2A5Z_ARATH
ID 2A5Z_ARATH Reviewed; 546 AA.
AC Q9LVE2; Q0WUV1;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 2.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Serine/threonine protein phosphatase 2A 59 kDa regulatory subunit B' zeta isoform;
DE Short=AtB' zeta;
DE Short=PP2A, B' subunit, zeta isoform;
GN Name=B'ZETA; OrderedLocusNames=At3g21650; ORFNames=MIL23.22;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [2]
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 [3]
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 [4]
RP NOMENCLATURE.
RX PubMed=12068121; DOI=10.1104/pp.020004;
RA Terol J., Bargues M., Carrasco P., Perez-Alonso M., Paricio N.;
RT "Molecular characterization and evolution of the protein phosphatase 2A B'
RT regulatory subunit family in plants.";
RL Plant Physiol. 129:808-822(2002).
RN [5]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=19672620; DOI=10.1007/s00425-009-0998-z;
RA Matre P., Meyer C., Lillo C.;
RT "Diversity in subcellular targeting of the PP2A B'eta subfamily members.";
RL Planta 230:935-945(2009).
RN [6]
RP FUNCTION.
RX PubMed=25085430; DOI=10.15252/embj.201488698;
RA Segonzac C., Macho A.P., Sanmartin M., Ntoukakis V., Sanchez-Serrano J.J.,
RA Zipfel C.;
RT "Negative control of BAK1 by protein phosphatase 2A during plant innate
RT immunity.";
RL EMBO J. 33:2069-2079(2014).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=26012558; DOI=10.1111/pce.12575;
RA Konert G., Rahikainen M., Trotta A., Durian G., Salojaervi J.,
RA Khorobrykh S., Tyystjaervi E., Kangasjaervi S.;
RT "Subunits B'gamma and B'zeta of protein phosphatase 2A regulate photo-
RT oxidative stress responses and growth in Arabidopsis thaliana.";
RL Plant Cell Environ. 38:2641-2651(2015).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=26517938; DOI=10.1016/j.molp.2015.10.007;
RA Wang R., Liu M., Yuan M., Oses-Prieto J.A., Cai X., Sun Y.,
RA Burlingame A.L., Wang Z.Y., Tang W.;
RT "The brassinosteroid-activated BRI1 receptor kinase is switched off by
RT dephosphorylation mediated by cytoplasm-localized PP2A B' subunits.";
RL Mol. Plant 9:148-157(2016).
CC -!- FUNCTION: The B regulatory subunit may modulate substrate selectivity
CC and catalytic activity, and also may direct the localization of the
CC catalytic enzyme to a particular subcellular compartment (By
CC similarity). The holoenzyme composed of PP2AA1, PP2A4 and B'ZETA acts
CC as negative regulator of plant innate immunity by controlling BAK1
CC phosphorylation state and activation in surface-localized immune
CC receptor complexes (PubMed:25085430). Required for the formation of the
CC PP2A holoenzyme that negatively regulates brassinosteroid signaling by
CC dephosphorylating and inactivating BRI1 in the cytoplasm
CC (PubMed:26517938). Involved in growth regulation and stress signaling.
CC Involved in the regulation of reactive oxygen species (ROS) signaling
CC (PubMed:26012558). {ECO:0000250|UniProtKB:Q13362,
CC ECO:0000269|PubMed:25085430, ECO:0000269|PubMed:26012558,
CC ECO:0000269|PubMed:26517938}.
CC -!- SUBUNIT: PP2A consists of a common heteromeric enzyme, composed of a
CC catalytic subunit (subunits C), a constant regulatory subunit (subunit
CC A), and a variety of regulatory subunits such as subunits B (the
CC R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families).
CC {ECO:0000250|UniProtKB:Q13362}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:19672620,
CC ECO:0000269|PubMed:26517938}. Mitochondrion
CC {ECO:0000269|PubMed:19672620}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, emerging lateral roots,
CC cotyledons, leaves, floral stalks and flowers.
CC {ECO:0000269|PubMed:26012558}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:19672620}.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02360.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB019232; BAB02360.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76534.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64496.1; -; Genomic_DNA.
DR EMBL; AK227037; BAE99097.1; -; mRNA.
DR RefSeq; NP_001326520.1; NM_001338546.1.
DR RefSeq; NP_188802.1; NM_113060.5.
DR AlphaFoldDB; Q9LVE2; -.
DR SMR; Q9LVE2; -.
DR BioGRID; 7051; 2.
DR STRING; 3702.AT3G21650.1; -.
DR PaxDb; Q9LVE2; -.
DR PRIDE; Q9LVE2; -.
DR ProteomicsDB; 245076; -.
DR EnsemblPlants; AT3G21650.1; AT3G21650.1; AT3G21650.
DR EnsemblPlants; AT3G21650.2; AT3G21650.2; AT3G21650.
DR GeneID; 821719; -.
DR Gramene; AT3G21650.1; AT3G21650.1; AT3G21650.
DR Gramene; AT3G21650.2; AT3G21650.2; AT3G21650.
DR KEGG; ath:AT3G21650; -.
DR Araport; AT3G21650; -.
DR TAIR; locus:2089905; AT3G21650.
DR eggNOG; KOG2085; Eukaryota.
DR HOGENOM; CLU_012437_4_1_1; -.
DR OMA; MHDLEDE; -.
DR OrthoDB; 890437at2759; -.
DR PhylomeDB; Q9LVE2; -.
DR PRO; PR:Q9LVE2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LVE2; baseline and differential.
DR Genevisible; Q9LVE2; AT.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IEA:InterPro.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IEA:InterPro.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:1900458; P:negative regulation of brassinosteroid mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0045824; P:negative regulation of innate immune response; IDA:UniProtKB.
DR GO; GO:0080183; P:response to photooxidative stress; IMP:UniProtKB.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002554; PP2A_B56.
DR PANTHER; PTHR10257; PTHR10257; 1.
DR Pfam; PF01603; B56; 1.
DR PIRSF; PIRSF028043; PP2A_B56; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 2: Evidence at transcript level;
KW Brassinosteroid signaling pathway; Cytoplasm; Mitochondrion; Plant defense;
KW Reference proteome; Stress response.
FT CHAIN 1..546
FT /note="Serine/threonine protein phosphatase 2A 59 kDa
FT regulatory subunit B' zeta isoform"
FT /id="PRO_0000071465"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 546 AA; 61731 MW; 92CF0EE7E1126D78 CRC64;
MIKQIFGKLP RKPSKSLQND SNGEGGVNNS YYASNSSTTS ISKPSSTSSK SSSASGSRVA
NGTLAPNSMS SNRNTNQGKK PLGGDAVVQA GPFPSSGGVY EALPSFRDVP ISEKPNLFIG
KLSMCCVVFD FSDPSKNLKE KEIKRQTLLE LVDYVASVGF KFNDVSMQEL TKMVAVNLFR
TFPSANHESK ILEIHDMDDE EPSLEPAWPH VQVVYEILLR FVASPMTDAK LAKRYIDHSF
VLKLLDLFDS EDQREREYLK TILHRVYGKF MVHRPYIRKA INNIFYRFIS ETEKHNGIAE
LLEILGSIIN GFALPLKEEH KLFLLRALIP LHKPKCSSVY HQQLSYCIVQ FVEKDFKLAD
TVIRGLLKYW PVTNSSKEVM FLGELEEVLE ATQAAEFQRC MVPLSRQIAR CLNSSHFQVA
ERALFLWNND HIRNLITQNH KVIMPIVFPA LERNTRGHWN QAVQSLTINV RKVLCEIDQV
LFDECLAKFQ VEEVNKTEVK AKRERTWQRL EDLATSKTVV TNEAVLVPRF VSSVNLTTSS
SESTGS
