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Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform (AtA alpha) (PP2A, subunit A, alpha isoform) (PR-65 A) (Protein ROOTS CURL IN NAPHTHYLPHTHALAMIC ACID 1) (Protein enhancer of ethylene-response 1)

 2AAA_ARATH              Reviewed;         588 AA.
Q38845; Q38855; Q38952; Q56WI3; Q570B7;
06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
23-MAY-2018, entry version 132.
RecName: Full=Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform;
Short=AtA alpha;
Short=PP2A, subunit A, alpha isoform;
Short=PR-65 A;
AltName: Full=Protein ROOTS CURL IN NAPHTHYLPHTHALAMIC ACID 1;
AltName: Full=Protein enhancer of ethylene-response 1;
Name=PP2AA1; Synonyms=EER1, RCN1, REGA; OrderedLocusNames=At1g25490;
ORFNames=F2J7.19;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Landsberg erecta; TISSUE=Leaf;
PubMed=7811971; DOI=10.1007/BF00040694;
Slabas A.R., Fordham-Skelton A.P., Fletcher D., Martinez-Rivas J.M.,
Swinhoe R., Croy R.R.D., Evans I.M.;
"Characterisation of cDNA and genomic clones encoding homologues of
the 65 kDa regulatory subunit of protein phosphatase 2A in Arabidopsis
thaliana.";
Plant Mol. Biol. 26:1125-1138(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
PubMed=8641277;
Garbers C., DeLong A., Deruere J., Bernasconi P., Soell D.;
"A mutation in protein phosphatase 2A regulatory subunit A affects
auxin transport in Arabidopsis.";
EMBO J. 15:2115-2124(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=cv. Columbia;
PubMed=8756607; DOI=10.1007/BF00021804;
Corum J.W. III, Hartung A.J., Stamey R.T., Rundle S.J.;
"Characterization of DNA sequences encoding a novel isoform of the 55
kDa B regulatory subunit of the type 2A protein serine/threonine
phosphatase of Arabidopsis thaliana.";
Plant Mol. Biol. 31:419-427(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[5]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 265-588.
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[8]
INTERACTION WITH PP2A SUBUNITS B AND C.
PubMed=10091592; DOI=10.1046/j.1432-1327.1999.00154.x;
Haynes J.G., Hartung A.J., Hendershot J.D. III, Passingham R.S.,
Rundle S.J.;
"Molecular characterization of the B' regulatory subunit gene family
of Arabidopsis protein phosphatase 2A.";
Eur. J. Biochem. 260:127-136(1999).
[9]
INTERACTION WITH CYP20-1/ROC7.
PubMed=10628867; DOI=10.1007/s004380051147;
Jackson K., Soell D.;
"Mutations in a new Arabidopsis cyclophilin disrupt its interaction
with protein phosphatase 2A.";
Mol. Gen. Genet. 262:830-838(1999).
[10]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=10607292; DOI=10.1046/j.1365-313x.1999.00607.x;
Deruere J., Jackson K., Garbers C., Soell D., Delong A.;
"The RCN1-encoded A subunit of protein phosphatase 2A increases
phosphatase activity in vivo.";
Plant J. 20:389-399(1999).
[11]
FUNCTION.
PubMed=11449059; DOI=10.1105/tpc.13.7.1683;
Rashotte A.M., DeLong A., Muday G.K.;
"Genetic and chemical reductions in protein phosphatase activity alter
auxin transport, gravity response, and lateral root growth.";
Plant Cell 13:1683-1697(2001).
[12]
FUNCTION.
PubMed=11161061; DOI=10.1104/pp.125.2.1061;
Larsen P.B., Chang C.;
"The Arabidopsis eer1 mutant has enhanced ethylene responses in the
hypocotyl and stem.";
Plant Physiol. 125:1061-1073(2001).
[13]
INTERACTION WITH TON2.
STRAIN=cv. Columbia;
PubMed=11971138; DOI=10.1105/tpc.010402;
Camilleri C., Azimzadeh J., Pastuglia M., Bellini C., Grandjean O.,
Bouchez D.;
"The Arabidopsis TONNEAU2 gene encodes a putative novel protein
phosphatase 2A regulatory subunit essential for the control of the
cortical cytoskeleton.";
Plant Cell 14:833-845(2002).
[14]
FUNCTION.
PubMed=12417706; DOI=10.1105/tpc.003335;
Kwak J.M., Moon J.-H., Murata Y., Kuchitsu K., Leonhardt N.,
DeLong A., Schroeder J.I.;
"Disruption of a guard cell-expressed protein phosphatase 2A
regulatory subunit, RCN1, confers abscisic acid insensitivity in
Arabidopsis.";
Plant Cell 14:2849-2861(2002).
[15]
FUNCTION.
PubMed=12787251; DOI=10.1046/j.1365-313X.2003.01762.x;
Larsen P.B., Cancel J.D.;
"Enhanced ethylene responsiveness in the Arabidopsis eer1 mutant
results from a loss-of-function mutation in the protein phosphatase 2A
A regulatory subunit, RCN1.";
Plant J. 34:709-718(2003).
[16]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=14973165; DOI=10.1105/tpc.018994;
Zhou H.-W., Nussbaumer C., Chao Y., DeLong A.;
"Disparate roles for the regulatory A subunit isoforms in Arabidopsis
protein phosphatase 2A.";
Plant Cell 16:709-722(2004).
[17]
INTERACTION WITH PHOSPHATIDIC ACID.
PubMed=15272872; DOI=10.1111/j.1365-313X.2004.02152.x;
Testerink C., Dekker H.L., Lim Z.-Y., Johns M.K., Holmes A.B.,
De Koster C.G., Ktistakis N.T., Munnik T.;
"Isolation and identification of phosphatidic acid targets from
plants.";
Plant J. 39:527-536(2004).
[18]
INTERACTION WITH CHIP, AND PTM.
PubMed=16640601; DOI=10.1111/j.1365-313X.2006.02730.x;
Luo J., Shen G., Yan J., He C., Zhang H.;
"AtCHIP functions as an E3 ubiquitin ligase of protein phosphatase 2A
subunits and alters plant response to abscisic acid treatment.";
Plant J. 46:649-657(2006).
[19]
INTERACTION WITH B''ALPHA AND B''BETA.
PubMed=21478440; DOI=10.1105/tpc.110.074278;
Leivar P., Antolin-Llovera M., Ferrero S., Closa M., Arro M.,
Ferrer A., Boronat A., Campos N.;
"Multilevel control of Arabidopsis 3-hydroxy-3-methylglutaryl coenzyme
A reductase by protein phosphatase 2A.";
Plant Cell 23:1494-1511(2011).
[20]
SUBCELLULAR LOCATION.
PubMed=22404109; DOI=10.1111/j.1365-313X.2012.04984.x;
Tran H.T., Nimick M., Uhrig R.G., Templeton G., Morrice N.,
Gourlay R., DeLong A., Moorhead G.B.;
"Arabidopsis thaliana histone deacetylase 14 (HDA14) is an alpha-
tubulin deacetylase that associates with PP2A and enriches in the
microtubule fraction with the putative histone acetyltransferase
ELP3.";
Plant J. 71:263-272(2012).
[21]
FUNCTION.
PubMed=25085430; DOI=10.15252/embj.201488698;
Segonzac C., Macho A.P., Sanmartin M., Ntoukakis V.,
Sanchez-Serrano J.J., Zipfel C.;
"Negative control of BAK1 by protein phosphatase 2A during plant
innate immunity.";
EMBO J. 33:2069-2079(2014).
[22]
INTERACTION WITH SIC/RON3.
STRAIN=cv. Columbia, and cv. Landsberg erecta;
PubMed=26888284; DOI=10.1073/pnas.1501343112;
Karampelias M., Neyt P., De Groeve S., Aesaert S., Coussens G.,
Rolcik J., Bruno L., De Winne N., Van Minnebruggen A., Van Montagu M.,
Ponce M.R., Micol J.L., Friml J., De Jaeger G., Van Lijsebettens M.;
"ROTUNDA3 function in plant development by phosphatase 2A-mediated
regulation of auxin transporter recycling.";
Proc. Natl. Acad. Sci. U.S.A. 113:2768-2773(2016).
-!- FUNCTION: The A subunit of protein phosphatase 2A serves as a
scaffolding molecule to coordinate the assembly of the catalytic
subunit and a variable regulatory B subunit. Seems to act as a
positive regulator of PP2A catalytic activity. Confers resistance
to phosphatase inhibitors such as okadaic acid and cantharidin.
Involved during developmental process such as seedling and floral
developments, root gravitropism, and stomatal opening regulation.
Involved in the regulation of auxin efflux, especially during
basipetal (tips to base) auxin transport in roots, and appears to
contribute to the perception of auxin efflux inhibitors such as 1-
N-naphthylphthalamic acid (NPA) and to semicarbazone I
(substituted phenylsemicarbazone of 2-acetylarylcarboxylic acids)
(SCB-I). Modulates the magnitude of ethylene response in the
hypocotyl and stem, and functions as a general positive transducer
of early ABA signaling. The holoenzyme composed of PP2AA1, PP2A4
and B'ZETA or B'ETA acts as negative regulator of plant innate
immunity by controlling BAK1 phosphorylation state and activation
in surface-localized immune receptor complexes (PubMed:25085430).
{ECO:0000269|PubMed:10607292, ECO:0000269|PubMed:11161061,
ECO:0000269|PubMed:11449059, ECO:0000269|PubMed:12417706,
ECO:0000269|PubMed:12787251, ECO:0000269|PubMed:14973165,
ECO:0000269|PubMed:25085430, ECO:0000269|PubMed:8641277}.
-!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme,
composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa
constant regulatory subunit (subunit A), that associates with a
variety of regulatory subunits such as subunits B (the
R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families) and
the regulatory subunits TON2. Interacts with CYP20-1/ROC7. Also
interacts with phosphatidic acid (PA), a lipid signaling molecule.
Interacts with CHIP. Interacts with SIC/RON3 (PubMed:26888284).
{ECO:0000250|UniProtKB:P62714, ECO:0000269|PubMed:10091592,
ECO:0000269|PubMed:10628867, ECO:0000269|PubMed:11971138,
ECO:0000269|PubMed:15272872, ECO:0000269|PubMed:16640601,
ECO:0000269|PubMed:21478440, ECO:0000269|PubMed:26888284}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:22404109}. Nucleus
{ECO:0000269|PubMed:22404109}.
-!- TISSUE SPECIFICITY: Mostly expressed in cell-dividing tissues such
as apical meristems. Ubiquitous, with higher levels in roots and
flowers (at protein level). {ECO:0000269|PubMed:10607292,
ECO:0000269|PubMed:14973165, ECO:0000269|PubMed:8756607}.
-!- DOMAIN: Each HEAT repeat appears to consist of two alpha helices
joined by a hydrophilic region, the intrarepeat loop. The repeat
units may be arranged laterally to form a rod-like structure (By
similarity). {ECO:0000250}.
-!- PTM: Ubiquitinated. CHIP-mediated ubiquitination enhances
phosphatase activity after an abiotic stress such as low
temperature or darkness.
-!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit A
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X82001; CAA57527.1; -; Genomic_DNA.
EMBL; U21557; AAC49255.1; -; mRNA.
EMBL; U27299; AAB60713.1; -; mRNA.
EMBL; AC079281; AAG50801.1; -; Genomic_DNA.
EMBL; CP002684; AEE30632.1; -; Genomic_DNA.
EMBL; AY120757; AAM53315.1; -; mRNA.
EMBL; BT000108; AAN15427.1; -; mRNA.
EMBL; AK220793; BAD94039.1; -; mRNA.
EMBL; AK222057; BAD94840.1; -; mRNA.
PIR; B86385; B86385.
PIR; S51807; S51807.
PIR; S69215; S69215.
RefSeq; NP_173920.1; NM_102360.4.
UniGene; At.160; -.
ProteinModelPortal; Q38845; -.
SMR; Q38845; -.
BioGrid; 24372; 45.
IntAct; Q38845; 34.
STRING; 3702.AT1G25490.1; -.
PaxDb; Q38845; -.
PRIDE; Q38845; -.
EnsemblPlants; AT1G25490.1; AT1G25490.1; AT1G25490.
GeneID; 839135; -.
Gramene; AT1G25490.1; AT1G25490.1; AT1G25490.
KEGG; ath:AT1G25490; -.
Araport; AT1G25490; -.
TAIR; locus:2031165; AT1G25490.
eggNOG; KOG0211; Eukaryota.
eggNOG; ENOG410XQVI; LUCA.
HOGENOM; HOG000078539; -.
InParanoid; Q38845; -.
KO; K03456; -.
OMA; FLIAEIM; -.
OrthoDB; EOG093604ZV; -.
PhylomeDB; Q38845; -.
Reactome; R-ATH-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
Reactome; R-ATH-198753; ERK/MAPK targets.
Reactome; R-ATH-202670; ERKs are inactivated.
Reactome; R-ATH-69231; Cyclin D associated events in G1.
Reactome; R-ATH-69273; Cyclin A/B1/B2 associated events during G2/M transition.
Reactome; R-ATH-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
PRO; PR:Q38845; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q38845; baseline and differential.
Genevisible; Q38845; AT.
GO; GO:0005618; C:cell wall; IDA:TAIR.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0000159; C:protein phosphatase type 2A complex; TAS:TAIR.
GO; GO:0009738; P:abscisic acid-activated signaling pathway; TAS:TAIR.
GO; GO:0009926; P:auxin polar transport; IDA:TAIR.
GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
GO; GO:0009873; P:ethylene-activated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0009789; P:positive regulation of abscisic acid-activated signaling pathway; IMP:TAIR.
GO; GO:0035304; P:regulation of protein dephosphorylation; IMP:TAIR.
GO; GO:0010119; P:regulation of stomatal movement; IMP:TAIR.
GO; GO:0009723; P:response to ethylene; IMP:TAIR.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR000357; HEAT.
InterPro; IPR021133; HEAT_type_2.
Pfam; PF02985; HEAT; 1.
SUPFAM; SSF48371; SSF48371; 1.
PROSITE; PS50077; HEAT_REPEAT; 12.
1: Evidence at protein level;
Abscisic acid signaling pathway; Auxin signaling pathway;
Complete proteome; Cytoplasm; Ethylene signaling pathway; Nucleus;
Plant defense; Reference proteome; Repeat; Ubl conjugation.
CHAIN 1 588 Serine/threonine-protein phosphatase 2A
65 kDa regulatory subunit A alpha
isoform.
/FTId=PRO_0000071409.
REPEAT 2 42 HEAT 1.
REPEAT 44 80 HEAT 2.
REPEAT 81 119 HEAT 3.
REPEAT 158 196 HEAT 4.
REPEAT 197 235 HEAT 5.
REPEAT 236 274 HEAT 6.
REPEAT 275 313 HEAT 7.
REPEAT 315 352 HEAT 8.
REPEAT 353 391 HEAT 9.
REPEAT 393 430 HEAT 10.
REPEAT 432 469 HEAT 11.
REPEAT 470 508 HEAT 12.
REPEAT 509 547 HEAT 13.
REPEAT 549 586 HEAT 14.
CONFLICT 104 104 E -> G (in Ref. 1; CAA57527).
{ECO:0000305}.
CONFLICT 270 270 E -> K (in Ref. 1; CAA57527).
{ECO:0000305}.
CONFLICT 435 435 D -> Y (in Ref. 1; CAA57527).
{ECO:0000305}.
CONFLICT 457 457 A -> AAA (in Ref. 1; CAA57527 and 3;
AAB60713). {ECO:0000305}.
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


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