RGLG4_ARATH
ID RGLG4_ARATH Reviewed; 401 AA.
AC Q9SAL0;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 158.
DE RecName: Full=E3 ubiquitin-protein ligase RGLG4 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=RING domain ligase 4 {ECO:0000303|PubMed:22898498};
GN Name=RGLG4 {ECO:0000303|PubMed:22898498};
GN OrderedLocusNames=At1g79380 {ECO:0000312|Araport:AT1G79380};
GN ORFNames=T8K14.20 {ECO:0000312|EMBL:AAD30238.1};
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].
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 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 [6]
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.
CC {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: Repressed 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}.
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DR EMBL; AC007202; AAD30238.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36236.1; -; Genomic_DNA.
DR EMBL; AF372928; AAK50068.1; -; mRNA.
DR EMBL; AY133585; AAM91415.1; -; mRNA.
DR PIR; G96824; G96824.
DR RefSeq; NP_565206.1; NM_106586.4.
DR AlphaFoldDB; Q9SAL0; -.
DR SMR; Q9SAL0; -.
DR STRING; 3702.AT1G79380.1; -.
DR iPTMnet; Q9SAL0; -.
DR PaxDb; Q9SAL0; -.
DR PRIDE; Q9SAL0; -.
DR ProteomicsDB; 236856; -.
DR EnsemblPlants; AT1G79380.1; AT1G79380.1; AT1G79380.
DR GeneID; 844276; -.
DR Gramene; AT1G79380.1; AT1G79380.1; AT1G79380.
DR KEGG; ath:AT1G79380; -.
DR Araport; AT1G79380; -.
DR TAIR; locus:2206395; AT1G79380.
DR eggNOG; KOG1327; Eukaryota.
DR HOGENOM; CLU_035766_1_1_1; -.
DR InParanoid; Q9SAL0; -.
DR OMA; CYRRITP; -.
DR OrthoDB; 1067545at2759; -.
DR PhylomeDB; Q9SAL0; -.
DR PRO; PR:Q9SAL0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SAL0; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
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 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; SM00184; RING; 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..401
FT /note="E3 ubiquitin-protein ligase RGLG4"
FT /id="PRO_0000438717"
FT DOMAIN 79..299
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT ZN_FING 357..390
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 401 AA; 43730 MW; A094024885D22A01 CRC64;
MTMGNFLKRF GSGKSRSSRN MTLGTTSSQS HEPSPSDPSL SLADNTNATK KKYALIPDRF
SSLDQVSKAL REAGLESSNL ILGVDFTKSN EWTGKTSFDG KCLHALGETS NPYEKAIFVI
GQTLAPFDED NLIPCFGFGD STTHDEEVFG FHSDNSPCHG FEEVLACYKR IAPNLRLSGP
TSYGPLIDAA VDIVEKNNGQ FHVLVIVADG QVTRGTDMAE GELSQQEKTT IDAIVNASSY
ALSIVLVGVG DGPWEDMRKF DDKIPKREFD NFQFVNFTEI MTRNSPESAK ETAFALAALM
EIPFQYQAAI ELRLLGKQTG LAKTIVPRPP PIPYTPPTNA ELPSTASPAS PEQTQSCPIC
LTNRKDVAFS CGHMTCGDCG SKISNCPICR VRITNRLKLY T
