RGL2_ARATH
ID RGL2_ARATH Reviewed; 547 AA.
AC Q8GXW1; Q9SRP9;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=DELLA protein RGL2 {ECO:0000303|PubMed:11877383};
DE AltName: Full=GRAS family protein 15;
DE Short=AtGRAS-15;
DE AltName: Full=RGA-like protein 2 {ECO:0000303|PubMed:11877383};
DE AltName: Full=Scarecrow-like protein 19 {ECO:0000303|PubMed:10341448};
DE Short=AtSCL19 {ECO:0000303|PubMed:10341448};
GN Name=RGL2 {ECO:0000303|PubMed:11877383};
GN Synonyms=SCL19 {ECO:0000303|PubMed:10341448};
GN OrderedLocusNames=At3g03450 {ECO:0000312|Araport:AT3G03450};
GN ORFNames=T21P5.13 {ECO:0000312|EMBL:AAF01590.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP IDENTIFICATION.
RX PubMed=10341448; DOI=10.1046/j.1365-313x.1999.00431.x;
RA Pysh L.D., Wysocka-Diller J.W., Camilleri C., Bouchez D., Benfey P.N.;
RT "The GRAS gene family in Arabidopsis: sequence characterization and basic
RT expression analysis of the SCARECROW-LIKE genes.";
RL Plant J. 18:111-119(1999).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
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 [6]
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 [7]
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 [8]
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 [9]
RP PROBABLE UBIQUITINATION, DEGRADATION, AND 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 [10]
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 [11]
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 [12]
RP PROBABLE UBIQUITINATION, DEGRADATION, PHOSPHORYLATION, AND MUTAGENESIS OF
RP 44-ASP--ALA-48; TYR-52; SER-57; SER-86; SER-103; SER-212; THR-271; THR-319;
RP SER-381; THR-411; SER-436; SER-437; SER-441; SER-456; THR-481; SER-501;
RP SER-508; THR-535 AND SER-542.
RX PubMed=16167898; DOI=10.1111/j.1365-313x.2005.02512.x;
RA Hussain A., Cao D., Cheng H., Wen Z., Peng J.;
RT "Identification of the conserved serine/threonine residues important for
RT gibberellin-sensitivity of Arabidopsis RGL2 protein.";
RL Plant J. 44:88-99(2005).
RN [13]
RP FUNCTION.
RX PubMed=17141619; DOI=10.1016/j.cub.2006.10.057;
RA Penfield S., Gilday A.D., Halliday K.J., Graham I.A.;
RT "DELLA-mediated cotyledon expansion breaks coat-imposed seed dormancy.";
RL Curr. Biol. 16:2366-2370(2006).
RN [14]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY GLUCOSE.
RX PubMed=16916886; DOI=10.1093/jxb/erl096;
RA Yuan K., Wysocka-Diller J.;
RT "Phytohormone signalling pathways interact with sugars during seed
RT germination and seedling development.";
RL J. Exp. Bot. 57:3359-3367(2006).
RN [15]
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 [16]
RP FUNCTION.
RX PubMed=16400150; DOI=10.1126/science.1118642;
RA Achard P., Cheng H., De Grauwe L., Decat J., Schoutteten H., Moritz T.,
RA Van Der Straeten D., Peng J., Harberd N.P.;
RT "Integration of plant responses to environmentally activated phytohormonal
RT signals.";
RL Science 311:91-94(2006).
RN [17]
RP FUNCTION, AND INDUCTION.
RX PubMed=17384169; DOI=10.1105/tpc.106.048009;
RA Ariizumi T., Steber C.M.;
RT "Seed germination of GA-insensitive sleepy1 mutants does not require RGL2
RT protein disappearance in Arabidopsis.";
RL Plant Cell 19:791-804(2007).
RN [18]
RP FUNCTION.
RX PubMed=17704233; DOI=10.1104/pp.107.104794;
RA Gan Y., Yu H., Peng J., Broun P.;
RT "Genetic and molecular regulation by DELLA proteins of trichome development
RT in Arabidopsis.";
RL Plant Physiol. 145:1031-1042(2007).
RN [19]
RP PHOSPHORYLATION OF TYR RESIDUES, AND MUTAGENESIS OF TYR-52; TYR-89;
RP TYR-223; TYR-259 AND TYR-435.
RX PubMed=17333251; DOI=10.1007/s00425-007-0497-z;
RA Hussain A., Cao D., Peng J.;
RT "Identification of conserved tyrosine residues important for gibberellin
RT sensitivity of Arabidopsis RGL2 protein.";
RL Planta 226:475-483(2007).
RN [20]
RP FUNCTION.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=18450451; DOI=10.1016/j.cub.2008.03.060;
RA Navarro L., Bari R., Achard P., Lison P., Nemri A., Harberd N.P.,
RA Jones J.D.G.;
RT "DELLAs control plant immune responses by modulating the balance of
RT jasmonic acid and salicylic acid signaling.";
RL Curr. Biol. 18:650-655(2008).
RN [21]
RP FUNCTION, AND INDUCTION BY SALT AND MANNITOL TREATMENT.
RX PubMed=18450450; DOI=10.1016/j.cub.2008.04.034;
RA Achard P., Renou J.-P., Berthome R., Harberd N.P., Genschik P.;
RT "Plant DELLAs restrain growth and promote survival of adversity by reducing
RT the levels of reactive oxygen species.";
RL Curr. Biol. 18:656-660(2008).
RN [22]
RP FUNCTION, INDUCTION BY ABA, AND TISSUE SPECIFICITY.
RX PubMed=18941053; DOI=10.1105/tpc.108.061515;
RA Piskurewicz U., Jikumaru Y., Kinoshita N., Nambara E., Kamiya Y.,
RA Lopez-Molina L.;
RT "The gibberellic acid signaling repressor RGL2 inhibits Arabidopsis seed
RT germination by stimulating abscisic acid synthesis and ABI5 activity.";
RL Plant Cell 20:2729-2745(2008).
RN [23]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY IMBIBITION.
RX PubMed=18162586; DOI=10.1104/pp.107.113738;
RA Toh S., Imamura A., Watanabe A., Nakabayashi K., Okamoto M., Jikumaru Y.,
RA Hanada A., Aso Y., Ishiyama K., Tamura N., Iuchi S., Kobayashi M.,
RA Yamaguchi S., Kamiya Y., Nambara E., Kawakami N.;
RT "High temperature-induced abscisic acid biosynthesis and its role in the
RT inhibition of gibberellin action in Arabidopsis seeds.";
RL Plant Physiol. 146:1368-1385(2008).
RN [24]
RP DEGRADATION BY PROTEASOME.
RX PubMed=19717618; DOI=10.1105/tpc.108.065433;
RA Wang F., Zhu D., Huang X., Li S., Gong Y., Yao Q., Fu X., Fan L.-M.,
RA Deng X.W.;
RT "Biochemical insights on degradation of Arabidopsis DELLA proteins gained
RT from a cell-free assay system.";
RL Plant Cell 21:2378-2390(2009).
RN [25]
RP TISSUE SPECIFICITY, AND INTERACTION WITH GID1A; GID1B AND GID1C.
RX PubMed=19500306; DOI=10.1111/j.1365-313x.2009.03936.x;
RA Suzuki H., Park S.-H., Okubo K., Kitamura J., Ueguchi-Tanaka M., Iuchi S.,
RA Katoh E., Kobayashi M., Yamaguchi I., Matsuoka M., Asami T., Nakajima M.;
RT "Differential expression and affinities of Arabidopsis gibberellin
RT receptors can explain variation in phenotypes of multiple knock-out
RT mutants.";
RL Plant J. 60:48-55(2009).
RN [26]
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 [27]
RP FUNCTION, INDUCTION DURING IMBIBITION, AND TISSUE SPECIFICITY.
RX PubMed=20956298; DOI=10.1073/pnas.1012896107;
RA Lee K.P., Piskurewicz U., Tureckova V., Strnad M., Lopez-Molina L.;
RT "A seed coat bedding assay shows that RGL2-dependent release of abscisic
RT acid by the endosperm controls embryo growth in Arabidopsis dormant
RT seeds.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:19108-19113(2010).
RN [28]
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 [29]
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 [30]
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 [31]
RP INTERACTION WITH TCP14 AND TCP15.
RX PubMed=25655823; DOI=10.1016/j.molp.2014.11.018;
RA Resentini F., Felipo-Benavent A., Colombo L., Blazquez M.A., Alabadi D.,
RA Masiero S.;
RT "TCP14 and TCP15 mediate the promotion of seed germination by gibberellins
RT in Arabidopsis thaliana.";
RL Mol. Plant 8:482-485(2015).
CC -!- FUNCTION: Probable transcriptional regulator that acts as a repressor
CC of the gibberellin (GA) signaling pathway. No effect of the BOI
CC proteins on its stability. Probably acts by participating in large
CC multiprotein complexes that repress transcription of GA-inducible
CC genes. Upon GA application, it is degraded by the proteasome, allowing
CC the GA signaling pathway. Acts as a major GA-response repressor of seed
CC germination, including seed thermoinhibition. Promotes the biosynthesis
CC of abscisic acid (ABA), especially in seed coats to maintain seed
CC dormancy. Delays flowering and adult leaf production. Also regulates
CC the floral development, petal, stamen and anther development, by
CC repressing the continued growth of floral organs. Its activity is
CC probably regulated by other phytohormones such as auxin and ethylene.
CC Involved in the regulation of seed dormancy and germination, including
CC glucose-induced delay of seed germination (PubMed:24989044). Promotes
CC salt tolerance. Acts as a repressor of positive regulators of trichome
CC initiation. Required during the flagellin-derived peptide flg22-
CC mediated growth inhibition. Contributes to the susceptibility to the
CC biotrophic pathogen P.syringae pv. tomato and to the resistance to the
CC necrotrophic pathogens B.cinerea A.brassicicola, probably by repressing
CC the SA-defense pathway and preventing cell death. Prevents stress-
CC induced reactive oxygen species (ROS) accumulation (e.g. salt stress)
CC by acting on the ROS scavenging system, and delays ROS-induced cell
CC death, thus promoting stress tolerance. {ECO:0000269|PubMed:11877383,
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:16400150,
CC ECO:0000269|PubMed:16916886, ECO:0000269|PubMed:17141619,
CC ECO:0000269|PubMed:17384169, ECO:0000269|PubMed:17704233,
CC ECO:0000269|PubMed:18162586, ECO:0000269|PubMed:18450450,
CC ECO:0000269|PubMed:18450451, ECO:0000269|PubMed:18941053,
CC ECO:0000269|PubMed:20093430, ECO:0000269|PubMed:20956298,
CC ECO:0000269|PubMed:24989044}.
CC -!- SUBUNIT: Interacts directly with the GID2/SLY1 component of the
CC SCF(GID2) complex. Interacts (via N-terminus) with GID1A, GID1B and
CC GID1C (via N-terminus). Binds to bHLH transcription factors such as
CC PIF1, PIF4, PIF6 and SPT. Interacts with the BOI proteins BOI, BRG1,
CC BRG2 and BRG3. Interacts with TCP14 and TCP15 (PubMed:25655823). Binds
CC to and coactivates GAF1/IDD2 and ENY/IDD1 (PubMed:25035403). Binds to
CC PDF2 and ATML1 (PubMed:24989044). {ECO:0000269|PubMed:15173565,
CC ECO:0000269|PubMed:16709201, ECO:0000269|PubMed:19500306,
CC ECO:0000269|PubMed:20093430, ECO:0000269|PubMed:23482857,
CC ECO:0000269|PubMed:24989044, ECO:0000269|PubMed:25035403,
CC ECO:0000269|PubMed:25655823}.
CC -!- INTERACTION:
CC Q8GXW1; A0A1I9LL75: At3g13740; NbExp=4; IntAct=EBI-963665, EBI-25511008;
CC Q8GXW1; Q9FMT4: At5g14170; NbExp=3; IntAct=EBI-963665, EBI-3387100;
CC Q8GXW1; A0A178UG69: At5g25580; NbExp=3; IntAct=EBI-963665, EBI-25517434;
CC Q8GXW1; A0A178VU28: AXX17_At2g44430; NbExp=3; IntAct=EBI-963665, EBI-25528007;
CC Q8GXW1; Q38897: BEL1; NbExp=3; IntAct=EBI-963665, EBI-1153783;
CC Q8GXW1; Q94KL5: BLH4; NbExp=3; IntAct=EBI-963665, EBI-1153797;
CC Q8GXW1; B9DGI8: BZIP63; NbExp=5; IntAct=EBI-963665, EBI-942713;
CC Q8GXW1; Q39055: CNX2; NbExp=3; IntAct=EBI-963665, EBI-4446408;
CC Q8GXW1; Q9SMN1: GAMMACAL2; NbExp=3; IntAct=EBI-963665, EBI-532001;
CC Q8GXW1; Q9MAA7: GID1A; NbExp=8; IntAct=EBI-963665, EBI-963597;
CC Q8GXW1; Q9LYC1: GID1B; NbExp=5; IntAct=EBI-963665, EBI-963686;
CC Q8GXW1; Q940G6: GID1C; NbExp=6; IntAct=EBI-963665, EBI-963794;
CC Q8GXW1; Q9SND4: HEC2; NbExp=3; IntAct=EBI-963665, EBI-1536720;
CC Q8GXW1; Q93WJ9: KAN1; NbExp=3; IntAct=EBI-963665, EBI-4426504;
CC Q8GXW1; P48000: KNAT3; NbExp=3; IntAct=EBI-963665, EBI-1153908;
CC Q8GXW1; Q9C5J9: LIP1; NbExp=3; IntAct=EBI-963665, EBI-4449491;
CC Q8GXW1; Q9FFJ9: MJJ3.20; NbExp=3; IntAct=EBI-963665, EBI-15211238;
CC Q8GXW1; Q9C5C0: MPK18; NbExp=3; IntAct=EBI-963665, EBI-1238534;
CC Q8GXW1; Q9SJG9: MPK20; NbExp=3; IntAct=EBI-963665, EBI-2358896;
CC Q8GXW1; Q9FX36: MYB54; NbExp=3; IntAct=EBI-963665, EBI-25511270;
CC Q8GXW1; Q8VYP8: MYJ24.12; NbExp=3; IntAct=EBI-963665, EBI-4442894;
CC Q8GXW1; Q42536: PORA; NbExp=5; IntAct=EBI-963665, EBI-4424685;
CC Q8GXW1; Q9LTI5: SCL11; NbExp=3; IntAct=EBI-963665, EBI-25517369;
CC Q8GXW1; B9DI20: SPL13A; NbExp=3; IntAct=EBI-963665, EBI-15206662;
CC Q8GXW1; Q9S7W5: TCP13; NbExp=3; IntAct=EBI-963665, EBI-4424877;
CC Q8GXW1; Q9LEZ9: TCP17; NbExp=3; IntAct=EBI-963665, EBI-15192327;
CC Q8GXW1; Q9LMA8: TIFY10A; NbExp=3; IntAct=EBI-963665, EBI-1388539;
CC Q8GXW1; Q8W4J8: TIFY7; NbExp=3; IntAct=EBI-963665, EBI-1792583;
CC Q8GXW1; Q0WQX9: WAVH2; NbExp=3; IntAct=EBI-963665, EBI-4426718;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20093430}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in germinating seeds,
CC flowers and siliques. Only detectable in the inflorescence, with high
CC levels in young flower buds and significant levels in siliques. In
CC imbibed seeds, it is restricted to seed coats, elongating regions of
CC pre-emergent and recently emerged radicles, endosperm (especially
CC micropylar endosperm), and embryonic axis. Not expressed in leaves,
CC bolting stems or roots. {ECO:0000269|PubMed:11877383,
CC ECO:0000269|PubMed:18941053, ECO:0000269|PubMed:19500306,
CC ECO:0000269|PubMed:20093430, ECO:0000269|PubMed:20956298}.
CC -!- INDUCTION: Up-regulated transiently following seed imbibition to
CC decline rapidly as germination proceeds; this induction is delayed at
CC supraoptimal temperature conditions (e.g. 34 degrees Celsius).
CC Accumulates in seed coats of dormant seeds where germination does not
CC occur after imbibition. Increased levels upon abscisic acid (ABA)
CC treatment. Down-regulated by norflurazon (NF), an ABA biosynthesis
CC inhibitor. Induced by stress such as glucose, salt or mannitol
CC treatment. 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 (PubMed:24989044).
CC {ECO:0000269|PubMed:11877383, ECO:0000269|PubMed:16916886,
CC ECO:0000269|PubMed:17384169, ECO:0000269|PubMed:18162586,
CC ECO:0000269|PubMed:18450450, ECO:0000269|PubMed:18941053,
CC ECO:0000269|PubMed:20956298, ECO:0000269|PubMed:24989044}.
CC -!- DOMAIN: The DELLA motif is required for its GA-induced degradation but
CC not for the interaction with GID2.
CC -!- PTM: Phosphorylated. Phosphorylation on Tyr residues is required for
CC proteasome-mediated degradation in response to gibberellic acid (GA).
CC Dephosphorylation may be prerequisite for its degradation by the
CC proteasome. {ECO:0000269|PubMed:16167898, ECO:0000269|PubMed:17333251}.
CC -!- PTM: Ubiquitinated (Probable). Upon GA application or seed imbibation,
CC it is ubiquitinated by the SCF(GID2) complex, leading to its subsequent
CC degradation. {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Higher germination rate in the presence of
CC glucose and at supraoptimal temperature conditions. Rga, gai, rgl1,
CC rgl2 and rgl3 pentuple mutant displays constitutive GA responses even
CC in the absence of GA treatment. {ECO:0000269|PubMed:16916886,
CC ECO:0000269|PubMed:18162586, ECO:0000269|PubMed:23482857}.
CC -!- SIMILARITY: Belongs to the GRAS family. DELLA subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Kiss of life - Issue 137 of
CC April 2012;
CC URL="https://web.expasy.org/spotlight/back_issues/137";
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DR EMBL; AC009895; AAF01590.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73945.1; -; Genomic_DNA.
DR EMBL; AK118009; BAC42642.1; -; mRNA.
DR RefSeq; NP_186995.1; NM_111216.3.
DR AlphaFoldDB; Q8GXW1; -.
DR SMR; Q8GXW1; -.
DR BioGRID; 6584; 48.
DR DIP; DIP-37661N; -.
DR IntAct; Q8GXW1; 36.
DR STRING; 3702.AT3G03450.1; -.
DR PaxDb; Q8GXW1; -.
DR PRIDE; Q8GXW1; -.
DR EnsemblPlants; AT3G03450.1; AT3G03450.1; AT3G03450.
DR GeneID; 821251; -.
DR Gramene; AT3G03450.1; AT3G03450.1; AT3G03450.
DR KEGG; ath:AT3G03450; -.
DR Araport; AT3G03450; -.
DR TAIR; locus:2099624; AT3G03450.
DR eggNOG; ENOG502QPMG; Eukaryota.
DR HOGENOM; CLU_011924_4_0_1; -.
DR InParanoid; Q8GXW1; -.
DR OMA; VQQENFA; -.
DR OrthoDB; 559310at2759; -.
DR PhylomeDB; Q8GXW1; -.
DR PRO; PR:Q8GXW1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8GXW1; baseline and differential.
DR Genevisible; Q8GXW1; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:TAIR.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
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:0009938; P:negative regulation of gibberellic acid mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0010187; P:negative regulation of seed germination; 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; IEP:TAIR.
DR GO; GO:0009723; P:response to ethylene; IBA:GO_Central.
DR GO; GO:0009739; P:response to gibberellin; IEP:TAIR.
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; IPR021914; TF_DELLA_N.
DR InterPro; IPR005202; TF_GRAS.
DR PANTHER; PTHR31636; PTHR31636; 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; Differentiation; Flowering;
KW Gibberellin signaling pathway; Nucleus; Phosphoprotein; Plant defense;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..547
FT /note="DELLA protein RGL2"
FT /id="PRO_0000132237"
FT DOMAIN 171..545
FT /note="GRAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..236
FT /note="Leucine repeat I (LRI)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 255..320
FT /note="VHIID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 334..366
FT /note="Leucine repeat II (LRII)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 377..466
FT /note="PFYRE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 469..545
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 87..91
FT /note="VHYNP motif"
FT MOTIF 286..290
FT /note="VHIID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT MOTIF 385..389
FT /note="LXXLL motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT COMPBIAS 25..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 44..48
FT /note="Missing: Resistant to GA-mediated degradation."
FT /evidence="ECO:0000269|PubMed:16167898"
FT MUTAGEN 52
FT /note="Y->A,E: Resistant to GA-mediated degradation."
FT /evidence="ECO:0000269|PubMed:16167898,
FT ECO:0000269|PubMed:17333251"
FT MUTAGEN 52
FT /note="Y->F: No effect on GA-mediated degradation."
FT /evidence="ECO:0000269|PubMed:16167898,
FT ECO:0000269|PubMed:17333251"
FT MUTAGEN 57
FT /note="S->D: No effect on GA-mediated degradation."
FT /evidence="ECO:0000269|PubMed:16167898"
FT MUTAGEN 86
FT /note="S->D: No effect on GA-mediated degradation."
FT /evidence="ECO:0000269|PubMed:16167898"
FT MUTAGEN 89
FT /note="Y->A,E: Resistant to GA-mediated degradation."
FT /evidence="ECO:0000269|PubMed:17333251"
FT MUTAGEN 89
FT /note="Y->F: No effect on GA-mediated degradation."
FT /evidence="ECO:0000269|PubMed:17333251"
FT MUTAGEN 103
FT /note="S->D: No effect on GA-mediated degradation."
FT /evidence="ECO:0000269|PubMed:16167898"
FT MUTAGEN 212
FT /note="S->D: No effect on GA-mediated degradation."
FT /evidence="ECO:0000269|PubMed:16167898"
FT MUTAGEN 223
FT /note="Y->A,E: Resistant to GA-mediated degradation."
FT /evidence="ECO:0000269|PubMed:17333251"
FT MUTAGEN 223
FT /note="Y->F: No effect on GA-mediated degradation."
FT /evidence="ECO:0000269|PubMed:17333251"
FT MUTAGEN 259
FT /note="Y->A: Partially resistant to GA-mediated
FT degradation."
FT /evidence="ECO:0000269|PubMed:17333251"
FT MUTAGEN 271
FT /note="T->C: Partially resistant to GA-mediated
FT degradation."
FT /evidence="ECO:0000269|PubMed:16167898"
FT MUTAGEN 271
FT /note="T->E: Null mutant; resistant to GA-mediated
FT degradation."
FT /evidence="ECO:0000269|PubMed:16167898"
FT MUTAGEN 319
FT /note="T->C: No effect on GA-mediated degradation."
FT /evidence="ECO:0000269|PubMed:16167898"
FT MUTAGEN 319
FT /note="T->E: Resistant to GA-mediated degradation."
FT /evidence="ECO:0000269|PubMed:16167898"
FT MUTAGEN 381
FT /note="S->D: No effect on GA-mediated degradation."
FT /evidence="ECO:0000269|PubMed:16167898"
FT MUTAGEN 411
FT /note="T->C: No effect on GA-mediated degradation."
FT /evidence="ECO:0000269|PubMed:16167898"
FT MUTAGEN 411
FT /note="T->E: Resistant to GA-mediated degradation."
FT /evidence="ECO:0000269|PubMed:16167898"
FT MUTAGEN 435
FT /note="Y->A,E: Resistant to GA-mediated degradation."
FT /evidence="ECO:0000269|PubMed:17333251"
FT MUTAGEN 435
FT /note="Y->F: No effect on GA-mediated degradation."
FT /evidence="ECO:0000269|PubMed:17333251"
FT MUTAGEN 436
FT /note="S->D: No effect on GA-mediated degradation."
FT /evidence="ECO:0000269|PubMed:16167898"
FT MUTAGEN 437
FT /note="S->D: No effect on GA-mediated degradation."
FT /evidence="ECO:0000269|PubMed:16167898"
FT MUTAGEN 441
FT /note="S->C: No effect on GA-mediated degradation."
FT /evidence="ECO:0000269|PubMed:16167898"
FT MUTAGEN 441
FT /note="S->D: Resistant to GA-mediated degradation."
FT /evidence="ECO:0000269|PubMed:16167898"
FT MUTAGEN 456
FT /note="S->D: No effect on GA-mediated degradation."
FT /evidence="ECO:0000269|PubMed:16167898"
FT MUTAGEN 481
FT /note="T->E: No effect on GA-mediated degradation."
FT /evidence="ECO:0000269|PubMed:16167898"
FT MUTAGEN 501
FT /note="S->D: No effect on GA-mediated degradation."
FT /evidence="ECO:0000269|PubMed:16167898"
FT MUTAGEN 508
FT /note="S->D: No effect on GA-mediated degradation."
FT /evidence="ECO:0000269|PubMed:16167898"
FT MUTAGEN 535
FT /note="T->C: No effect on GA-mediated degradation."
FT /evidence="ECO:0000269|PubMed:16167898"
FT MUTAGEN 535
FT /note="T->E: Resistant to GA-mediated degradation."
FT /evidence="ECO:0000269|PubMed:16167898"
FT MUTAGEN 542
FT /note="S->C: No effect on GA-mediated degradation."
FT /evidence="ECO:0000269|PubMed:16167898"
FT MUTAGEN 542
FT /note="S->D: Resistant to GA-mediated degradation."
FT /evidence="ECO:0000269|PubMed:16167898"
FT CONFLICT 210
FT /note="A -> T (in Ref. 3; BAC42642)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 547 AA; 60494 MW; C4D18D5951D95634 CRC64;
MKRGYGETWD PPPKPLPASR SGEGPSMADK KKADDDNNNS NMDDELLAVL GYKVRSSEMA
EVAQKLEQLE MVLSNDDVGS TVLNDSVHYN PSDLSNWVES MLSELNNPAS SDLDTTRSCV
DRSEYDLRAI PGLSAFPKEE EVFDEEASSK RIRLGSWCES SDESTRSVVL VDSQETGVRL
VHALVACAEA IHQENLNLAD ALVKRVGTLA GSQAGAMGKV ATYFAQALAR RIYRDYTAET
DVCAAVNPSF EEVLEMHFYE SCPYLKFAHF TANQAILEAV TTARRVHVID LGLNQGMQWP
ALMQALALRP GGPPSFRLTG IGPPQTENSD SLQQLGWKLA QFAQNMGVEF EFKGLAAESL
SDLEPEMFET RPESETLVVN SVFELHRLLA RSGSIEKLLN TVKAIKPSIV TVVEQEANHN
GIVFLDRFNE ALHYYSSLFD SLEDSYSLPS QDRVMSEVYL GRQILNVVAA EGSDRVERHE
TAAQWRIRMK SAGFDPIHLG SSAFKQASML LSLYATGDGY RVEENDGCLM IGWQTRPLIT
TSAWKLA
