BRG3_ARATH
ID BRG3_ARATH Reviewed; 335 AA.
AC Q9LDD1; Q8L903;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Probable BOI-related E3 ubiquitin-protein ligase 3;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q9FHE4};
DE AltName: Full=RING-type E3 ubiquitin transferase BRG3 {ECO:0000305};
GN Name=BRG3; OrderedLocusNames=At3g12920; ORFNames=MGH6.3;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION, INDUCTION BY PATHOGEN; SALICYLIC ACID; GIBBERELLIC ACID;
RP 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 [7]
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: Probable E3 ubiquitin-protein ligase. Has no effect on the
CC stability of the DELLA proteins. {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:0000250|UniProtKB:Q9FHE4};
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 -!- INDUCTION: Down-regulated by pathogen, salicylic acid and 1-
CC aminocyclopropane-1-carboxylic acid (ACC). Up-regulated by salt,
CC gibberellic acid and methyl jasmonate. {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; AB026645; BAB02499.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75262.1; -; Genomic_DNA.
DR EMBL; AK118454; BAC43062.1; -; mRNA.
DR EMBL; BT006236; AAP12885.1; -; mRNA.
DR EMBL; AY088707; AAM67026.1; -; mRNA.
DR RefSeq; NP_566438.1; NM_112128.5.
DR AlphaFoldDB; Q9LDD1; -.
DR SMR; Q9LDD1; -.
DR BioGRID; 5811; 2.
DR STRING; 3702.AT3G12920.1; -.
DR iPTMnet; Q9LDD1; -.
DR PaxDb; Q9LDD1; -.
DR PRIDE; Q9LDD1; -.
DR ProteomicsDB; 240553; -.
DR EnsemblPlants; AT3G12920.1; AT3G12920.1; AT3G12920.
DR GeneID; 820477; -.
DR Gramene; AT3G12920.1; AT3G12920.1; AT3G12920.
DR KEGG; ath:AT3G12920; -.
DR Araport; AT3G12920; -.
DR TAIR; locus:2089225; AT3G12920.
DR eggNOG; KOG1100; Eukaryota.
DR HOGENOM; CLU_038018_3_1_1; -.
DR InParanoid; Q9LDD1; -.
DR OMA; HVERMRM; -.
DR OrthoDB; 1084167at2759; -.
DR PhylomeDB; Q9LDD1; -.
DR UniPathway; UPA00144; -.
DR PRO; PR:Q9LDD1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LDD1; baseline and differential.
DR Genevisible; Q9LDD1; AT.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
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 PIRSF; PIRSF036836; RNase_bind_SBP1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Plant defense; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..335
FT /note="Probable BOI-related E3 ubiquitin-protein ligase 3"
FT /id="PRO_0000424719"
FT ZN_FING 287..322
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 196..232
FT /note="WRD domain"
FT CONFLICT 25
FT /note="S -> N (in Ref. 5; AAM67026)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="R -> G (in Ref. 5; AAM67026)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="N -> K (in Ref. 5; AAM67026)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="C -> Y (in Ref. 5; AAM67026)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 335 AA; 37709 MW; C21C6D7820779237 CRC64;
MAVEAHHLNP LFSSNREMIH PVEASGVVYN TQMRYGTVPT FNPTVECQTS LFNPIYNISP
VDRLVHQSMK PTIQSVDSSL TFNSDNNVDF LRPVSSRKRS REESVVLNPS AYMQIQKNPT
DPLMFLGQDL SSNVQQHHFD IDRLISNHVE RMRMEIEEKR KTQGRRIVEA VEQGLMKTLR
AKDDEINHIG KLNLFLEEKV KSLCVENQIW RDVAQSNEAT VNALRSNLQQ VLAAVERNRW
EEPPTVADDA QSCCGSNDEG DSEEERWKLA GEAQDTKKMC RVGMSMCRSC GKGEASVLLL
PCRHMCLCSV CGSSLNTCPI CKSPKTASLH VNLSS
