthoDB; 808922at2759; -.
DR PhylomeDB; O04951; -.
DR PRO; PR:O04951; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O04951; baseline and differential.
DR Genevisible; O04951; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:2000012; P:regulation of auxin polar transport; IMP:TAIR.
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 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
