BRG1_ARATH
ID BRG1_ARATH Reviewed; 294 AA.
AC Q9FHE4; Q3E8H0;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=BOI-related E3 ubiquitin-protein ligase 1;
DE EC=2.3.2.27 {ECO:0000269|PubMed:20921156};
DE AltName: Full=RING-type E3 ubiquitin transferase BRG1 {ECO:0000305};
GN Name=BRG1; OrderedLocusNames=At5g45100; ORFNames=K17O22.9;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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] (ISOFORM 1).
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, INDUCTION BY PATHOGEN; SALICYLIC ACID;
RP GIBBERELLIC ACID; ACC; METHYL JASMONATE AND SALT, AND DISRUPTION PHENOTYPE.
RX PubMed=20921156; DOI=10.1104/pp.110.163915;
RA Luo H., Laluk K., Lai Z., Veronese P., Song F., Mengiste T.;
RT "The Arabidopsis Botrytis Susceptible1 Interactor defines a subclass of
RT RING E3 ligases that regulate pathogen and stress responses.";
RL Plant Physiol. 154:1766-1782(2010).
RN [5]
RP FUNCTION, INTERACTION WITH GAI; RGA; RGL1; RGL2 AND RGL3, AND DISRUPTION
RP 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: E3 ubiquitin-protein ligase involved in regulation of abiotic
CC stress responses. Not involved in ubiquitination of MYB108/BOS1. Has no
CC effect on the stability of the DELLA proteins.
CC {ECO:0000269|PubMed:20921156, ECO:0000269|PubMed:23482857}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:20921156};
CC -!- PATHWAY: Protein degradation; proteasomal ubiquitin-dependent pathway.
CC -!- SUBUNIT: Interacts with the DELLA proteins GAI, RGA, RGL1, RGL2 and
CC RGL3. {ECO:0000269|PubMed:23482857}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FHE4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FHE4-2; Sequence=VSP_053490;
CC -!- INDUCTION: Up-regulated by salt and salicylic acid. Down-regulated by
CC gibberellic acid and methyl jasmonate. Not regulated by pathogen or 1-
CC aminocyclopropane-1-carboxylic acid (ACC).
CC {ECO:0000269|PubMed:20921156}.
CC -!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2
CC ubiquitin-conjugating enzyme. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Decreased resistance to
CC B.cinerea and increased cell death upon pathogen infection. Boi, brg1,
CC brg2 and brg3 quadruple mutant shows a higher GA signaling resulting in
CC a higher seed germination in the presence of paclobutrazol, precocious
CC juvenile-to-adult phase transition and early flowering.
CC {ECO:0000269|PubMed:20921156, ECO:0000269|PubMed:23482857}.
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DR EMBL; AB019224; BAB09495.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95201.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95202.1; -; Genomic_DNA.
DR EMBL; AY058839; AAL24227.1; -; mRNA.
DR EMBL; AY143844; AAN28783.1; -; mRNA.
DR RefSeq; NP_199323.2; NM_123878.3. [Q9FHE4-2]
DR RefSeq; NP_851134.1; NM_180803.2. [Q9FHE4-1]
DR AlphaFoldDB; Q9FHE4; -.
DR SMR; Q9FHE4; -.
DR BioGRID; 19792; 1.
DR STRING; 3702.AT5G45100.1; -.
DR PaxDb; Q9FHE4; -.
DR PRIDE; Q9FHE4; -.
DR ProteomicsDB; 240673; -. [Q9FHE4-1]
DR EnsemblPlants; AT5G45100.1; AT5G45100.1; AT5G45100. [Q9FHE4-1]
DR EnsemblPlants; AT5G45100.2; AT5G45100.2; AT5G45100. [Q9FHE4-2]
DR GeneID; 834543; -.
DR Gramene; AT5G45100.1; AT5G45100.1; AT5G45100. [Q9FHE4-1]
DR Gramene; AT5G45100.2; AT5G45100.2; AT5G45100. [Q9FHE4-2]
DR KEGG; ath:AT5G45100; -.
DR Araport; AT5G45100; -.
DR TAIR; locus:2153227; AT5G45100.
DR eggNOG; KOG1100; Eukaryota.
DR InParanoid; Q9FHE4; -.
DR OMA; QGNANIY; -.
DR OrthoDB; 889964at2759; -.
DR PhylomeDB; Q9FHE4; -.
DR UniPathway; UPA00144; -.
DR PRO; PR:Q9FHE4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FHE4; baseline and differential.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0043067; P:regulation of programmed cell death; IMP:TAIR.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR017066; E3ligase_BOI-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR42647; PTHR42647; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Metal-binding; Plant defense;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..294
FT /note="BOI-related E3 ubiquitin-protein ligase 1"
FT /id="PRO_0000424717"
FT ZN_FING 244..281
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 168..204
FT /note="WRD domain"
FT COILED 183..212
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..27
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_053490"
SQ SEQUENCE 294 AA; 32549 MW; 83081890E73D7B72 CRC64;
MAVEARHMNL FSSQYITNRE CVKSQTNMNN GQQIAGGGFP VTIGDRNLQY IDPINSFNKS
ESELTAISKR QRDSTFDSDA LIASQKRRAI AFSPASLIDA ELVSQIQQQN SEIDRFVAQQ
TETLRIELEA RQRTQTRMLA SAVQNAILKK LKAKDEEIIR MGKLNWVLQE RVKNLYVENQ
IWRDLAQTNE ATANNLRSNL EQVLAQVDDL DAFRRPLVEE ADDAESSCGS CDGGDVTAVV
NGGCKRCGEL TASVLVLPCR HLCLCTVCGS SALLRTCPVC DMVMTASVHV NMSS
