RGL1_ARATH
ID RGL1_ARATH Reviewed; 511 AA.
AC Q9C8Y3; O65367;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 138.
DE RecName: Full=DELLA protein RGL1;
DE AltName: Full=GRAS family protein 9;
DE Short=AtGRAS-9;
DE AltName: Full=RGA-like protein 1;
DE Short=RGA-like protein;
GN Name=RGL1; Synonyms=RGAL; OrderedLocusNames=At1g66350; ORFNames=T27F4.10;
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 [GENOMIC DNA].
RA Sanchez-Fernandez R., Ardiles-Diaz W., Van Montagu M., Inze D., May M.J.;
RT "Cloning of a novel Arabidopsis thaliana RGA-like gene, a putative member
RT of the VHIID domain transcription factor family.";
RL J. Exp. Bot. 49:1609-1610(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, LACK OF
RP DEGRADATION, AND TISSUE SPECIFICITY.
RC TISSUE=Seedling;
RX PubMed=11826301; DOI=10.1105/tpc.010325;
RA Wen C.-K., Chang C.;
RT "Arabidopsis RGL1 encodes a negative regulator of gibberellin responses.";
RL Plant Cell 14:87-100(2002).
RN [3]
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 [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 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 [7]
RP FUNCTION.
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 [8]
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 [9]
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 [10]
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 [11]
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 [12]
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 [13]
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 [14]
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 [15]
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 [16]
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).
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. Has overlapping but distinct roles in GA signaling compared to
CC RGA and GAI. Regulates the floral development. May also participate in
CC seed germination and in ovule and anther development. Its activity is
CC probably regulated by other phytohormones such as auxin and ethylene.
CC {ECO:0000269|PubMed:11826301, 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}.
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). Interacts with the BOI proteins BOI, BRG1, BRG2
CC and BRG3. Binds to and coactivates GAF1/IDD2 and ENY/IDD1
CC (PubMed:25035403). {ECO:0000269|PubMed:15173565,
CC ECO:0000269|PubMed:16709201, ECO:0000269|PubMed:23482857,
CC ECO:0000269|PubMed:25035403}.
CC -!- INTERACTION:
CC Q9C8Y3; Q8S307: BZR1; NbExp=3; IntAct=EBI-963647, EBI-1803261;
CC Q9C8Y3; Q9MAA7: GID1A; NbExp=7; IntAct=EBI-963647, EBI-963597;
CC Q9C8Y3; Q9LYC1: GID1B; NbExp=6; IntAct=EBI-963647, EBI-963686;
CC Q9C8Y3; Q940G6: GID1C; NbExp=6; IntAct=EBI-963647, EBI-963794;
CC Q9C8Y3; Q38829: IAA11; NbExp=3; IntAct=EBI-963647, EBI-2367923;
CC Q9C8Y3; O24407: IAA16; NbExp=3; IntAct=EBI-963647, EBI-632231;
CC Q9C8Y3; P93830: IAA17; NbExp=3; IntAct=EBI-963647, EBI-632243;
CC Q9C8Y3; P49678: IAA2; NbExp=3; IntAct=EBI-963647, EBI-632343;
CC Q9C8Y3; Q38822: IAA3; NbExp=3; IntAct=EBI-963647, EBI-307174;
CC Q9C8Y3; P33077: IAA4; NbExp=3; IntAct=EBI-963647, EBI-632187;
CC Q9C8Y3; Q38825: IAA7; NbExp=3; IntAct=EBI-963647, EBI-602959;
CC Q9C8Y3; Q38826: IAA8; NbExp=3; IntAct=EBI-963647, EBI-632200;
CC Q9C8Y3; O48847: LUH; NbExp=3; IntAct=EBI-963647, EBI-3387563;
CC Q9C8Y3; Q9ZP59: TULP1; NbExp=3; IntAct=EBI-963647, EBI-4476686;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11826301}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in germinating seeds and
CC flowers and siliques. Highly expressed in inflorescences and weakly or
CC not expressed in rosette leaves, etiolated seedlings, siliques, mature
CC stems and roots. RGA and GAI transcripts were detected at slightly
CC varying levels in all tissues examined. RGL2 signal was undetected, and
CC RGL3 signal was very weak in all tissues examined (rosette leaves,
CC seedlings, inflorescences, and siliques) except inflorescences. In the
CC flower, it is expressed in developing ovules as well as in developing
CC anthers throughout microspore development.
CC {ECO:0000269|PubMed:11826301}.
CC -!- INDUCTION: Not up-regulated upon GA treatment.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- PTM: May be ubiquitinated, as suggested by its interaction with GID2.
CC Ubiquitination is however unsure since in contrast to other DELLA
CC proteins, it is not ubiquitinated and degraded upon GA application.
CC Nevertheless, ubiquitination may be triggered by other processes.
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}.
CC -!- CAUTION: According to PubMed:11877383, it is not involved in seed
CC germination. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA12242.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ224957; CAA12242.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY048749; AAL05911.1; -; mRNA.
DR EMBL; AC020665; AAG52171.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34499.1; -; Genomic_DNA.
DR EMBL; AY070035; AAL49792.1; -; mRNA.
DR EMBL; AY096506; AAM20156.1; -; mRNA.
DR PIR; G96688; G96688.
DR RefSeq; NP_176809.1; NM_105306.4.
DR AlphaFoldDB; Q9C8Y3; -.
DR SMR; Q9C8Y3; -.
DR BioGRID; 28174; 28.
DR DIP; DIP-37660N; -.
DR IntAct; Q9C8Y3; 22.
DR MINT; Q9C8Y3; -.
DR STRING; 3702.AT1G66350.1; -.
DR PaxDb; Q9C8Y3; -.
DR PRIDE; Q9C8Y3; -.
DR ProteomicsDB; 236885; -.
DR EnsemblPlants; AT1G66350.1; AT1G66350.1; AT1G66350.
DR GeneID; 842953; -.
DR Gramene; AT1G66350.1; AT1G66350.1; AT1G66350.
DR KEGG; ath:AT1G66350; -.
DR Araport; AT1G66350; -.
DR TAIR; locus:2201557; AT1G66350.
DR eggNOG; ENOG502QPMG; Eukaryota.
DR HOGENOM; CLU_011924_4_0_1; -.
DR InParanoid; Q9C8Y3; -.
DR OMA; KREHNHR; -.
DR OrthoDB; 559310at2759; -.
DR PhylomeDB; Q9C8Y3; -.
DR PRO; PR:Q9C8Y3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C8Y3; baseline and differential.
DR Genevisible; Q9C8Y3; 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; IBA:GO_Central.
DR GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; 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; IMP:TAIR.
DR GO; GO:0010187; P:negative regulation of seed germination; IBA:GO_Central.
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; IBA:GO_Central.
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: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; IPR030006; TF_DELLA.
DR InterPro; IPR021914; TF_DELLA_N.
DR InterPro; IPR005202; TF_GRAS.
DR PANTHER; PTHR31636; PTHR31636; 1.
DR PANTHER; PTHR31636:SF47; PTHR31636:SF47; 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; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..511
FT /note="DELLA protein RGL1"
FT /id="PRO_0000132236"
FT DOMAIN 143..506
FT /note="GRAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..204
FT /note="Leucine repeat I (LRI)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 223..288
FT /note="VHIID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 298..330
FT /note="Leucine repeat II (LRII)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 341..427
FT /note="PFYRE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 430..506
FT /note="SAW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT MOTIF 32..36
FT /note="DELLA motif"
FT MOTIF 54..58
FT /note="LEXLE motif"
FT MOTIF 73..77
FT /note="VHYNP motif"
FT MOTIF 157..161
FT /note="LxCxE motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT MOTIF 254..258
FT /note="VHIID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT MOTIF 349..353
FT /note="LXXLL motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT CONFLICT 129
FT /note="R -> E (in Ref. 1; CAA12242)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="L -> S (in Ref. 1; CAA12242)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 511 AA; 56754 MW; 1E60071697C92A9F CRC64;
MKREHNHRES SAGEGGSSSM TTVIKEEAAG VDELLVVLGY KVRSSDMADV AHKLEQLEMV
LGDGISNLSD ETVHYNPSDL SGWVESMLSD LDPTRIQEKP DSEYDLRAIP GSAVYPRDEH
VTRRSKRTRI ESELSSTRSV VVLDSQETGV RLVHALLACA EAVQQNNLKL ADALVKHVGL
LASSQAGAMR KVATYFAEGL ARRIYRIYPR DDVALSSFSD TLQIHFYESC PYLKFAHFTA
NQAILEVFAT AEKVHVIDLG LNHGLQWPAL IQALALRPNG PPDFRLTGIG YSLTDIQEVG
WKLGQLASTI GVNFEFKSIA LNNLSDLKPE MLDIRPGLES VAVNSVFELH RLLAHPGSID
KFLSTIKSIR PDIMTVVEQE ANHNGTVFLD RFTESLHYYS SLFDSLEGPP SQDRVMSELF
LGRQILNLVA CEGEDRVERH ETLNQWRNRF GLGGFKPVSI GSNAYKQASM LLALYAGADG
YNVEENEGCL LLGWQTRPLI ATSAWRINRV E
