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 27-MAR-2024, entry version 144. 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; A0A178VU28: At2g46735; NbExp=3; IntAct=EBI-963665, EBI-25528007; CC Q8GXW1; Q9FMT4: At5g14170; NbExp=3; IntAct=EBI-963665, EBI-3387100; CC Q8GXW1; A0A178UG69: At5g25580; NbExp=3; IntAct=EBI-963665, EBI-25517434; 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; A0A1I9LL75: RNC4; NbExp=4; IntAct=EBI-963665, EBI-25511008; 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"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.Q8GXW1; -. DR PaxDb; 3702-AT3G03450-1; -. 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; AT3G03450; RGL2. DR eggNOG; ENOG502QPMG; Eukaryota. DR HOGENOM; CLU_011924_4_0_1; -. DR InParanoid; Q8GXW1; -. DR OMA; AQWRIRM; -. DR OrthoDB; 455942at2759; -. DR PhylomeDB; Q8GXW1; -. DR PRO; PR:Q8GXW1; -. DR Proteomes; UP000006548; Chromosome 3. DR ExpressionAtlas; Q8GXW1; baseline and differential. 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:0009938; P:negative regulation of gibberellic acid mediated signaling pathway; TAS:TAIR. DR GO; GO:0010187; P:negative regulation of seed germination; IMP:TAIR. 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:0009737; P:response to abscisic acid; IEP:TAIR. DR GO; GO:0009739; P:response to gibberellin; IEP:TAIR. DR Gene3D; 1.10.10.1290; Transcriptional regulator DELLA, N-terminal domain; 1. DR InterPro; IPR038088; DELLA_N_sf. DR InterPro; IPR021914; TF_DELLA_N. DR InterPro; IPR005202; TF_GRAS. DR PANTHER; PTHR31636:SF246; DELLA PROTEIN RGL2; 1. DR PANTHER; PTHR31636; OSJNBA0084A10.13 PROTEIN-RELATED; 1. DR Pfam; PF12041; DELLA; 1. DR Pfam; PF03514; GRAS; 1. DR SMART; SM01129; DELLA; 1. DR PROSITE; PS50985; GRAS; 1. DR Genevisible; Q8GXW1; AT. 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 //