2AAA_ARATH
ID 2AAA_ARATH Reviewed; 588 AA.
AC Q38845; Q38855; Q38952; Q56WI3; Q570B7;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 151.
DE RecName: Full=Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform;
DE Short=AtA alpha;
DE Short=PP2A, subunit A, alpha isoform;
DE Short=PR-65 A;
DE AltName: Full=Protein ROOTS CURL IN NAPHTHYLPHTHALAMIC ACID 1;
DE AltName: Full=Protein enhancer of ethylene-response 1;
GN Name=PP2AA1; Synonyms=EER1, RCN1, REGA; OrderedLocusNames=At1g25490;
GN ORFNames=F2J7.19;
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 [GENOMIC DNA].
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 [MRNA], AND FUNCTION.
RX PubMed=8641277; DOI=10.1002/j.1460-2075.1996.tb00565.x;
RA Garbers C., DeLong A., Deruere J., Bernasconi P., Soell D.;
RT "A mutation in protein phosphatase 2A regulatory subunit A affects auxin
RT transport in Arabidopsis.";
RL EMBO J. 15:2115-2124(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=8756607; DOI=10.1007/bf00021804;
RA Corum J.W. III, Hartung A.J., Stamey R.T., Rundle S.J.;
RT "Characterization of DNA sequences encoding a novel isoform of the 55 kDa B
RT regulatory subunit of the type 2A protein serine/threonine phosphatase of
RT Arabidopsis thaliana.";
RL Plant Mol. Biol. 31:419-427(1996).
RN [4]
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 [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 265-588.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP INTERACTION WITH PP2A SUBUNITS B AND C.
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 [9]
RP INTERACTION WITH CYP20-1/ROC7.
RX PubMed=10628867; DOI=10.1007/s004380051147;
RA Jackson K., Soell D.;
RT "Mutations in a new Arabidopsis cyclophilin disrupt its interaction with
RT protein phosphatase 2A.";
RL Mol. Gen. Genet. 262:830-838(1999).
RN [10]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=10607292; DOI=10.1046/j.1365-313x.1999.00607.x;
RA Deruere J., Jackson K., Garbers C., Soell D., Delong A.;
RT "The RCN1-encoded A subunit of protein phosphatase 2A increases phosphatase
RT activity in vivo.";
RL Plant J. 20:389-399(1999).
RN [11]
RP FUNCTION.
RX PubMed=11449059; DOI=10.2307/3871394;
RA Rashotte A.M., DeLong A., Muday G.K.;
RT "Genetic and chemical reductions in protein phosphatase activity alter
RT auxin transport, gravity response, and lateral root growth.";
RL Plant Cell 13:1683-1697(2001).
RN [12]
RP FUNCTION.
RX PubMed=11161061; DOI=10.1104/pp.125.2.1061;
RA Larsen P.B., Chang C.;
RT "The Arabidopsis eer1 mutant has enhanced ethylene responses in the
RT hypocotyl and stem.";
RL Plant Physiol. 125:1061-1073(2001).
RN [13]
RP INTERACTION WITH TON2.
RC STRAIN=cv. Columbia;
RX PubMed=11971138; DOI=10.1105/tpc.010402;
RA Camilleri C., Azimzadeh J., Pastuglia M., Bellini C., Grandjean O.,
RA Bouchez D.;
RT "The Arabidopsis TONNEAU2 gene encodes a putative novel protein phosphatase
RT 2A regulatory subunit essential for the control of the cortical
RT cytoskeleton.";
RL Plant Cell 14:833-845(2002).
RN [14]
RP FUNCTION.
RX PubMed=12417706; DOI=10.1105/tpc.003335;
RA Kwak J.M., Moon J.-H., Murata Y., Kuchitsu K., Leonhardt N., DeLong A.,
RA Schroeder J.I.;
RT "Disruption of a guard cell-expressed protein phosphatase 2A regulatory
RT subunit, RCN1, confers abscisic acid insensitivity in Arabidopsis.";
RL Plant Cell 14:2849-2861(2002).
RN [15]
RP FUNCTION.
RX PubMed=12787251; DOI=10.1046/j.1365-313x.2003.01762.x;
RA Larsen P.B., Cancel J.D.;
RT "Enhanced ethylene responsiveness in the Arabidopsis eer1 mutant results
RT from a loss-of-function mutation in the protein phosphatase 2A A regulatory
RT subunit, RCN1.";
RL Plant J. 34:709-718(2003).
RN [16]
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 [17]
RP INTERACTION WITH PHOSPHATIDIC ACID.
RX PubMed=15272872; DOI=10.1111/j.1365-313x.2004.02152.x;
RA Testerink C., Dekker H.L., Lim Z.-Y., Johns M.K., Holmes A.B.,
RA De Koster C.G., Ktistakis N.T., Munnik T.;
RT "Isolation and identification of phosphatidic acid targets from plants.";
RL Plant J. 39:527-536(2004).
RN [18]
RP INTERACTION WITH CHIP, AND PTM.
RX PubMed=16640601; DOI=10.1111/j.1365-313x.2006.02730.x;
RA Luo J., Shen G., Yan J., He C., Zhang H.;
RT "AtCHIP functions as an E3 ubiquitin ligase of protein phosphatase 2A
RT subunits and alters plant response to abscisic acid treatment.";
RL Plant J. 46:649-657(2006).
RN [19]
RP INTERACTION WITH B''ALPHA AND B''BETA.
RX PubMed=21478440; DOI=10.1105/tpc.110.074278;
RA Leivar P., Antolin-Llovera M., Ferrero S., Closa M., Arro M., Ferrer A.,
RA Boronat A., Campos N.;
RT "Multilevel control of Arabidopsis 3-hydroxy-3-methylglutaryl coenzyme A
RT reductase by protein phosphatase 2A.";
RL Plant Cell 23:1494-1511(2011).
RN [20]
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 [21]
RP FUNCTION.
RX PubMed=25085430; DOI=10.15252/embj.201488698;
RA Segonzac C., Macho A.P., Sanmartin M., Ntoukakis V., Sanchez-Serrano J.J.,
RA Zipfel C.;
RT "Negative control of BAK1 by protein phosphatase 2A during plant innate
RT immunity.";
RL EMBO J. 33:2069-2079(2014).
RN [22]
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. Seems to act as a positive
CC regulator of PP2A catalytic activity. Confers resistance to phosphatase
CC inhibitors such as okadaic acid and cantharidin. Involved during
CC developmental process such as seedling and floral developments, root
CC gravitropism, and stomatal opening regulation. Involved in the
CC regulation of auxin efflux, especially during basipetal (tips to base)
CC auxin transport in roots, and appears to contribute to the perception
CC of auxin efflux inhibitors such as 1-N-naphthylphthalamic acid (NPA)
CC and to semicarbazone I (substituted phenylsemicarbazone of 2-
CC acetylarylcarboxylic acids) (SCB-I). Modulates the magnitude of
CC ethylene response in the hypocotyl and stem, and functions as a general
CC positive transducer of early ABA signaling. The holoenzyme composed of
CC PP2AA1, PP2A4 and B'ZETA or B'ETA acts as negative regulator of plant
CC innate immunity by controlling BAK1 phosphorylation state and
CC activation in surface-localized immune receptor complexes
CC (PubMed:25085430). {ECO:0000269|PubMed:10607292,
CC ECO:0000269|PubMed:11161061, ECO:0000269|PubMed:11449059,
CC ECO:0000269|PubMed:12417706, ECO:0000269|PubMed:12787251,
CC ECO:0000269|PubMed:14973165, ECO:0000269|PubMed:25085430,
CC ECO:0000269|PubMed:8641277}.
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) and the regulatory
CC subunits TON2. Interacts with CYP20-1/ROC7. Also interacts with
CC phosphatidic acid (PA), a lipid signaling molecule. Interacts with
CC CHIP. Interacts with SIC/RON3 (PubMed:26888284).
CC {ECO:0000250|UniProtKB:P62714, ECO:0000269|PubMed:10091592,
CC ECO:0000269|PubMed:10628867, ECO:0000269|PubMed:11971138,
CC ECO:0000269|PubMed:15272872, ECO:0000269|PubMed:16640601,
CC ECO:0000269|PubMed:21478440, ECO:0000269|PubMed:26888284}.
CC -!- INTERACTION:
CC Q38845; Q9S7Z2: AFP4; NbExp=3; IntAct=EBI-1645478, EBI-1778843;
CC Q38845; Q9FLI3: AHG1; NbExp=3; IntAct=EBI-1645478, EBI-2363348;
CC Q38845; O80931: AS1; NbExp=3; IntAct=EBI-1645478, EBI-763232;
CC Q38845; Q8VZE5: At1g05410; NbExp=3; IntAct=EBI-1645478, EBI-4425726;
CC Q38845; F4I9J8: At1g51520; NbExp=3; IntAct=EBI-1645478, EBI-25521101;
CC Q38845; Q9SJ60: At2g35900; NbExp=3; IntAct=EBI-1645478, EBI-4456633;
CC Q38845; Q9LYL6: At3g56270; NbExp=3; IntAct=EBI-1645478, EBI-1238139;
CC Q38845; A0A384L7B9: At3g62550; NbExp=3; IntAct=EBI-1645478, EBI-25517258;
CC Q38845; A0A178U8H4: AXX17_At5g17430; NbExp=3; IntAct=EBI-1645478, EBI-25521064;
CC Q38845; Q8GZ13: BEE1; NbExp=3; IntAct=EBI-1645478, EBI-4440101;
CC Q38845; Q93VJ4: BEE2; NbExp=3; IntAct=EBI-1645478, EBI-4424312;
CC Q38845; Q9LEZ3: BIM1; NbExp=3; IntAct=EBI-1645478, EBI-617095;
CC Q38845; Q9SEZ7: CIPK16; NbExp=3; IntAct=EBI-1645478, EBI-1573415;
CC Q38845; Q9FJ55: CIPK19; NbExp=3; IntAct=EBI-1645478, EBI-16967606;
CC Q38845; Q2V452: CIPK3; NbExp=3; IntAct=EBI-1645478, EBI-1748724;
CC Q38845; Q9SU72: EDS1; NbExp=3; IntAct=EBI-1645478, EBI-1390454;
CC Q38845; Q9MAI5: ERF8; NbExp=3; IntAct=EBI-1645478, EBI-2000137;
CC Q38845; Q9C920: KDSB; NbExp=3; IntAct=EBI-1645478, EBI-25521209;
CC Q38845; Q9C5J9: LIP1; NbExp=4; IntAct=EBI-1645478, EBI-4449491;
CC Q38845; Q8LFL8: LSM1B; NbExp=3; IntAct=EBI-1645478, EBI-4434198;
CC Q38845; Q9LPZ1: MORF9; NbExp=3; IntAct=EBI-1645478, EBI-4424647;
CC Q38845; A0A1P8BA81: MTI20.21; NbExp=3; IntAct=EBI-1645478, EBI-25517523;
CC Q38845; Q8H133: PLP8; NbExp=3; IntAct=EBI-1645478, EBI-16967096;
CC Q38845; Q8S8E3: PYL6; NbExp=3; IntAct=EBI-1645478, EBI-2363192;
CC Q38845; Q84MC7: PYL9; NbExp=3; IntAct=EBI-1645478, EBI-2349513;
CC Q38845; Q93ZX1: RFC4; NbExp=3; IntAct=EBI-1645478, EBI-4470690;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:22404109}.
CC Nucleus {ECO:0000269|PubMed:22404109}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in cell-dividing tissues such as
CC apical meristems. Ubiquitous, with higher levels in roots and flowers
CC (at protein level). {ECO:0000269|PubMed:10607292,
CC ECO:0000269|PubMed:14973165, ECO:0000269|PubMed:8756607}.
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 -!- PTM: Ubiquitinated. CHIP-mediated ubiquitination enhances phosphatase
CC activity after an abiotic stress such as low temperature or darkness.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit A family.
CC {ECO:0000305}.
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DR EMBL; X82001; CAA57527.1; -; Genomic_DNA.
DR EMBL; U21557; AAC49255.1; -; mRNA.
DR EMBL; U27299; AAB60713.1; -; mRNA.
DR EMBL; AC079281; AAG50801.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30632.1; -; Genomic_DNA.
DR EMBL; AY120757; AAM53315.1; -; mRNA.
DR EMBL; BT000108; AAN15427.1; -; mRNA.
DR EMBL; AK220793; BAD94039.1; -; mRNA.
DR EMBL; AK222057; BAD94840.1; -; mRNA.
DR PIR; B86385; B86385.
DR PIR; S51807; S51807.
DR PIR; S69215; S69215.
DR RefSeq; NP_173920.1; NM_102360.4.
DR AlphaFoldDB; Q38845; -.
DR SMR; Q38845; -.
DR BioGRID; 24372; 106.
DR IntAct; Q38845; 61.
DR STRING; 3702.AT1G25490.1; -.
DR PaxDb; Q38845; -.
DR PRIDE; Q38845; -.
DR ProteomicsDB; 245086; -.
DR EnsemblPlants; AT1G25490.1; AT1G25490.1; AT1G25490.
DR GeneID; 839135; -.
DR Gramene; AT1G25490.1; AT1G25490.1; AT1G25490.
DR KEGG; ath:AT1G25490; -.
DR Araport; AT1G25490; -.
DR TAIR; locus:2031165; AT1G25490.
DR eggNOG; KOG0211; Eukaryota.
DR HOGENOM; CLU_015533_2_1_1; -.
DR InParanoid; Q38845; -.
DR OMA; FLIAEIM; -.
DR OrthoDB; 447572at2759; -.
DR PhylomeDB; Q38845; -.
DR PRO; PR:Q38845; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q38845; baseline and differential.
DR Genevisible; Q38845; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
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:1901149; F:salicylic acid binding; HDA:TAIR.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; TAS:TAIR.
DR GO; GO:0009926; P:auxin polar transport; IDA:TAIR.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009873; P:ethylene-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009789; P:positive regulation of abscisic acid-activated signaling pathway; IMP:TAIR.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0035304; P:regulation of protein dephosphorylation; IMP:TAIR.
DR GO; GO:0010119; P:regulation of stomatal movement; IMP:TAIR.
DR GO; GO:0009723; P:response to ethylene; IMP: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; 12.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Auxin signaling pathway; Cytoplasm;
KW Ethylene signaling pathway; Nucleus; Plant defense; Reference proteome;
KW Repeat; Ubl conjugation.
FT CHAIN 1..588
FT /note="Serine/threonine-protein phosphatase 2A 65 kDa
FT regulatory subunit A alpha isoform"
FT /id="PRO_0000071409"
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 CONFLICT 104
FT /note="E -> G (in Ref. 1; CAA57527)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="E -> K (in Ref. 1; CAA57527)"
FT /evidence="ECO:0000305"
FT CONFLICT 435
FT /note="D -> Y (in Ref. 1; CAA57527)"
FT /evidence="ECO:0000305"
FT CONFLICT 457
FT /note="A -> AAA (in Ref. 1; CAA57527 and 3; AAB60713)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 588 AA; 65494 MW; F27E294E85B8DAFA CRC64;
MAMVDEPLYP IAVLIDELKN DDIQLRLNSI RRLSTIARAL GEERTRKELI PFLSENSDDD
DEVLLAMAEE LGVFIPFVGG IEFAHVLLPP LESLCTVEET CVREKAVESL CKIGSQMKEN
DLVESFVPLV KRLAGGEWFA ARVSACGIFH VAYQGCTDVL KTELRATYSQ LCKDDMPMVR
RAAASNLGKF ATTVESTFLI AEIMTMFDDL TKDDQDSVRL LAVEGCAALG KLLEPQDCVA
RILPVIVNFS QDKSWRVRYM VANQLYELCE AVGPDCTRTD LVPAYVRLLR DNEAEVRIAA
AGKVTKFCRL LNPELAIQHI LPCVKELSSD SSQHVRSALA SVIMGMAPIL GKDSTIEHLL
PIFLSLLKDE FPDVRLNIIS KLDQVNQVIG IDLLSQSLLP AIVELAEDRH WRVRLAIIEY
VPLLASQLGI GFFDDKLGAL CMQWLQDKVY SIREAAANNL KRLAEEFGPE WAMQHLVPQV
LDMVNNPHYL HRMMVLRAIS LMAPVMGSEI TCSKFLPVVV EASKDRVPNI KFNVAKLLQS
LIPIVDQSVV DKTIRQCLVD LSEDPDVDVR YFANQALNSI DGSTAAQS
