BRG2_ARATH
ID BRG2_ARATH Reviewed; 358 AA.
AC F4IDI6; F4IDI7; O64540; Q0WLS3; Q0WLZ6; Q8LAY3;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Probable BOI-related E3 ubiquitin-protein ligase 2;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q9FHE4};
DE AltName: Full=RING-type E3 ubiquitin transferase BRG2 {ECO:0000305};
GN Name=BRG2; OrderedLocusNames=At1g79110; ORFNames=YUP8H12R.27;
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=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 [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).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4IDI6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4IDI6-2; Sequence=VSP_053491;
CC -!- INDUCTION: Down-regulated by pathogen and salicylic acid. Up-regulated
CC by salt, gibberellic acid and methyl jasmonate. Not regulated by 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC17064.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC002986; AAC17064.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE36205.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36206.1; -; Genomic_DNA.
DR EMBL; AY087533; AAM65075.1; -; mRNA.
DR EMBL; AK229952; BAF01778.1; -; mRNA.
DR EMBL; AK230118; BAF01934.1; -; mRNA.
DR EMBL; AK230039; BAF01861.1; -; mRNA.
DR PIR; T01044; T01044.
DR RefSeq; NP_565200.1; NM_106562.2. [F4IDI6-1]
DR RefSeq; NP_974174.1; NM_202445.3. [F4IDI6-2]
DR AlphaFoldDB; F4IDI6; -.
DR BioGRID; 29471; 1.
DR STRING; 3702.AT1G79110.1; -.
DR PaxDb; F4IDI6; -.
DR PRIDE; F4IDI6; -.
DR EnsemblPlants; AT1G79110.1; AT1G79110.1; AT1G79110. [F4IDI6-1]
DR EnsemblPlants; AT1G79110.2; AT1G79110.2; AT1G79110. [F4IDI6-2]
DR GeneID; 844252; -.
DR Gramene; AT1G79110.1; AT1G79110.1; AT1G79110. [F4IDI6-1]
DR Gramene; AT1G79110.2; AT1G79110.2; AT1G79110. [F4IDI6-2]
DR KEGG; ath:AT1G79110; -.
DR Araport; AT1G79110; -.
DR TAIR; locus:2207385; AT1G79110.
DR eggNOG; KOG1100; Eukaryota.
DR HOGENOM; CLU_038018_3_1_1; -.
DR InParanoid; F4IDI6; -.
DR OrthoDB; 1084167at2759; -.
DR UniPathway; UPA00144; -.
DR PRO; PR:F4IDI6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4IDI6; baseline and differential.
DR Genevisible; F4IDI6; AT.
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 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..358
FT /note="Probable BOI-related E3 ubiquitin-protein ligase 2"
FT /id="PRO_0000424718"
FT ZN_FING 310..345
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 214..250
FT /note="WRD domain"
FT COILED 171..234
FT /evidence="ECO:0000255"
FT VAR_SEQ 164..166
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_053491"
FT CONFLICT 51
FT /note="V -> A (in Ref. 4; BAF01778/BAF01934)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="V -> M (in Ref. 3; AAM65075)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="L -> P (in Ref. 3; AAM65075)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="R -> G (in Ref. 4; BAF01861)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 358 AA; 40085 MW; 070236A5B4D8F673 CRC64;
MAVDAHHLFL SPPQLFSNRE LTMNNNTMEP TSGGFCNNNQ TGYGVVSPFS VPNHTSTTTT
ATPPLLHVYG GSDTIPTTAG YYADGATNLD CEFFPLPTRK RSRDSSRSNY HHLLLQNPRS
SSCVNAATTT TTTTLFSFLG QDIDISSHMN QQQHEIDRFV SLHLYQMERV KYEIEEKRKR
QARTIMEAIE QGLVKRLRVK EEERERIGKV NHALEERVKS LSIENQIWRD LAQTNEATAN
HLRTNLEHVL AQVKDVSRGA GLEKNMNEED DAESCCGSSC GGGGEETVRR RVGLEREAQD
KAERRRRRMC RNCGEEESCV LLLPCRHLCL CGVCGSSVHT CPICTSPKNA SVHVNMSS
