RGL3_ARATH
ID RGL3_ARATH Reviewed; 523 AA.
AC Q9LF53;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=DELLA protein RGL3;
DE AltName: Full=GRAS family protein 27;
DE Short=AtGRAS-27;
DE AltName: Full=RGA-like protein 3;
GN Name=RGL3; OrderedLocusNames=At5g17490; ORFNames=K3M16.60;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 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 [5]
RP TISSUE SPECIFICITY.
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 [6]
RP IDENTIFICATION.
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 [7]
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 [8]
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 [9]
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 [10]
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 [11]
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).
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. Its activity may be regulated by phytohormones such as auxin and
CC ethylene (By similarity). {ECO:0000250, ECO:0000269|PubMed:12610625,
CC ECO:0000269|PubMed:14615596}.
CC -!- SUBUNIT: Interacts directly with the GID2/SLY1 component of the
CC SCF(GID2) complex, suggesting that it may be ubiquitinated. Interacts
CC (via N-terminus) with GID1A, GID1B and GID1B (via N-terminus).
CC Interacts with the BOI proteins BOI, BRG1, BRG2 and BRG3.
CC {ECO:0000269|PubMed:15173565, ECO:0000269|PubMed:16709201,
CC ECO:0000269|PubMed:23482857}.
CC -!- INTERACTION:
CC Q9LF53; Q9FMT4: At5g14170; NbExp=3; IntAct=EBI-15681313, EBI-3387100;
CC Q9LF53; Q94C60: At5g63670; NbExp=3; IntAct=EBI-15681313, EBI-25522213;
CC Q9LF53; A0A384KCR9: AXX17_At3g07670; NbExp=4; IntAct=EBI-15681313, EBI-25511181;
CC Q9LF53; A0A384KCV6: AXX17_At3g40470; NbExp=4; IntAct=EBI-15681313, EBI-25511108;
CC Q9LF53; A0A178UH48: AXX17_At5g15360; NbExp=3; IntAct=EBI-15681313, EBI-25522309;
CC Q9LF53; B9DGI8: BZIP63; NbExp=3; IntAct=EBI-15681313, EBI-942713;
CC Q9LF53; Q84JC2: DOGL4; NbExp=3; IntAct=EBI-15681313, EBI-1238377;
CC Q9LF53; Q9MAA7: GID1A; NbExp=5; IntAct=EBI-15681313, EBI-963597;
CC Q9LF53; Q9LYC1: GID1B; NbExp=4; IntAct=EBI-15681313, EBI-963686;
CC Q9LF53; Q940G6: GID1C; NbExp=4; IntAct=EBI-15681313, EBI-963794;
CC Q9LF53; Q8LF89: GRXC8; NbExp=3; IntAct=EBI-15681313, EBI-4434651;
CC Q9LF53; Q93WJ9: KAN1; NbExp=3; IntAct=EBI-15681313, EBI-4426504;
CC Q9LF53; Q9FFJ9: MJJ3.20; NbExp=3; IntAct=EBI-15681313, EBI-15211238;
CC Q9LF53; Q84JZ6: MORF3; NbExp=3; IntAct=EBI-15681313, EBI-4465639;
CC Q9LF53; Q9LPZ1: MORF9; NbExp=3; IntAct=EBI-15681313, EBI-4424647;
CC Q9LF53; Q9FX36: MYB54; NbExp=3; IntAct=EBI-15681313, EBI-25511270;
CC Q9LF53; Q38899: ORC2; NbExp=3; IntAct=EBI-15681313, EBI-2114089;
CC Q9LF53; Q9SZC9: PAA1; NbExp=3; IntAct=EBI-15681313, EBI-4441998;
CC Q9LF53; Q9ZNT7: PHB2; NbExp=3; IntAct=EBI-15681313, EBI-531812;
CC Q9LF53; Q9S7W5: TCP13; NbExp=3; IntAct=EBI-15681313, EBI-4424877;
CC Q9LF53; Q9LEZ9: TCP17; NbExp=3; IntAct=EBI-15681313, EBI-15192327;
CC Q9LF53; Q8W4J8: TIFY7; NbExp=3; IntAct=EBI-15681313, EBI-1792583;
CC Q9LF53; Q5CCK4: VAL2; NbExp=3; IntAct=EBI-15681313, EBI-15193683;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed at very low level. Mainly expressed in
CC germinating seeds and flowers and siliques. Not expressed in other
CC tissues. {ECO:0000269|PubMed:11826301}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- PTM: May be ubiquitinated. {ECO:0000250}.
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; AL391150; CAC01893.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92433.1; -; Genomic_DNA.
DR EMBL; AK117226; BAC41902.1; -; mRNA.
DR EMBL; BT005905; AAO64840.1; -; mRNA.
DR PIR; T51475; T51475.
DR RefSeq; NP_197251.1; NM_121755.3.
DR AlphaFoldDB; Q9LF53; -.
DR SMR; Q9LF53; -.
DR BioGRID; 16891; 48.
DR DIP; DIP-60636N; -.
DR IntAct; Q9LF53; 29.
DR STRING; 3702.AT5G17490.1; -.
DR PaxDb; Q9LF53; -.
DR PRIDE; Q9LF53; -.
DR ProteomicsDB; 236970; -.
DR EnsemblPlants; AT5G17490.1; AT5G17490.1; AT5G17490.
DR GeneID; 831615; -.
DR Gramene; AT5G17490.1; AT5G17490.1; AT5G17490.
DR KEGG; ath:AT5G17490; -.
DR Araport; AT5G17490; -.
DR TAIR; locus:2157477; AT5G17490.
DR eggNOG; ENOG502QPMG; Eukaryota.
DR HOGENOM; CLU_011924_4_0_1; -.
DR InParanoid; Q9LF53; -.
DR OMA; RRIYRIH; -.
DR OrthoDB; 559310at2759; -.
DR PhylomeDB; Q9LF53; -.
DR PRO; PR:Q9LF53; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LF53; baseline and differential.
DR Genevisible; Q9LF53; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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: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; 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; 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; Gibberellin signaling pathway; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..523
FT /note="DELLA protein RGL3"
FT /id="PRO_0000132238"
FT DOMAIN 148..516
FT /note="GRAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..209
FT /note="Leucine repeat I (LRI)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 228..293
FT /note="VHIID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 305..337
FT /note="Leucine repeat II (LRII)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 348..437
FT /note="PFYRE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 440..516
FT /note="SAW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT MOTIF 34..38
FT /note="DELLA motif"
FT MOTIF 56..60
FT /note="LEXLE motif"
FT MOTIF 78..82
FT /note="VHYNP motif"
FT MOTIF 259..263
FT /note="VHIID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT MOTIF 356..360
FT /note="LXXLL motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 523 AA; 57327 MW; 0F6CE0BD13403C35 CRC64;
MKRSHQETSV EEEAPSMVEK LENGCGGGGD DNMDEFLAVL GYKVRSSDMA DVAQKLEQLE
MVLSNDIASS SNAFNDTVHY NPSDLSGWAQ SMLSDLNYYP DLDPNRICDL RPITDDDECC
SSNSNSNKRI RLGPWCDSVT SESTRSVVLI EETGVRLVQA LVACAEAVQL ENLSLADALV
KRVGLLAASQ AGAMGKVATY FAEALARRIY RIHPSAAAID PSFEEILQMN FYDSCPYLKF
AHFTANQAIL EAVTTSRVVH VIDLGLNQGM QWPALMQALA LRPGGPPSFR LTGVGNPSNR
EGIQELGWKL AQLAQAIGVE FKFNGLTTER LSDLEPDMFE TRTESETLVV NSVFELHPVL
SQPGSIEKLL ATVKAVKPGL VTVVEQEANH NGDVFLDRFN EALHYYSSLF DSLEDGVVIP
SQDRVMSEVY LGRQILNLVA TEGSDRIERH ETLAQWRKRM GSAGFDPVNL GSDAFKQASL
LLALSGGGDG YRVEENDGSL MLAWQTKPLI AASAWKLAAE LRR
