2AAG_ARATH
ID 2AAG_ARATH Reviewed; 587 AA.
AC Q38951; Q8LPH9; Q9FX65;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 25-MAY-2022, entry version 142.
DE RecName: Full=Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A gamma isoform;
DE Short=AtA gamma;
DE Short=PP2A, subunit A, gamma isoform;
GN Name=PP2AA3; Synonyms=DF2; OrderedLocusNames=At1g13320; ORFNames=T6J4.8;
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;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 80-587.
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 [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 TISSUE SPECIFICITY.
RX PubMed=16166256; DOI=10.1104/pp.105.063743;
RA Czechowski T., Stitt M., Altmann T., Udvardi M.K., Scheible W.R.;
RT "Genome-wide identification and testing of superior reference genes for
RT transcript normalization in Arabidopsis.";
RL Plant Physiol. 139:5-17(2005).
RN [7]
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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [9]
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 [10]
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).
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.
CC {ECO:0000269|PubMed:14973165}.
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 CHIP (PubMed:16640601). Interacts with SRK2E/OST1
CC (PubMed:26175513). {ECO:0000250|UniProtKB:P62714,
CC ECO:0000269|PubMed:16640601, ECO:0000269|PubMed:26175513}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:22404109}.
CC Nucleus {ECO:0000269|PubMed:22404109}.
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=Q38951-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously at stable levels. However,
CC higher protein levels in roots and flowers (at protein level).
CC {ECO:0000269|PubMed:14973165, ECO:0000269|PubMed:16166256}.
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 -!- MISCELLANEOUS: Due to the stability of its transcription,
CC PubMed:16166256 proposed this gene as a reference gene for transcript
CC normalization.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit A family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG09551.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC011810; AAG09551.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28998.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29000.1; -; Genomic_DNA.
DR EMBL; AY099760; AAM20611.1; -; mRNA.
DR EMBL; BT002601; AAO00961.1; -; mRNA.
DR EMBL; X82003; CAA57529.1; -; mRNA.
DR PIR; H86267; H86267.
DR PIR; S51809; S51809.
DR RefSeq; NP_001184981.1; NM_001198052.1. [Q38951-1]
DR RefSeq; NP_172790.2; NM_101203.5. [Q38951-1]
DR AlphaFoldDB; Q38951; -.
DR SMR; Q38951; -.
DR BioGRID; 23132; 46.
DR IntAct; Q38951; 5.
DR STRING; 3702.AT1G13320.3; -.
DR iPTMnet; Q38951; -.
DR PaxDb; Q38951; -.
DR PRIDE; Q38951; -.
DR ProteomicsDB; 245113; -. [Q38951-1]
DR EnsemblPlants; AT1G13320.1; AT1G13320.1; AT1G13320. [Q38951-1]
DR EnsemblPlants; AT1G13320.3; AT1G13320.3; AT1G13320. [Q38951-1]
DR GeneID; 837892; -.
DR Gramene; AT1G13320.1; AT1G13320.1; AT1G13320. [Q38951-1]
DR Gramene; AT1G13320.3; AT1G13320.3; AT1G13320. [Q38951-1]
DR KEGG; ath:AT1G13320; -.
DR Araport; AT1G13320; -.
DR TAIR; locus:2205354; AT1G13320.
DR eggNOG; KOG0211; Eukaryota.
DR InParanoid; Q38951; -.
DR OMA; EALVMIT; -.
DR OrthoDB; 447572at2759; -.
DR PhylomeDB; Q38951; -.
DR PRO; PR:Q38951; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q38951; baseline and differential.
DR Genevisible; Q38951; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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: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; IPR021133; HEAT_type_2.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 12.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Nucleus; Reference proteome;
KW Repeat; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..587
FT /note="Serine/threonine-protein phosphatase 2A 65 kDa
FT regulatory subunit A gamma isoform"
FT /id="PRO_0000071411"
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..194
FT /note="HEAT 4"
FT REPEAT 197..235
FT /note="HEAT 5"
FT REPEAT 236..274
FT /note="HEAT 6"
FT REPEAT 276..313
FT /note="HEAT 7"
FT REPEAT 314..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:0007744|PubMed:22223895"
FT CONFLICT 290
FT /note="C -> R (in Ref. 4; CAA57529)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 587 AA; 65517 MW; 741159FDEB9589B9 CRC64;
MSMVDEPLYP IAVLIDELKN DDIQRRLNSI KRLSIIARAL GEERTRKELI PFLSENNDDD
DEVLLAMAEE LGGFILYVGG VEYAYVLLPP LETLSTVEET CVREKAVDSL CRIGAQMRES
DLVEHFTPLA KRLSAGEWFT ARVSACGIFH IAYPSAPDVL KTELRSIYGQ LCQDDMPMVR
RAAATNLGKF AATIESAHLK TDIMSMFEDL TQDDQDSVRL LAVEGCAALG KLLEPQDCVA
HILPVIVNFS QDKSWRVRYM VANQLYELCE AVGPEPTRTD LVPAYARLLC DNEAEVRIAA
AGKVTKFCRI LNPELAIQHI LPCVKELSSD SSQHVRSALA SVIMGMAPVL GKDATIEHLL
PIFLSLLKDE FPDVRLNIIS KLDQVNQVIG IDLLSQSLLP AIVELAEDRH WRVRLAIIEY
IPLLASQLGV GFFDEKLGAL CMQWLQDKVH SIREAAANNL KRLAEEFGPE WAMQHIVPQV
LEMINNPHYL YRMTILRAVS LLAPVMGSEI TCSKLLPAVI TASKDRVPNI KFNVAKMMQS
LIPIVDQAVV ENMIRPCLVE LSEDPDVDVR YFANQALQSI DNVMMSS
