2AAB_ARATH
ID 2AAB_ARATH Reviewed; 587 AA.
AC Q38950; Q9LRZ9;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 25-MAY-2022, entry version 147.
DE RecName: Full=Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform;
DE Short=AtA beta;
DE Short=PP2A, subunit A, beta isoform;
GN Name=PP2AA2; Synonyms=DF1; OrderedLocusNames=At3g25800; ORFNames=K13N2.14;
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].
RC STRAIN=cv. Landsberg erecta; TISSUE=Leaf;
RX PubMed=7811971; DOI=10.1007/bf00040694;
RA Slabas A.R., Fordham-Skelton A.P., Fletcher D., Martinez-Rivas J.M.,
RA Swinhoe R., Croy R.R.D., Evans I.M.;
RT "Characterisation of cDNA and genomic clones encoding homologues of the 65
RT kDa regulatory subunit of protein phosphatase 2A in Arabidopsis thaliana.";
RL Plant Mol. Biol. 26:1125-1138(1994).
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 FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=14973165; DOI=10.1105/tpc.018994;
RA Zhou H.-W., Nussbaumer C., Chao Y., DeLong A.;
RT "Disparate roles for the regulatory A subunit isoforms in Arabidopsis
RT protein phosphatase 2A.";
RL Plant Cell 16:709-722(2004).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=22404109; DOI=10.1111/j.1365-313x.2012.04984.x;
RA Tran H.T., Nimick M., Uhrig R.G., Templeton G., Morrice N., Gourlay R.,
RA DeLong A., Moorhead G.B.;
RT "Arabidopsis thaliana histone deacetylase 14 (HDA14) is an alpha-tubulin
RT deacetylase that associates with PP2A and enriches in the microtubule
RT fraction with the putative histone acetyltransferase ELP3.";
RL Plant J. 71:263-272(2012).
RN [7]
RP FUNCTION, INTERACTION WITH B'THETA, AND SUBCELLULAR LOCATION.
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 [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 SIC/RON3.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=26888284; DOI=10.1073/pnas.1501343112;
RA Karampelias M., Neyt P., De Groeve S., Aesaert S., Coussens G., Rolcik J.,
RA Bruno L., De Winne N., Van Minnebruggen A., Van Montagu M., Ponce M.R.,
RA Micol J.L., Friml J., De Jaeger G., Van Lijsebettens M.;
RT "ROTUNDA3 function in plant development by phosphatase 2A-mediated
RT regulation of auxin transporter recycling.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:2768-2773(2016).
CC -!- FUNCTION: The A subunit of protein phosphatase 2A serves as a
CC scaffolding molecule to coordinate the assembly of the catalytic
CC subunit and a variable regulatory B subunit. Involved during
CC developmental process such as seedling and floral developments. Seems
CC to act as a negative regulator of PP2A catalytic activity. Associates
CC with the serine/threonine-protein phosphatase PP2A catalytic subunit C
CC and regulatory subunit B' to positively regulates beta-oxidation of
CC fatty acids and protoauxins in peroxisomes by dephosphorylating
CC peroxisomal beta-oxidation-related proteins (PubMed:25489022).
CC {ECO:0000269|PubMed:14973165, ECO:0000269|PubMed:25489022}.
CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, composed
CC of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant
CC regulatory subunit (subunit A), that associates with a variety of
CC regulatory subunits such as subunits B (the R2/B/PR55/B55,
CC R3/B''/PR72/PR130/PR59 and R5/B'/B56 families) (By similarity).
CC Interacts with B'THETA (PubMed:25489022). Interacts with SRK2E/OST1
CC (PubMed:26175513). Interacts with SIC/RON3 (PubMed:26888284).
CC {ECO:0000250|UniProtKB:P62714, ECO:0000269|PubMed:25489022,
CC ECO:0000269|PubMed:26175513, ECO:0000269|PubMed:26888284}.
CC -!- INTERACTION:
CC Q38950; Q9SZU7: KAI2; NbExp=3; IntAct=EBI-4467372, EBI-25519488;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:22404109,
CC ECO:0000269|PubMed:25489022}. Nucleus {ECO:0000269|PubMed:22404109}.
CC Peroxisome {ECO:0000269|PubMed:25489022}. Note=Interacts with B'THETA
CC in the cytosol and peroxisomal import occurs by a piggybacking
CC transport. {ECO:0000269|PubMed:25489022}.
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=Q38950-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Ubiquitous, with higher levels in roots and flowers
CC (at protein level). {ECO:0000269|PubMed:14973165}.
CC -!- DOMAIN: Each HEAT repeat appears to consist of two alpha helices joined
CC by a hydrophilic region, the intrarepeat loop. The repeat units may be
CC arranged laterally to form a rod-like structure (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit A family.
CC {ECO:0000305}.
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DR EMBL; X82002; CAA57528.1; -; mRNA.
DR EMBL; AB028607; BAA95767.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77069.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64959.1; -; Genomic_DNA.
DR EMBL; BT002488; AAO00848.1; -; mRNA.
DR EMBL; BT008356; AAP37715.1; -; mRNA.
DR PIR; S51808; S51808.
DR RefSeq; NP_001326959.1; NM_001338767.1. [Q38950-1]
DR RefSeq; NP_189208.1; NM_113479.5. [Q38950-1]
DR AlphaFoldDB; Q38950; -.
DR SMR; Q38950; -.
DR BioGRID; 7502; 46.
DR IntAct; Q38950; 5.
DR STRING; 3702.AT3G25800.1; -.
DR PaxDb; Q38950; -.
DR PRIDE; Q38950; -.
DR ProteomicsDB; 244571; -. [Q38950-1]
DR EnsemblPlants; AT3G25800.1; AT3G25800.1; AT3G25800. [Q38950-1]
DR EnsemblPlants; AT3G25800.3; AT3G25800.3; AT3G25800. [Q38950-1]
DR GeneID; 822171; -.
DR Gramene; AT3G25800.1; AT3G25800.1; AT3G25800. [Q38950-1]
DR Gramene; AT3G25800.3; AT3G25800.3; AT3G25800. [Q38950-1]
DR KEGG; ath:AT3G25800; -.
DR Araport; AT3G25800; -.
DR TAIR; locus:2085994; AT3G25800.
DR eggNOG; KOG0211; Eukaryota.
DR HOGENOM; CLU_015533_2_1_1; -.
DR InParanoid; Q38950; -.
DR OMA; SSLCMSW; -.
DR PhylomeDB; Q38950; -.
DR PRO; PR:Q38950; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q38950; baseline and differential.
DR Genevisible; Q38950; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IBA:GO_Central.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
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; IPR000357; HEAT.
DR InterPro; IPR021133; HEAT_type_2.
DR Pfam; PF02985; HEAT; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 13.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Nucleus; Peroxisome;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q38951"
FT CHAIN 2..587
FT /note="Serine/threonine-protein phosphatase 2A 65 kDa
FT regulatory subunit A beta isoform"
FT /id="PRO_0000071410"
FT REPEAT 2..42
FT /note="HEAT 1"
FT REPEAT 44..80
FT /note="HEAT 2"
FT REPEAT 81..119
FT /note="HEAT 3"
FT REPEAT 158..196
FT /note="HEAT 4"
FT REPEAT 197..235
FT /note="HEAT 5"
FT REPEAT 236..274
FT /note="HEAT 6"
FT REPEAT 275..313
FT /note="HEAT 7"
FT REPEAT 315..352
FT /note="HEAT 8"
FT REPEAT 353..391
FT /note="HEAT 9"
FT REPEAT 393..430
FT /note="HEAT 10"
FT REPEAT 432..469
FT /note="HEAT 11"
FT REPEAT 470..508
FT /note="HEAT 12"
FT REPEAT 509..547
FT /note="HEAT 13"
FT REPEAT 549..586
FT /note="HEAT 14"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q38951"
FT CONFLICT 319
FT /note="H -> D (in Ref. 1; CAA57528)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 587 AA; 65598 MW; DD754EE7E514CA7F CRC64;
MSMIDEPLYP IAVLIDELKN DDIQLRLNSI RRLSTIARAL GEERTRKELI PFLSENNDDD
DEVLLAMAEE LGVFIPYVGG VEYAHVLLPP LETLSTVEET CVREKAVESL CRVGSQMRES
DLVDHFISLV KRLAAGEWFT ARVSACGVFH IAYPSAPDML KTELRSLYTQ LCQDDMPMVR
RAAATNLGKF AATVESAHLK TDVMSMFEDL TQDDQDSVRL LAVEGCAALG KLLEPQDCVQ
HILPVIVNFS QDKSWRVRYM VANQLYELCE AVGPEPTRTE LVPAYVRLLR DNEAEVRIAA
AGKVTKFCRI LNPEIAIQHI LPCVKELSSD SSQHVRSALA SVIMGMAPVL GKDATIEHLL
PIFLSLLKDE FPDVRLNIIS KLDQVNQVIG IDLLSQSLLP AIVELAEDRH WRVRLAIIEY
IPLLASQLGV GFFDDKLGAL CMQWLQDKVH SIRDAAANNL KRLAEEFGPE WAMQHIVPQV
LEMVNNPHYL YRMTILRAVS LLAPVMGSEI TCSKLLPVVM TASKDRVPNI KFNVAKVLQS
LIPIVDQSVV EKTIRPGLVE LSEDPDVDVR FFANQALQSI DNVMMSS
