2A5T_ARATH
ID 2A5T_ARATH Reviewed; 492 AA.
AC Q8LF36; Q0V836; Q9FX52;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 2.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Serine/threonine protein phosphatase 2A 57 kDa regulatory subunit B' theta isoform;
DE Short=AtB' theta;
DE Short=PP2A, B' subunit, theta isoform;
GN Name=B'THETA; OrderedLocusNames=At1g13460; ORFNames=T6J4.19;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF Clones.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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, MUTAGENESIS OF 489-LYS--LEU-492, AND DISRUPTION
RP 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, INTERACTION WITH PP2A2; PP2A5 AND PP2AA2, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=25489022; DOI=10.1104/pp.114.254409;
RA Kataya A.R., Heidari B., Hagen L., Kommedal R., Slupphaug G., Lillo C.;
RT "Protein phosphatase 2A holoenzyme is targeted to peroxisomes by
RT piggybacking and positively affects peroxisomal beta-oxidation.";
RL Plant Physiol. 167:493-506(2015).
RN [9]
RP FUNCTION, 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 (By
CC similarity). Associates with the serine/threonine-protein phosphatase
CC PP2A catalytic subunit C and regulatory subunit A to positively
CC regulates beta-oxidation of fatty acids and protoauxins in peroxisomes
CC by dephosphorylating peroxisomal beta-oxidation-related proteins
CC (PubMed:25489022). Required for the formation of the PP2A holoenzyme
CC 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:25489022, 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
CC PP2A2, PP2A5 and PP2AA2 (PubMed:25489022).
CC {ECO:0000250|UniProtKB:Q13362, ECO:0000269|PubMed:21258370,
CC ECO:0000269|PubMed:25489022}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:25489022,
CC ECO:0000269|PubMed:26517938}. Peroxisome {ECO:0000269|PubMed:19672620,
CC ECO:0000269|PubMed:25489022}.
CC -!- TISSUE SPECIFICITY: Highly expressed in dry seeds. Expressed in roots,
CC cotyledons, rosette leaves and flowers. {ECO:0000269|PubMed:25489022}.
CC -!- INDUCTION: Induced by epibrassinolide. {ECO:0000269|PubMed:26517938}.
CC -!- DISRUPTION PHENOTYPE: Reduced plant size and fresh weight.
CC {ECO:0000269|PubMed:19672620}.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56
CC family. {ECO:0000305}.
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DR EMBL; AC011810; AAG09562.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29021.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29022.1; -; Genomic_DNA.
DR EMBL; AY085069; AAM61625.1; -; mRNA.
DR EMBL; BT026384; ABH04491.1; -; mRNA.
DR RefSeq; NP_172803.1; NM_101216.2.
DR RefSeq; NP_973816.1; NM_202087.2.
DR AlphaFoldDB; Q8LF36; -.
DR SMR; Q8LF36; -.
DR BioGRID; 23146; 2.
DR STRING; 3702.AT1G13460.2; -.
DR PaxDb; Q8LF36; -.
DR PRIDE; Q8LF36; -.
DR ProteomicsDB; 244608; -.
DR EnsemblPlants; AT1G13460.1; AT1G13460.1; AT1G13460.
DR EnsemblPlants; AT1G13460.2; AT1G13460.2; AT1G13460.
DR GeneID; 837906; -.
DR Gramene; AT1G13460.1; AT1G13460.1; AT1G13460.
DR Gramene; AT1G13460.2; AT1G13460.2; AT1G13460.
DR KEGG; ath:AT1G13460; -.
DR Araport; AT1G13460; -.
DR TAIR; locus:2009912; AT1G13460.
DR eggNOG; KOG2085; Eukaryota.
DR HOGENOM; CLU_012437_4_1_1; -.
DR OMA; FMEINQR; -.
DR OrthoDB; 890437at2759; -.
DR PhylomeDB; Q8LF36; -.
DR PRO; PR:Q8LF36; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8LF36; baseline and differential.
DR Genevisible; Q8LF36; AT.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; 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:1900458; P:negative regulation of brassinosteroid mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0032000; P:positive regulation of fatty acid beta-oxidation; 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 1: Evidence at protein level;
KW Brassinosteroid signaling pathway; Cytoplasm; Peroxisome;
KW Reference proteome.
FT CHAIN 1..492
FT /note="Serine/threonine protein phosphatase 2A 57 kDa
FT regulatory subunit B' theta isoform"
FT /id="PRO_0000071467"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 490..492
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000269|PubMed:19672620"
FT COMPBIAS 8..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 489..492
FT /note="Missing: Loss of peroxisomal targeting."
FT /evidence="ECO:0000269|PubMed:19672620"
FT CONFLICT 34
FT /note="S -> G (in Ref. 4; AAM61625)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="Q -> K (in Ref. 4; AAM61625)"
FT /evidence="ECO:0000305"
FT CONFLICT 488
FT /note="Q -> K (in Ref. 4; AAM61625)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 492 AA; 56510 MW; E49174DE756FE2CE CRC64;
MWKQILSKLP KKSSSKNHSS SSSSTSKSSD NGASKSGNSQ TQNAPPVKPS ADSGFKEGNL
KGNGNGFTPY EALPGFKDVP NAEKQNLFVR KLSLCCVVFD FSDPTKNVKE KDIKRQTLLE
LVDYVASPNG KFSETVIQEV VRMVSVNIFR TLNPQPRENK VIDALDLEEE EPSMDPTWPH
LQLVYEILLR LIASPETDTK LAKKYIDQSF VSRLLDLFDS EDPRERDCLK TVLHRIYGKF
MVHRPFIRKS INNIFYRFVF ETEKHNGIAE FLEILGSIIN GFALPLKDEH KVFLVRALVP
LHKPKSLQMY HQQLSYCITQ FVEKDCKLAD TVIRGLLKSW PVTNSSKEVM FLNELEEVLE
ATQPPEFQRC MVPLFRQVAR CLNSLHFQVA ERALFLWNND HIENLIMQNR KVILPIIFPA
LERNTQKHWN QAVHSLTLNV QKIFNDIDAE LFKDCLAKFR EDESKEAEIG AKREATWKRL
EEIGNQKQKS SL
