2A5N_ARATH
ID 2A5N_ARATH Reviewed; 510 AA.
AC Q9LU89; B9DH07;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Serine/threonine protein phosphatase 2A 59 kDa regulatory subunit B' eta isoform;
DE Short=AtB' eta;
DE Short=PP2A, B' subunit, eta isoform;
GN Name=B'ETA; OrderedLocusNames=At3g26020; ORFNames=MPE11.19;
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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
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 [6]
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 [7]
RP INTERACTION WITH BZR1.
RX PubMed=21258370; DOI=10.1038/ncb2151;
RA Tang W., Yuan M., Wang R., Yang Y., Wang C., Oses-Prieto J.A., Kim T.W.,
RA Zhou H.W., Deng Z., Gampala S.S., Gendron J.M., Jonassen E.M., Lillo C.,
RA DeLong A., Burlingame A.L., Sun Y., Wang Z.Y.;
RT "PP2A activates brassinosteroid-responsive gene expression and plant growth
RT by dephosphorylating BZR1.";
RL Nat. Cell Biol. 13:124-131(2011).
RN [8]
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 [9]
RP FUNCTION, INTERACTION WITH BRI1, SUBCELLULAR LOCATION, AND INDUCTION BY
RP EPIBRASSINOLIDE.
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'ETA acts as
CC 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). {ECO:0000250|UniProtKB:Q13362,
CC ECO:0000269|PubMed:25085430, 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) (By
CC similarity). Interacts with BZR1 (PubMed:21258370). Interacts with BRI1
CC (PubMed:26517938). {ECO:0000250|UniProtKB:Q13362,
CC ECO:0000269|PubMed:21258370, ECO:0000269|PubMed:26517938}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:19672620}.
CC Cytoplasm {ECO:0000269|PubMed:26517938}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9LU89-1; Sequence=Displayed;
CC -!- INDUCTION: Induced by epibrassinolide. {ECO:0000269|PubMed:26517938}.
CC -!- DISRUPTION PHENOTYPE: Delayed flowering. {ECO:0000269|PubMed:19672620}.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56
CC family. {ECO:0000305}.
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DR EMBL; AB023041; BAB01065.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77102.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77103.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64831.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64832.1; -; Genomic_DNA.
DR EMBL; AF367267; AAK56256.1; -; mRNA.
DR EMBL; AY059158; AAL15383.1; -; mRNA.
DR EMBL; AK317352; BAH20024.1; -; mRNA.
DR RefSeq; NP_001030770.1; NM_001035693.2. [Q9LU89-1]
DR RefSeq; NP_001326835.1; NM_001338774.1. [Q9LU89-1]
DR RefSeq; NP_001326836.1; NM_001338775.1. [Q9LU89-1]
DR RefSeq; NP_189231.1; NM_113506.2. [Q9LU89-1]
DR AlphaFoldDB; Q9LU89; -.
DR SMR; Q9LU89; -.
DR BioGRID; 7530; 3.
DR IntAct; Q9LU89; 2.
DR PRIDE; Q9LU89; -.
DR ProteomicsDB; 244587; -. [Q9LU89-1]
DR EnsemblPlants; AT3G26020.1; AT3G26020.1; AT3G26020. [Q9LU89-1]
DR EnsemblPlants; AT3G26020.2; AT3G26020.2; AT3G26020. [Q9LU89-1]
DR EnsemblPlants; AT3G26020.5; AT3G26020.5; AT3G26020. [Q9LU89-1]
DR EnsemblPlants; AT3G26020.6; AT3G26020.6; AT3G26020. [Q9LU89-1]
DR GeneID; 822199; -.
DR Gramene; AT3G26020.1; AT3G26020.1; AT3G26020. [Q9LU89-1]
DR Gramene; AT3G26020.2; AT3G26020.2; AT3G26020. [Q9LU89-1]
DR Gramene; AT3G26020.5; AT3G26020.5; AT3G26020. [Q9LU89-1]
DR Gramene; AT3G26020.6; AT3G26020.6; AT3G26020. [Q9LU89-1]
DR KEGG; ath:AT3G26020; -.
DR Araport; AT3G26020; -.
DR HOGENOM; CLU_012437_4_1_1; -.
DR OMA; NHEDQER; -.
DR PhylomeDB; Q9LU89; -.
DR PRO; PR:Q9LU89; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LU89; baseline and differential.
DR Genevisible; Q9LU89; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
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 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 1: Evidence at protein level;
KW Alternative splicing; Brassinosteroid signaling pathway; Cytoplasm;
KW Nucleus; Plant defense; Reference proteome.
FT CHAIN 1..510
FT /note="Serine/threonine protein phosphatase 2A 59 kDa
FT regulatory subunit B' eta isoform"
FT /id="PRO_0000071466"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 510 AA; 58758 MW; 02D36540CB860D28 CRC64;
MWKQILSKLP NKKSSKHEHR GREHGGHSSS SSHTSGASTS KSTDNGAAKS HAKNASPAGK
SAASDSGFKD GNLKSSGNNN NNNNNGVFTP YEALPSFKDV PNTEKQNLFI KKLNLCRVVF
DFTDPTKNIK EKDIKRQTLL ELVDYVNSPN GKFSEVGIQE VVRMVSANIF RTLNPQPREN
KVIDALDLEE EEPSMDLAWP HLQLVYELFL RFVASPETDT KLAKRYIDQS FVLRLLDLFD
SEDPRERDCL KTILHRIYGK FMVHRPFIRK SINNIFYRFV FETEKHNGIA EFLEILGSII
NGFALPLKDE HKVFLVRVLI PLHKPKCLQM YHQQLSYCIT QFVEKDCKLA DTVIRGLLKY
WPVTNSSKEV MFLNELEEVL EATQPPEFQR CMVPLFRQIA RCLNSLHFQV AERALFLWNN
NHIENLIMQN RKVILPIIFP ALERNAQKHW NQAVHSLTLN VRKIFHDLDP ELFKECLAKF
KEDESKAAET EAKREATWKR LEELGVRKAS
