ID   RGA1_BRACM              Reviewed;         573 AA.
AC   Q5BN23;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=DELLA protein RGA1;
DE   AltName: Full=BrRGA1;
DE   AltName: Full=RGA-like protein 1;
GN   Name=RGA1;
OS   Brassica campestris (Field mustard).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3711;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND MUTAGENESIS OF GLN-328.
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).
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. Upon GA application, it is
CC       degraded by the proteasome, allowing the GA signaling pathway.
CC       {ECO:0000269|PubMed:15734906}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- DOMAIN: The DELLA motif is required for its GA-induced degradation.
CC       {ECO:0000250}.
CC   -!- PTM: Phosphorylated. {ECO:0000250}.
CC   -!- PTM: Ubiquitinated. Upon GA application it is ubiquitinated, leading to
CC       its subsequent degradation (Probable). {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the GRAS family. DELLA subfamily. {ECO:0000305}.
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DR   EMBL; AY928549; AAX33297.1; -; Genomic_DNA.
DR   RefSeq; XP_009101333.1; XM_009103085.2.
DR   AlphaFoldDB; Q5BN23; -.
DR   SMR; Q5BN23; -.
DR   STRING; 3711.Bra024875.1-P; -.
DR   EnsemblPlants; Bra024875.1; Bra024875.1-P; Bra024875.
DR   GeneID; 103827572; -.
DR   Gramene; Bra024875.1; Bra024875.1-P; Bra024875.
DR   KEGG; brp:103827572; -.
DR   OMA; SQWRNRF; -.
DR   OrthoDB; 559310at2759; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
DR   GO; GO:0009740; P:gibberellic acid mediated signaling pathway; IEA:UniProtKB-KW.
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   Gibberellin signaling pathway; Nucleus; Phosphoprotein; Repressor;
KW   Transcription; Transcription regulation; Ubl conjugation.
FT   CHAIN           1..573
FT                   /note="DELLA protein RGA1"
FT                   /id="PRO_0000132239"
FT   DOMAIN          199..568
FT                   /note="GRAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          158..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          206..260
FT                   /note="Leucine repeat I (LRI)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT   REGION          279..344
FT                   /note="VHIID"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT   REGION          358..390
FT                   /note="Leucine repeat II (LRII)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT   REGION          402..489
FT                   /note="PFYRE"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT   REGION          492..568
FT                   /note="SAW"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT   MOTIF           42..46
FT                   /note="DELLA motif"
FT   MOTIF           310..314
FT                   /note="VHIID"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT   MOTIF           410..414
FT                   /note="LXXLL motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT   COMPBIAS        9..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         328
FT                   /note="Q->R: In brrga1-1; causes a dwarf phenotype due to
FT                   its inability to be degraded."
FT                   /evidence="ECO:0000269|PubMed:15734906"
SQ   SEQUENCE   573 AA;  62512 MW;  8BD94B58039D7730 CRC64;
     MKRDLHQFQG PNHGTSIAGS STSSPAVFGK DKMMMVKEEE DDELLGVLGY KVRSSEMAEV
     ALKLEQLETM MGNAQEDGLA HLATDTVHYN PAELYSWLDN MLTELNPPAA TTGSNALNPE
     INNNNNNNSF FTGGDLKAIP GNAVCRRSNQ FAFAVDSSSN KRLKPSSSPD SMVTSPSPAG
     VIGTTVTTVT ESTRPLILVD SQDNGVRLVH ALMACAEAVQ SSNLTLAEAL VKQIGFLAVS
     QAGAMRKVAT YFAEALARRI YRLSPPQTQI DHSLSDTLQM HFYETCPYLK FAHFTANQAI
     LEAFEGKKRV HVIDFSMNQG LQWPALMQAL ALREGGPPSF RLTGIGPPAA DNSDHLHEVG
     CKLAQLAEAI HVEFEYRGFV ANSLADLDAS MLELRPSETE AVAVNSVFEL HKLLGRTGGI
     EKVFGVVKQI KPVIFTVVEQ ESNHNGPVFL DRFTESLHYY STLFDSLEGA PSSQDKVMSE
     VYLGKQICNL VACEGPDRVE RHETLSQWSN RFGSSGFAPA HLGSNAFKQA STLLALFNGG
     EGYRVEENNG CLMLSWHTRP LITTSAWKLS AVH