RGA_ARATH
ID RGA_ARATH Reviewed; 587 AA.
AC Q9SLH3; O23642; O23725; Q941D4;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=DELLA protein RGA {ECO:0000303|PubMed:9490740};
DE AltName: Full=GAI-related sequence {ECO:0000303|PubMed:9389651};
DE AltName: Full=GRAS family protein 10;
DE Short=AtGRAS-10;
DE AltName: Full=Repressor on the ga1-3 mutant {ECO:0000303|PubMed:9389651};
DE AltName: Full=Restoration of growth on ammonia protein 1 {ECO:0000303|PubMed:9237632};
GN Name=RGA {ECO:0000303|PubMed:9490740};
GN Synonyms=GRS {ECO:0000303|PubMed:9389651},
GN RGA1 {ECO:0000303|PubMed:9237632};
GN OrderedLocusNames=At2g01570 {ECO:0000312|Araport:AT2G01570};
GN ORFNames=F2I9.19 {ECO:0000312|EMBL:AAC67333.1};
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], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=9237632; DOI=10.1016/s0014-5793(97)00590-5;
RA Truong H.-N., Caboche M., Daniel-Vedele F.;
RT "Sequence and characterization of two Arabidopsis thaliana cDNAs isolated
RT by functional complementation of a yeast gln3 gdh1 mutant.";
RL FEBS Lett. 410:213-218(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=9389651; DOI=10.1101/gad.11.23.3194;
RA Peng J., Carol P., Richards D.E., King K.E., Cowling R.J., Murphy G.P.,
RA Harberd N.P.;
RT "The Arabidopsis GAI gene defines a signaling pathway that negatively
RT regulates gibberellin responses.";
RL Genes Dev. 11:3194-3205(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
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 [5]
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP ASP-478.
RX PubMed=9490740; DOI=10.2307/3870695;
RA Silverstone A.L., Ciampaglio C.N., Sun T.-P.;
RT "The Arabidopsis RGA gene encodes a transcriptional regulator repressing
RT the gibberellin signal transduction pathway.";
RL Plant Cell 10:155-169(1998).
RN [7]
RP FUNCTION.
RX PubMed=11606551; DOI=10.1093/genetics/159.2.767;
RA King K.E., Moritz T., Harberd N.P.;
RT "Gibberellins are not required for normal stem growth in Arabidopsis
RT thaliana in the absence of GAI and RGA.";
RL Genetics 159:767-776(2001).
RN [8]
RP FUNCTION.
RX PubMed=11606552; DOI=10.1093/genetics/159.2.777;
RA Dill A., Sun T.-P.;
RT "Synergistic derepression of gibberellin signaling by removing RGA and GAI
RT function in Arabidopsis thaliana.";
RL Genetics 159:777-785(2001).
RN [9]
RP DOMAIN, AND MUTAGENESIS OF 44-ASP--ALA-60.
RX PubMed=11717468; DOI=10.1073/pnas.251534098;
RA Dill A., Jung H.-S., Sun T.-P.;
RT "The DELLA motif is essential for gibberellin-induced degradation of RGA.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:14162-14167(2001).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=11877383; DOI=10.1101/gad.969002;
RA Lee S., Cheng H., King K.E., Wang W., He Y., Hussain A., Lo J.,
RA Harberd N.P., Peng J.;
RT "Gibberellin regulates Arabidopsis seed germination via RGL2, a GAI/RGA-
RT like gene whose expression is up-regulated following imbibition.";
RL Genes Dev. 16:646-658(2002).
RN [11]
RP FUNCTION.
RX PubMed=12610625; DOI=10.1038/nature01387;
RA Fu X., Harberd N.P.;
RT "Auxin promotes Arabidopsis root growth by modulating gibberellin
RT response.";
RL Nature 421:740-743(2003).
RN [12]
RP DEGRADATION.
RX PubMed=12724538; DOI=10.1105/tpc.010827;
RA McGinnis K.M., Thomas S.G., Soule J.D., Strader L.C., Zale J.M., Sun T.-P.,
RA Steber C.M.;
RT "The Arabidopsis SLEEPY1 gene encodes a putative F-box subunit of an SCF E3
RT ubiquitin ligase.";
RL Plant Cell 15:1120-1130(2003).
RN [13]
RP FUNCTION.
RX PubMed=14615596; DOI=10.1105/tpc.015685;
RA Achard P., Vriezen W.H., Van Der Straeten D., Harberd N.P.;
RT "Ethylene regulates Arabidopsis development via the modulation of DELLA
RT protein growth repressor function.";
RL Plant Cell 15:2816-2825(2003).
RN [14]
RP FUNCTION.
RX PubMed=14973286; DOI=10.1242/dev.00992;
RA Cheng H., Qin L., Lee S., Fu X., Richards D.E., Cao D., Luo D.,
RA Harberd N.P., Peng J.;
RT "Gibberellin regulates Arabidopsis floral development via suppression of
RT DELLA protein function.";
RL Development 131:1055-1064(2004).
RN [15]
RP PROBABLE UBIQUITINATION, AND INTERACTION WITH GID2.
RX PubMed=15155881; DOI=10.1105/tpc.020958;
RA Dill A., Thomas S.G., Hu J., Steber C.M., Sun T.-P.;
RT "The Arabidopsis F-box protein SLEEPY1 targets gibberellin signaling
RT repressors for gibberellin-induced degradation.";
RL Plant Cell 16:1392-1405(2004).
RN [16]
RP INTERACTION WITH GID2, AND PHOSPHORYLATION.
RX PubMed=15161962; DOI=10.1105/tpc.021386;
RA Fu X., Richards D.E., Fleck B., Xie D., Burton N., Harberd N.P.;
RT "The Arabidopsis mutant sleepy1gar2-1 protein promotes plant growth by
RT increasing the affinity of the SCFSLY1 E3 ubiquitin ligase for DELLA
RT protein substrates.";
RL Plant Cell 16:1406-1418(2004).
RN [17]
RP INTERACTION WITH GID2.
RX PubMed=15173565; DOI=10.1104/pp.104.039578;
RA Tyler L., Thomas S.G., Hu J., Dill A., Alonso J.M., Ecker J.R., Sun T.-P.;
RT "Della proteins and gibberellin-regulated seed germination and floral
RT development in Arabidopsis.";
RL Plant Physiol. 135:1008-1019(2004).
RN [18]
RP FUNCTION.
RX PubMed=15128937; DOI=10.1073/pnas.0402377101;
RA Yu H., Ito T., Zhao Y., Peng J., Kumar P., Meyerowitz E.M.;
RT "Floral homeotic genes are targets of gibberellin signaling in flower
RT development.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7827-7832(2004).
RN [19]
RP FUNCTION.
RX PubMed=16034591; DOI=10.1007/s00425-005-0057-3;
RA Cao D., Hussain A., Cheng H., Peng J.;
RT "Loss of function of four DELLA genes leads to light- and gibberellin-
RT independent seed germination in Arabidopsis.";
RL Planta 223:105-113(2005).
RN [20]
RP MUTAGENESIS OF GLN-341.
RX PubMed=15734906; DOI=10.1104/pp.104.057646;
RA Muangprom A., Thomas S.-G., Sun T.-P., Osborn T.C.;
RT "A novel dwarfing mutation in a green revolution gene from Brassica rapa.";
RL Plant Physiol. 137:931-938(2005).
RN [21]
RP INTERACTION WITH GID1A; GID1B AND GID1C.
RX PubMed=16709201; DOI=10.1111/j.1365-313x.2006.02748.x;
RA Nakajima M., Shimada A., Takashi Y., Kim Y.C., Park S.H.,
RA Ueguchi-Tanaka M., Suzuki H., Katoh E., Iuchi S., Kobayashi M., Maeda T.,
RA Matsuoka M., Yamaguchi I.;
RT "Identification and characterization of Arabidopsis gibberellin
RT receptors.";
RL Plant J. 46:880-889(2006).
RN [22]
RP FUNCTION.
RX PubMed=17933900; DOI=10.1105/tpc.107.054999;
RA Zentella R., Zhang Z.L., Park M., Thomas S.G., Endo A., Murase K.,
RA Fleet C.M., Jikumaru Y., Nambara E., Kamiya Y., Sun T.P.;
RT "Global analysis of della direct targets in early gibberellin signaling in
RT Arabidopsis.";
RL Plant Cell 19:3037-3057(2007).
RN [23]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP PIF1; PIF4; PIF6 AND SPT.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=20093430; DOI=10.1093/molbev/msq012;
RA Gallego-Bartolome J., Minguet E.G., Marin J.A., Prat S., Blazquez M.A.,
RA Alabadi D.;
RT "Transcriptional diversification and functional conservation between DELLA
RT proteins in Arabidopsis.";
RL Mol. Biol. Evol. 27:1247-1256(2010).
RN [24]
RP INTERACTION WITH MYC2.
RX PubMed=22669881; DOI=10.1105/tpc.112.098749;
RA Hong G.J., Xue X.Y., Mao Y.B., Wang L.J., Chen X.Y.;
RT "Arabidopsis MYC2 interacts with DELLA proteins in regulating sesquiterpene
RT synthase gene expression.";
RL Plant Cell 24:2635-2648(2012).
RN [25]
RP INTERACTION WITH BOI; BRG1; BRG2 AND BRG3, AND DISRUPTION PHENOTYPE.
RX PubMed=23482857; DOI=10.1105/tpc.112.108951;
RA Park J., Nguyen K.T., Park E., Jeon J.S., Choi G.;
RT "DELLA proteins and their interacting RING Finger proteins repress
RT gibberellin responses by binding to the promoters of a subset of
RT gibberellin-responsive genes in Arabidopsis.";
RL Plant Cell 25:927-943(2013).
RN [26]
RP INTERACTION WITH NFYC9.
RX PubMed=25105952; DOI=10.1038/ncomms5601;
RA Hou X., Zhou J., Liu C., Liu L., Shen L., Yu H.;
RT "Nuclear factor Y-mediated H3K27me3 demethylation of the SOC1 locus
RT orchestrates flowering responses of Arabidopsis.";
RL Nat. Commun. 5:4601-4601(2014).
RN [27]
RP FUNCTION, INDUCTION BY IMBIBITION, AND INTERACTION WITH PDF2 AND ATML1.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=24989044; DOI=10.1105/tpc.114.127647;
RA Rombola-Caldentey B., Rueda-Romero P., Iglesias-Fernandez R., Carbonero P.,
RA Onate-Sanchez L.;
RT "Arabidopsis DELLA and two HD-ZIP transcription factors regulate GA
RT signaling in the epidermis through the L1 box cis-element.";
RL Plant Cell 26:2905-2919(2014).
RN [28]
RP INTERACTION WITH GAF1/IDD2 AND ENY/IDD1.
RC STRAIN=cv. Columbia;
RX PubMed=25035403; DOI=10.1105/tpc.114.125690;
RA Fukazawa J., Teramura H., Murakoshi S., Nasuno K., Nishida N., Ito T.,
RA Yoshida M., Kamiya Y., Yamaguchi S., Takahashi Y.;
RT "DELLAs function as coactivators of GAI-ASSOCIATED FACTOR1 in regulation of
RT gibberellin homeostasis and signaling in Arabidopsis.";
RL Plant Cell 26:2920-2938(2014).
RN [29]
RP INTERACTION WITH TOPP4, AND PHOSPHORYLATION.
RX PubMed=25010794; DOI=10.1371/journal.pgen.1004464;
RA Qin Q., Wang W., Guo X., Yue J., Huang Y., Xu X., Li J., Hou S.;
RT "Arabidopsis DELLA protein degradation is controlled by a type-one protein
RT phosphatase, TOPP4.";
RL PLoS Genet. 10:E1004464-E1004464(2014).
RN [30]
RP INTERACTION WITH MGP/IDD3; IDD4; IDD5; BIB/IDD9 AND JKD/IDD10, AND
RP SUBCELLULAR LOCATION.
RX PubMed=24821766; DOI=10.1073/pnas.1321669111;
RA Yoshida H., Hirano K., Sato T., Mitsuda N., Nomoto M., Maeo K., Koketsu E.,
RA Mitani R., Kawamura M., Ishiguro S., Tada Y., Ohme-Takagi M., Matsuoka M.,
RA Ueguchi-Tanaka M.;
RT "DELLA protein functions as a transcriptional activator through the DNA
RT binding of the indeterminate domain family proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:7861-7866(2014).
RN [31]
RP INTERACTION WITH FLZ5.
RX DOI=10.1016/j.cpb.2015.10.004;
RA Nietzsche M., Landgraf R., Tohge T., Boernke F.;
RT "A protein-protein interaction network linking the energy-sensor kinase
RT SnRK1 to multiple signaling pathways in Arabidopsis thaliana.";
RL Curr. Plant Biol. 5:36-44(2016).
RN [32]
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=28412546; DOI=10.1016/j.molp.2017.03.012;
RA Perea-Resa C., Rodriguez-Milla M.A., Iniesto E., Rubio V., Salinas J.;
RT "Prefoldins negatively regulate cold acclimation in Arabidopsis thaliana by
RT promoting nuclear proteasome-mediated HY5 degradation.";
RL Mol. Plant 10:791-804(2017).
RN [33]
RP O-FUCOSYLATION.
RX PubMed=28244988; DOI=10.1038/nchembio.2320;
RA Zentella R., Sui N., Barnhill B., Hsieh W.P., Hu J., Shabanowitz J.,
RA Boyce M., Olszewski N.E., Zhou P., Hunt D.F., Sun T.P.;
RT "The Arabidopsis O-fucosyltransferase SPINDLY activates nuclear growth
RT repressor DELLA.";
RL Nat. Chem. Biol. 13:479-485(2017).
CC -!- FUNCTION: Probable transcriptional regulator that acts as a repressor
CC of the gibberellin (GA) signaling pathway. Probably acts by
CC participating in large multiprotein complexes that repress
CC transcription of GA-inducible genes. Positively regulates XERICO
CC expression in seeds. Upon GA application, it is degraded by the
CC proteasome, allowing the GA signaling pathway. Compared to other DELLA
CC proteins, it is the most sensitive to GA application. No effect of the
CC BOI proteins on its stability. Its activity is probably regulated by
CC other phytohormones such as auxin and ethylene, attenuation of auxin
CC transport delaying its GA-induced degradation. Involved in the
CC regulation of seed dormancy and germination, including glucose-induced
CC delay of seed germination (PubMed:24989044).
CC {ECO:0000269|PubMed:11606551, ECO:0000269|PubMed:11606552,
CC ECO:0000269|PubMed:12610625, ECO:0000269|PubMed:14615596,
CC ECO:0000269|PubMed:14973286, ECO:0000269|PubMed:15128937,
CC ECO:0000269|PubMed:16034591, ECO:0000269|PubMed:17933900,
CC ECO:0000269|PubMed:20093430, ECO:0000269|PubMed:24989044,
CC ECO:0000269|PubMed:9490740}.
CC -!- SUBUNIT: Interacts directly with the GID2/SLY1 component of the
CC SCF(GID2) complex. Interacts (via N-terminus) with GID1A, GID1B and
CC GID1B (via N-terminus). Binds to bHLH transcription factors such as
CC MYC2, PIF1, PIF4, PIF6 and SPT. Interacts with the BOI proteins BOI,
CC BRG1, BRG2 and BRG3. Interacts with NFYC9 (PubMed:25105952). Interacts
CC with TOPP4 (PubMed:25010794). Interacts with FLZ5 (Ref.31). Binds to
CC zinc finger proteins MGP/IDD3, IDD4, IDD5, BIB/IDD9 and JKD/IDD10 in
CC the nucleus (PubMed:24821766). Binds to and coactivates GAF1/IDD2 and
CC ENY/IDD1 (PubMed:25035403). Binds to PDF2 and ATML1 (PubMed:24989044).
CC {ECO:0000269|PubMed:15155881, ECO:0000269|PubMed:15161962,
CC ECO:0000269|PubMed:15173565, ECO:0000269|PubMed:16709201,
CC ECO:0000269|PubMed:20093430, ECO:0000269|PubMed:22669881,
CC ECO:0000269|PubMed:23482857, ECO:0000269|PubMed:24821766,
CC ECO:0000269|PubMed:24989044, ECO:0000269|PubMed:25010794,
CC ECO:0000269|PubMed:25035403, ECO:0000269|PubMed:25105952,
CC ECO:0000269|Ref.31}.
CC -!- INTERACTION:
CC Q9SLH3; Q9ZWJ9: ARR2; NbExp=5; IntAct=EBI-963624, EBI-1101028;
CC Q9SLH3; Q9FMT4: At5g14170; NbExp=3; IntAct=EBI-963624, EBI-3387100;
CC Q9SLH3; A0A178VU28: AXX17_At2g44430; NbExp=3; IntAct=EBI-963624, EBI-25528007;
CC Q9SLH3; Q38897: BEL1; NbExp=3; IntAct=EBI-963624, EBI-1153783;
CC Q9SLH3; Q9FXG8: BLH10; NbExp=3; IntAct=EBI-963624, EBI-1153895;
CC Q9SLH3; Q94KL5: BLH4; NbExp=3; IntAct=EBI-963624, EBI-1153797;
CC Q9SLH3; Q8S307: BZR1; NbExp=8; IntAct=EBI-963624, EBI-1803261;
CC Q9SLH3; Q39057: CO; NbExp=3; IntAct=EBI-963624, EBI-1639724;
CC Q9SLH3; Q9MAA7: GID1A; NbExp=13; IntAct=EBI-963624, EBI-963597;
CC Q9SLH3; Q9LYC1: GID1B; NbExp=13; IntAct=EBI-963624, EBI-963686;
CC Q9SLH3; Q940G6: GID1C; NbExp=11; IntAct=EBI-963624, EBI-963794;
CC Q9SLH3; Q9STX3: GID2; NbExp=4; IntAct=EBI-963624, EBI-619033;
CC Q9SLH3; Q9SND4: HEC2; NbExp=4; IntAct=EBI-963624, EBI-1536720;
CC Q9SLH3; Q9SB60: IPT4; NbExp=3; IntAct=EBI-963624, EBI-25522816;
CC Q9SLH3; Q93WJ9: KAN1; NbExp=3; IntAct=EBI-963624, EBI-4426504;
CC Q9SLH3; Q9FFJ9: MJJ3.20; NbExp=3; IntAct=EBI-963624, EBI-15211238;
CC Q9SLH3; Q9C5C0: MPK18; NbExp=4; IntAct=EBI-963624, EBI-1238534;
CC Q9SLH3; Q9LUC3: MPK19; NbExp=3; IntAct=EBI-963624, EBI-25512843;
CC Q9SLH3; Q9SJG9: MPK20; NbExp=5; IntAct=EBI-963624, EBI-2358896;
CC Q9SLH3; O80536: PIF3; NbExp=6; IntAct=EBI-963624, EBI-625701;
CC Q9SLH3; Q8W2F3: PIF4; NbExp=4; IntAct=EBI-963624, EBI-625716;
CC Q9SLH3; Q9FHZ1: SCL23; NbExp=3; IntAct=EBI-963624, EBI-1238460;
CC Q9SLH3; Q9LPR8: SCL3; NbExp=3; IntAct=EBI-963624, EBI-4429250;
CC Q9SLH3; Q9S7W5: TCP13; NbExp=3; IntAct=EBI-963624, EBI-4424877;
CC Q9SLH3; Q93Z00: TCP14; NbExp=3; IntAct=EBI-963624, EBI-4424563;
CC Q9SLH3; Q9MAH8: TCP3; NbExp=3; IntAct=EBI-963624, EBI-25522447;
CC Q9SLH3; Q8W4J8: TIFY7; NbExp=4; IntAct=EBI-963624, EBI-1792583;
CC Q9SLH3; O04336: WRKY21; NbExp=3; IntAct=EBI-963624, EBI-1239118;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20093430,
CC ECO:0000269|PubMed:24821766, ECO:0000269|PubMed:28412546,
CC ECO:0000269|PubMed:9490740}. Note=Accumulates in the nucleus in
CC response to cold. {ECO:0000269|PubMed:28412546}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Expressed in roots, rosette
CC leaves, bolting and mature stems, young and mature siliques, flower
CC buds and influorescences. {ECO:0000269|PubMed:11877383,
CC ECO:0000269|PubMed:20093430, ECO:0000269|PubMed:9237632,
CC ECO:0000269|PubMed:9490740}.
CC -!- INDUCTION: Upon seed imbibition, increased GA levels in the epidermis
CC reduce DELLA proteins (e.g. GAI/RGA2, RGA/RGA1/GRS and RGL2/SCL19)
CC abundance and release, in turn, ATML1 and PDF2 which activate LIP1
CC expression, thus enhancing germination potential.
CC {ECO:0000269|PubMed:24989044}.
CC -!- DOMAIN: The DELLA motif is required for its GA-induced degradation but
CC not for the interaction with GID2. {ECO:0000269|PubMed:11717468}.
CC -!- PTM: Phosphorylated. Phosphorylation may increase the interaction with
CC GID2. {ECO:0000269|PubMed:15161962}.
CC -!- PTM: Gibberellin (GA) induces dephosphorylation of RGA by TOPP4 and
CC subsequent degradation by the proteasomal pathway.
CC {ECO:0000269|PubMed:25010794}.
CC -!- PTM: Ubiquitinated. Upon GA application it is ubiquitinated by the
CC SCF(GID2) complex, leading to its subsequent degradation.
CC -!- PTM: O-fucosylated by SPY (PubMed:28244988). O-fucosylation enhances
CC RGA activity by promoting RGA binding to key transcription factors in
CC brassinosteroid and light signaling pathways (PubMed:28244988).
CC {ECO:0000269|PubMed:28244988}.
CC -!- DISRUPTION PHENOTYPE: Rga, gai, rgl1, rgl2 and rgl3 pentuple mutant
CC displays constitutive GA responses even in the absence of GA treatment.
CC {ECO:0000269|PubMed:23482857}.
CC -!- SIMILARITY: Belongs to the GRAS family. DELLA subfamily. {ECO:0000305}.
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DR EMBL; Y11336; CAA72177.1; -; mRNA.
DR EMBL; Y15194; CAA75493.1; -; mRNA.
DR EMBL; AC005560; AAC67333.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05469.1; -; Genomic_DNA.
DR EMBL; AY052239; AAK97709.1; -; mRNA.
DR EMBL; AY054160; AAL06821.1; -; mRNA.
DR EMBL; BT010467; AAQ65090.1; -; mRNA.
DR PIR; D84426; D84426.
DR RefSeq; NP_178266.1; NM_126218.3.
DR AlphaFoldDB; Q9SLH3; -.
DR SMR; Q9SLH3; -.
DR BioGRID; 89; 83.
DR DIP; DIP-32983N; -.
DR IntAct; Q9SLH3; 51.
DR MINT; Q9SLH3; -.
DR STRING; 3702.AT2G01570.1; -.
DR iPTMnet; Q9SLH3; -.
DR PaxDb; Q9SLH3; -.
DR PRIDE; Q9SLH3; -.
DR ProteomicsDB; 236232; -.
DR EnsemblPlants; AT2G01570.1; AT2G01570.1; AT2G01570.
DR GeneID; 814686; -.
DR Gramene; AT2G01570.1; AT2G01570.1; AT2G01570.
DR KEGG; ath:AT2G01570; -.
DR Araport; AT2G01570; -.
DR TAIR; locus:2005516; AT2G01570.
DR eggNOG; ENOG502QPMG; Eukaryota.
DR HOGENOM; CLU_011924_4_0_1; -.
DR InParanoid; Q9SLH3; -.
DR OMA; CKLAQFA; -.
DR OrthoDB; 559310at2759; -.
DR PhylomeDB; Q9SLH3; -.
DR PRO; PR:Q9SLH3; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SLH3; baseline and differential.
DR Genevisible; Q9SLH3; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:TAIR.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:TAIR.
DR GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
DR GO; GO:0009740; P:gibberellic acid mediated signaling pathway; TAS:TAIR.
DR GO; GO:0042538; P:hyperosmotic salinity response; IBA:GO_Central.
DR GO; GO:0009867; P:jasmonic acid mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0033206; P:meiotic cytokinesis; IMP:TAIR.
DR GO; GO:1905614; P:negative regulation of developmental vegetative growth; IGI:CAFA.
DR GO; GO:0009938; P:negative regulation of gibberellic acid mediated signaling pathway; IGI:CAFA.
DR GO; GO:1905622; P:negative regulation of leaf development; IMP:CAFA.
DR GO; GO:0010187; P:negative regulation of seed germination; IBA:GO_Central.
DR GO; GO:1900033; P:negative regulation of trichome patterning; IMP:CAFA.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:CAFA.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0042176; P:regulation of protein catabolic process; IMP:TAIR.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IBA:GO_Central.
DR GO; GO:2000033; P:regulation of seed dormancy process; IEP:UniProtKB.
DR GO; GO:0010029; P:regulation of seed germination; IEP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0009737; P:response to abscisic acid; IBA:GO_Central.
DR GO; GO:0009409; P:response to cold; IDA:UniProtKB.
DR GO; GO:0009723; P:response to ethylene; IBA:GO_Central.
DR GO; GO:0010218; P:response to far red light; IEP:TAIR.
DR GO; GO:0009739; P:response to gibberellin; IMP:CAFA.
DR GO; GO:0009863; P:salicylic acid mediated signaling pathway; IBA:GO_Central.
DR Gene3D; 1.10.10.1290; -; 1.
DR InterPro; IPR038088; DELLA_N_sf.
DR InterPro; IPR030006; TF_DELLA.
DR InterPro; IPR021914; TF_DELLA_N.
DR InterPro; IPR005202; TF_GRAS.
DR PANTHER; PTHR31636; PTHR31636; 1.
DR PANTHER; PTHR31636:SF245; PTHR31636:SF245; 1.
DR Pfam; PF12041; DELLA; 1.
DR Pfam; PF03514; GRAS; 1.
DR PROSITE; PS50985; GRAS; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Gibberellin signaling pathway; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..587
FT /note="DELLA protein RGA"
FT /id="PRO_0000132234"
FT DOMAIN 212..581
FT /note="GRAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..273
FT /note="Leucine repeat I (LRI)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 292..357
FT /note="VHIID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 371..403
FT /note="Leucine repeat II (LRII)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 415..502
FT /note="PFYRE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 505..581
FT /note="SAW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT MOTIF 44..48
FT /note="DELLA motif"
FT MOTIF 66..70
FT /note="LEXLE motif"
FT MOTIF 89..93
FT /note="VHYNP motif"
FT MOTIF 323..327
FT /note="VHIID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT MOTIF 423..427
FT /note="LXXLL motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT COMPBIAS 11..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 44..60
FT /note="Missing: In rga-delta17; induces resistance to GA-
FT induced degradation but does not affect nuclear
FT localization."
FT /evidence="ECO:0000269|PubMed:11717468"
FT MUTAGEN 341
FT /note="Q->R: Causes a semidwarf phenotype by abolishing the
FT interaction with GID2 leading to prevent its degradation."
FT /evidence="ECO:0000269|PubMed:15734906"
FT MUTAGEN 478
FT /note="D->N: In rga-2; partially suppresses phenotypic
FT defects of GA-mutant ga1-3."
FT /evidence="ECO:0000269|PubMed:9490740"
FT CONFLICT 86
FT /note="T -> A (in Ref. 2; CAA75493)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="K -> E (in Ref. 2; CAA75493)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="G -> A (in Ref. 1; CAA72177 and 2; CAA75493)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="V -> D (in Ref. 5; AAK97709)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="I -> V (in Ref. 2; CAA75493)"
FT /evidence="ECO:0000305"
FT CONFLICT 587
FT /note="Y -> H (in Ref. 1; CAA72177)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 587 AA; 64035 MW; FC92E7F9408072AA CRC64;
MKRDHHQFQG RLSNHGTSSS SSSISKDKMM MVKKEEDGGG NMDDELLAVL GYKVRSSEMA
EVALKLEQLE TMMSNVQEDG LSHLATDTVH YNPSELYSWL DNMLSELNPP PLPASSNGLD
PVLPSPEICG FPASDYDLKV IPGNAIYQFP AIDSSSSSNN QNKRLKSCSS PDSMVTSTST
GTQIGGVIGT TVTTTTTTTT AAGESTRSVI LVDSQENGVR LVHALMACAE AIQQNNLTLA
EALVKQIGCL AVSQAGAMRK VATYFAEALA RRIYRLSPPQ NQIDHCLSDT LQMHFYETCP
YLKFAHFTAN QAILEAFEGK KRVHVIDFSM NQGLQWPALM QALALREGGP PTFRLTGIGP
PAPDNSDHLH EVGCKLAQLA EAIHVEFEYR GFVANSLADL DASMLELRPS DTEAVAVNSV
FELHKLLGRP GGIEKVLGVV KQIKPVIFTV VEQESNHNGP VFLDRFTESL HYYSTLFDSL
EGVPNSQDKV MSEVYLGKQI CNLVACEGPD RVERHETLSQ WGNRFGSSGL APAHLGSNAF
KQASMLLSVF NSGQGYRVEE SNGCLMLGWH TRPLITTSAW KLSTAAY
