ID   2A5B_ARATH              Reviewed;         499 AA.
AC   O04376;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 124.
DE   RecName: Full=Serine/threonine protein phosphatase 2A 57 kDa regulatory subunit B' beta isoform;
DE            Short=AtB' beta;
DE            Short=PP2A, B' subunit, beta isoform;
GN   Name=B'BETA; OrderedLocusNames=At3g09880; ORFNames=F8A24.7;
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], AND TISSUE SPECIFICITY.
RX   PubMed=9128737; DOI=10.1111/j.1432-1033.1997.00156.x;
RA   Latorre K.A., Harris D.M., Rundle S.J.;
RT   "Differential expression of three Arabidopsis genes encoding the B'
RT   regulatory subunit of protein phosphatase 2A.";
RL   Eur. J. Biochem. 245:156-163(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(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;
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   [5]
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   [6]
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   [7]
RP   FUNCTION, AND 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   IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH SRK2E/OST1.
RX   PubMed=26175513; DOI=10.1104/pp.15.00575;
RA   Waadt R., Manalansan B., Rauniyar N., Munemasa S., Booker M.A., Brandt B.,
RA   Waadt C., Nusinow D.A., Kay S.A., Kunz H.H., Schumacher K., DeLong A.,
RA   Yates J.R. III, Schroeder J.I.;
RT   "Identification of Open Stomata1-interacting proteins reveals interactions
RT   with sucrose non-fermenting1-related protein kinases2 and with type 2a
RT   protein phosphatases that function in abscisic acid responses.";
RL   Plant Physiol. 169:760-779(2015).
RN   [9]
RP   INTERACTION WITH BRI1, 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). Required for the formation of the PP2A holoenzyme that
CC       positively regulates brassinosteroid signaling by dephosphorylating and
CC       activating BZR1 (PubMed:21258370). {ECO:0000250|UniProtKB:Q13362,
CC       ECO:0000269|PubMed:21258370}.
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       (Probable). Interacts with BZR1 (PubMed:21258370). Interacts with BRI1
CC       (PubMed:26517938). Interacts with SRK2E/OST1 (PubMed:26175513).
CC       {ECO:0000269|PubMed:21258370, ECO:0000269|PubMed:26175513,
CC       ECO:0000269|PubMed:26517938, ECO:0000305|PubMed:10091592}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26517938}. Cytoplasm
CC       {ECO:0000269|PubMed:26517938}.
CC   -!- TISSUE SPECIFICITY: Expressed ubiquitously, higher levels in cotyledons
CC       and flowers. {ECO:0000269|PubMed:9128737}.
CC   -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56
CC       family. {ECO:0000305}.
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DR   EMBL; U73527; AAB58901.1; -; mRNA.
DR   EMBL; AC015985; AAF23248.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE74825.1; -; Genomic_DNA.
DR   EMBL; AY113852; AAM44900.1; -; mRNA.
DR   EMBL; AY072226; AAL60047.1; -; mRNA.
DR   RefSeq; NP_187599.1; NM_111823.3.
DR   AlphaFoldDB; O04376; -.
DR   SMR; O04376; -.
DR   BioGRID; 5480; 4.
DR   STRING; 3702.AT3G09880.1; -.
DR   PaxDb; O04376; -.
DR   PRIDE; O04376; -.
DR   ProteomicsDB; 245133; -.
DR   EnsemblPlants; AT3G09880.1; AT3G09880.1; AT3G09880.
DR   GeneID; 820146; -.
DR   Gramene; AT3G09880.1; AT3G09880.1; AT3G09880.
DR   KEGG; ath:AT3G09880; -.
DR   Araport; AT3G09880; -.
DR   TAIR; locus:2085099; AT3G09880.
DR   eggNOG; KOG2085; Eukaryota.
DR   HOGENOM; CLU_012437_4_1_1; -.
DR   OMA; CSHEYNE; -.
DR   OrthoDB; 890437at2759; -.
DR   PhylomeDB; O04376; -.
DR   PRO; PR:O04376; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; O04376; baseline and differential.
DR   Genevisible; O04376; AT.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; 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:0009554; P:megasporogenesis; IGI:TAIR.
DR   GO; GO:0051177; P:meiotic sister chromatid cohesion; IGI:TAIR.
DR   GO; GO:0009556; P:microsporogenesis; IGI:TAIR.
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   Brassinosteroid signaling pathway; Cytoplasm; Nucleus; Reference proteome.
FT   CHAIN           1..499
FT                   /note="Serine/threonine protein phosphatase 2A 57 kDa
FT                   regulatory subunit B' beta isoform"
FT                   /id="PRO_0000071461"
FT   REGION          1..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   499 AA;  57472 MW;  BA375FA980286A0F CRC64;
     MFKKIMKGGH RKPSKSEANE PSSYGIGLPD NRSGPGSNVV VSHASRGALV NSSPSPVTAT
     PPPPPLGSVE PLPLFRDVPV SERQTLFLRK LQNCCFLFDF TDTIKNARDK EIKRQTLLEL
     VDFIQSGSSK ISESCQEEMI KMISVNIFRS LPPASHENTG QEPADPEEEE PYLEPSWPHL
     QLVYELLLRY VVSTDTDTKV AKRYIDHSFV LKLLDLFDSE DPREREYLKT ILHRIYGKFM
     VHRPFIRKAI NNIFYRFIYE TERHSGIGEL LEILGSIING FALPMKEEHK LFLIRVLIPL
     HKPKPIVVYH QQLSYCIVQF VEKDYKLADT VIRGLLKYWP VTNCSKENLF LGELEEVLEA
     TQPVEFQRCM VPLFQQIGRC LTSSHFQVAE RALFLWNNEH IVGLIAQNRS VILPIIYPTL
     EKNIQSHWNQ AVHGLTTNIK KMFMEMDPEL FEECQRQYEE KQAKSKEVEE QRQYTWKRLA
     EAAAERDGGG GEEDHMITS