2A5A_ARATH
ID 2A5A_ARATH Reviewed; 495 AA.
AC O04375;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Serine/threonine protein phosphatase 2A 57 kDa regulatory subunit B' alpha isoform;
DE Short=AtB' alpha;
DE Short=PP2A, B' subunit, alpha isoform;
GN Name=B'ALPHA; OrderedLocusNames=At5g03470; ORFNames=F12E4.240;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 leaves.
CC {ECO:0000269|PubMed:9128737}.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56
CC family. {ECO:0000305}.
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DR EMBL; U73526; AAB58900.1; -; mRNA.
DR EMBL; AL162751; CAB83307.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90609.1; -; Genomic_DNA.
DR EMBL; BT002933; AAO22747.1; -; mRNA.
DR PIR; T48372; T48372.
DR RefSeq; NP_195967.1; NM_120427.3.
DR AlphaFoldDB; O04375; -.
DR SMR; O04375; -.
DR BioGRID; 17104; 3.
DR STRING; 3702.AT5G03470.1; -.
DR PaxDb; O04375; -.
DR PRIDE; O04375; -.
DR ProteomicsDB; 245146; -.
DR EnsemblPlants; AT5G03470.1; AT5G03470.1; AT5G03470.
DR GeneID; 831828; -.
DR Gramene; AT5G03470.1; AT5G03470.1; AT5G03470.
DR KEGG; ath:AT5G03470; -.
DR Araport; AT5G03470; -.
DR TAIR; locus:2142619; AT5G03470.
DR eggNOG; KOG2085; Eukaryota.
DR HOGENOM; CLU_012437_4_1_1; -.
DR OMA; EREDPMI; -.
DR OrthoDB; 890437at2759; -.
DR PhylomeDB; O04375; -.
DR PRO; PR:O04375; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; O04375; baseline and differential.
DR Genevisible; O04375; 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; ISS:TAIR.
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 GO; GO:0042325; P:regulation of phosphorylation; ISS: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..495
FT /note="Serine/threonine protein phosphatase 2A 57 kDa
FT regulatory subunit B' alpha isoform"
FT /id="PRO_0000071460"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 495 AA; 57536 MW; 545F041C4ACB4A29 CRC64;
MFKKIMKGAN RKASKAEAND SSMYGFDPPG RSGPGSNMIV NHASRGSLVP SSPNSMAAAT
TQPPPMYSVE PLPLFRDVSV SERQSLFLRK LQICCFQFDF TDTLKNAREK EIKRQTLLEL
VDFIQSGAGK LTEVCQEEMV KMISVNIFRC LPPASHENTG QEPADLEEEE PYLEPSWPHL
QLIYELLLRY IVPSDTDTKV AKRYIDHSFV LRLLELFETE DPREREYLKT ILHRIYGKFM
VHRPFIRKAM NHIFYRFIYE TERHSGIGEL LEILGSIING FALPMKEEHK LFLIRALIPL
HKPKPIAMYH QQLSYCIVQF VEKDYKLADT VIRGLLKFWP VTNCTKEVLF LGELEEVLEA
TQTVEFQRCM VPLFQQIARC LSSSNFQVAE RALFLWNNEH VVGLIAQNRG VILPIIFASL
EKNIESHWNQ AVHGLSANIK RMFMEMDPEL FEECQQQYEE KQAKSKQVEE QRQNRWRRLD
EAVEERERED PMITS
