2A5D_ARATH
ID 2A5D_ARATH Reviewed; 477 AA.
AC Q9ZQY6;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Serine/threonine protein phosphatase 2A 55 kDa regulatory subunit B' delta isoform;
DE Short=AtB' delta;
DE Short=PP2A, B' subunit, delta isoform;
GN Name=B'DELTA; OrderedLocusNames=At3g26030; ORFNames=MPE11.23;
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], TISSUE SPECIFICITY, AND INTERACTION WITH
RP PP2AA1.
RC STRAIN=cv. Columbia;
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 [2]
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 [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 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 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 [7]
RP SUBCELLULAR LOCATION, AND INDUCTION BY 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.
CC {ECO:0000250|UniProtKB:Q13362}.
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 SRK2E/OST1 (PubMed:26175513).
CC {ECO:0000269|PubMed:26175513, ECO:0000305|PubMed:10091592}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26517938}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously.
CC {ECO:0000269|PubMed:10091592}.
CC -!- INDUCTION: Induced by epibrassinolide. {ECO:0000269|PubMed:26517938}.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56
CC family. {ECO:0000305}.
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DR EMBL; AF062396; AAD02810.1; -; mRNA.
DR EMBL; AB023041; BAB01066.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77106.1; -; Genomic_DNA.
DR EMBL; AY091037; AAM13858.1; -; mRNA.
DR EMBL; AY117349; AAM51424.1; -; mRNA.
DR RefSeq; NP_189232.1; NM_113507.3.
DR AlphaFoldDB; Q9ZQY6; -.
DR SMR; Q9ZQY6; -.
DR BioGRID; 7531; 8.
DR IntAct; Q9ZQY6; 7.
DR STRING; 3702.AT3G26030.1; -.
DR PaxDb; Q9ZQY6; -.
DR PRIDE; Q9ZQY6; -.
DR ProteomicsDB; 245134; -.
DR EnsemblPlants; AT3G26030.1; AT3G26030.1; AT3G26030.
DR GeneID; 822200; -.
DR Gramene; AT3G26030.1; AT3G26030.1; AT3G26030.
DR KEGG; ath:AT3G26030; -.
DR Araport; AT3G26030; -.
DR TAIR; locus:2092080; AT3G26030.
DR eggNOG; KOG2085; Eukaryota.
DR HOGENOM; CLU_012437_4_1_1; -.
DR OMA; FERCMIP; -.
DR OrthoDB; 890437at2759; -.
DR PhylomeDB; Q9ZQY6; -.
DR PRO; PR:Q9ZQY6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9ZQY6; baseline and differential.
DR Genevisible; Q9ZQY6; AT.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005730; C:nucleolus; HDA: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:0007165; P:signal transduction; IEA:InterPro.
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 Cytoplasm; Reference proteome.
FT CHAIN 1..477
FT /note="Serine/threonine protein phosphatase 2A 55 kDa
FT regulatory subunit B' delta isoform"
FT /id="PRO_0000071463"
SQ SEQUENCE 477 AA; 55240 MW; 232DD0C6DD844414 CRC64;
MFKQILGKLP KKTSAKFWDN GESQTLDNNN NQGGGDEVLS QRTSSNGDTS LDCVSSFDVL
PRLRDVSISE KQELFLKKLR LCCLVFDFVA EPQQNFKEKE IKRQTLLEVV DYVISSGNGK
FPESVIQEAT KMISANLFSN PHRQWKNKTP EALDLEEEEG SLNPSWPHLQ IVYEFLLRIV
ASPNTDPKIS KKYIDHTFVL KLLDLFDSED PREREYLKTI LHRIYGRFMV HRPFIRKTMN
NILYDFIFET GKHSGIAEFL EVLGSIINGF ALPLKEEHKL FLTRVLIPLH KLKCLPNYHQ
QLSYCVIQFV EKDCKLADTV IRGMLKYWPV TNSAKEIMFL NELEEILEAT QLTEFERCMV
PLSRQIAQCL SSSHFQVAER ALYLWNNDHV TNLVRQNSRI ILPIVFPALE KNGSSHWNQA
VKNLTENVLK VLSDTNPDLF EECLHKFQED QQKAEDTKKK NGETWRQLEE IVASMAK