RGLG3_ARATH
ID RGLG3_ARATH Reviewed; 367 AA.
AC Q8RX26; Q9LVN6;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=E3 ubiquitin-protein ligase RGLG3 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=RING domain ligase 3 {ECO:0000303|PubMed:22898498};
GN Name=RGLG3 {ECO:0000303|PubMed:22898498};
GN OrderedLocusNames=At5g63970 {ECO:0000312|Araport:AT5G63970};
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].
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, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=22898498; DOI=10.1104/pp.112.203422;
RA Zhang X., Wu Q., Ren J., Qian W., He S., Huang K., Yu X., Gao Y., Huang P.,
RA An C.;
RT "Two novel RING-type ubiquitin ligases, RGLG3 and RGLG4, are essential for
RT jasmonate-mediated responses in Arabidopsis.";
RL Plant Physiol. 160:808-822(2012).
RN [5]
RP INTERACTION WITH GAF1/IDD2 AND ENY/IDD1.
RC STRAIN=cv. Columbia;
RX PubMed=25035403; DOI=10.1105/tpc.114.125690;
RA Fukazawa J., Teramura H., Murakoshi S., Nasuno K., Nishida N., Ito T.,
RA Yoshida M., Kamiya Y., Yamaguchi S., Takahashi Y.;
RT "DELLAs function as coactivators of GAI-ASSOCIATED FACTOR1 in regulation of
RT gibberellin homeostasis and signaling in Arabidopsis.";
RL Plant Cell 26:2920-2938(2014).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=25788731; DOI=10.1093/jxb/erv068;
RA Zhang X., Wu Q., Cui S., Ren J., Qian W., Yang Y., He S., Chu J., Sun X.,
RA Yan C., Yu X., An C.;
RT "Hijacking of the jasmonate pathway by the mycotoxin fumonisin B1 (FB1) to
RT initiate programmed cell death in Arabidopsis is modulated by RGLG3 and
RT RGLG4.";
RL J. Exp. Bot. 66:2709-2721(2015).
RN [7]
RP FUNCTION, AND INTERACTION WITH UBC30; GRXS17 AND GLB3.
RX PubMed=27497447; DOI=10.1093/pcp/pcw122;
RA Nagels Durand A., Inigo S., Ritter A., Iniesto E., De Clercq R., Staes A.,
RA Van Leene J., Rubio V., Gevaert K., De Jaeger G., Pauwels L., Goossens A.;
RT "The Arabidopsis iron-sulfur protein GRXS17 is a target of the ubiquitin E3
RT ligases RGLG3 and RGLG4.";
RL Plant Cell Physiol. 57:1801-1813(2016).
CC -!- FUNCTION: Possesses E3 ubiquitin-protein ligase in vitro. Acts as
CC upstream modulator of jasmonate (JA) signaling in response to various
CC stimuli, such as JA-inhibited root growth, JA-inductive gene
CC expression, coronatine-mediated pathogen susceptibility, wound-
CC stimulated expression of JA-responsive genes and wound-induced JA
CC biosynthesis (PubMed:22898498). Controls fumonisin B1 (FB1)-triggered
CC programmed cell death (PCD) by modulating the JA signaling pathway. May
CC mediate salicylic acid (SA) suppression of JA signaling in FB1-induced
CC responses (PubMed:25788731). May mediate the formation of 'Lys-48'-
CC linked multiubiquitin chains. Mediates the polyubiquitination and
CC subsequent proteasomal degradation of the target protein GRXS17
CC (PubMed:27497447). {ECO:0000269|PubMed:22898498,
CC ECO:0000269|PubMed:25788731, ECO:0000269|PubMed:27497447}.
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:0000305};
CC -!- SUBUNIT: Interacts with UBC30, GRXS17 and GLB3 (PubMed:27497447). Binds
CC to and coactivates GAF1/IDD2 and ENY/IDD1 (PubMed:25035403).
CC {ECO:0000269|PubMed:25035403, ECO:0000269|PubMed:27497447}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25788731}. Nucleus
CC {ECO:0000269|PubMed:25788731}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:22898498}.
CC -!- INDUCTION: Induced by the mycotoxin fumonisin B1.
CC {ECO:0000269|PubMed:25788731}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. The double mutant plants rglg3 and rglg4 show decreased
CC sensitivity to jasmonate. {ECO:0000269|PubMed:22898498}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA96900.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB019227; BAA96900.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED97823.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97824.1; -; Genomic_DNA.
DR EMBL; AY090939; AAM13989.1; -; mRNA.
DR EMBL; AY123020; AAM67553.1; -; mRNA.
DR RefSeq; NP_001032132.1; NM_001037055.1.
DR RefSeq; NP_201202.2; NM_125793.6.
DR AlphaFoldDB; Q8RX26; -.
DR SMR; Q8RX26; -.
DR STRING; 3702.AT5G63970.1; -.
DR PaxDb; Q8RX26; -.
DR PRIDE; Q8RX26; -.
DR ProteomicsDB; 236899; -.
DR EnsemblPlants; AT5G63970.1; AT5G63970.1; AT5G63970.
DR EnsemblPlants; AT5G63970.2; AT5G63970.2; AT5G63970.
DR GeneID; 836518; -.
DR Gramene; AT5G63970.1; AT5G63970.1; AT5G63970.
DR Gramene; AT5G63970.2; AT5G63970.2; AT5G63970.
DR KEGG; ath:AT5G63970; -.
DR Araport; AT5G63970; -.
DR TAIR; locus:2160821; AT5G63970.
DR eggNOG; KOG1327; Eukaryota.
DR HOGENOM; CLU_035766_1_1_1; -.
DR InParanoid; Q8RX26; -.
DR OMA; QCLHTIN; -.
DR OrthoDB; 1067545at2759; -.
DR PhylomeDB; Q8RX26; -.
DR PRO; PR:Q8RX26; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8RX26; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0009867; P:jasmonic acid mediated signaling pathway; IMP:TAIR.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IEA:InterPro.
DR GO; GO:0009611; P:response to wounding; IMP:TAIR.
DR CDD; cd16729; RING-HC_RGLG_plant; 1.
DR CDD; cd01459; vWA_copine_like; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR010734; Copine_C.
DR InterPro; IPR045317; RING-HC_RGLG_plant.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF07002; Copine; 1.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Jasmonic acid signaling pathway; Metal-binding; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..367
FT /note="E3 ubiquitin-protein ligase RGLG3"
FT /id="PRO_0000438716"
FT DOMAIN 37..257
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT ZN_FING 323..356
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ SEQUENCE 367 AA; 41189 MW; 09A0D8288DF1E168 CRC64;
MNMSNKRNQQ PSYIADHFSS LDQVITSLRE AGLESSNLIL GIDFTKSNEW TGRYSFNRKS
LHAIGKRQNP YEKAISIIGR TLSPFDEDDL IPCFGFGDVT TRDQYVFSFY PENKSCDGLE
NAVKRYREIV PHLKLSGPTS FAPVIDAAIN IVEQNNMQYH VLVIIADGQV TRNPDVPLGR
LSPQEEATMN SIMAASHYPL SIVLVGVGDG PWDTMKQFDD NIPHREFDNF QFVNFTKIMS
EHKDAAKKEA AFALAALMEI PFQYKATLSL NRKPVRSSHQ HHKPLPPPPE VIERDNAVRS
VPNQMTETAE KSDRLAPSTV PVCPICLTNP KDMAFSCGHT TCKECGVVIT TCPLCRQPIT
TRIRLYT
