RGLG1_ARATH
ID RGLG1_ARATH Reviewed; 489 AA.
AC Q9SS90;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=E3 ubiquitin-protein ligase RGLG1 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=RING domain ligase 1 {ECO:0000303|PubMed:17586653};
GN Name=RGLG1 {ECO:0000303|PubMed:17586653}; OrderedLocusNames=At3g01650;
GN ORFNames=F4P13.19;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [4]
RP IDENTIFICATION, FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH UBC35, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=17586653; DOI=10.1105/tpc.107.052035;
RA Yin X.-J., Volk S., Ljung K., Mehlmer N., Dolezal K., Ditengou F.,
RA Hanano S., Davis S.J., Schmelzer E., Sandberg G., Teige M., Palme K.,
RA Pickart C., Bachmair A.;
RT "Ubiquitin lysine 63 chain forming ligases regulate apical dominance in
RT Arabidopsis.";
RL Plant Cell 19:1898-1911(2007).
RN [5]
RP FUNCTION, INTERACTION WITH ERF053, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=22095047; DOI=10.1104/pp.111.189738;
RA Cheng M.C., Hsieh E.J., Chen J.H., Chen H.Y., Lin T.P.;
RT "Arabidopsis RGLG2, functioning as a RING E3 ligase, interacts with AtERF53
RT and negatively regulates the plant drought stress response.";
RL Plant Physiol. 158:363-375(2012).
RN [6]
RP FUNCTION, AND INTERACTION WITH PP2CA.
RX PubMed=27577789; DOI=10.1105/tpc.16.00364;
RA Wu Q., Zhang X., Peirats-Llobet M., Belda-Palazon B., Wang X., Cui S.,
RA Yu X., Rodriguez P.L., An C.;
RT "Ubiquitin ligases RGLG1 and RGLG5 regulate abscisic acid signaling by
RT controlling the turnover of phosphatase PP2CA.";
RL Plant Cell 28:2178-2196(2016).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates the formation of
CC 'Lys-63'-linked ubiquitin chains. Regulates apical dominance by acting
CC on the auxin transport proteins abundance (PubMed:17586653). Together
CC with RGLG5, mediates the ubiquitination and subsequent proteasomal
CC degradation of the target protein PP2CA. Functions as positive
CC regulator of abscisic acid (ABA) signaling through ABA-dependent
CC degradation of PP2CA, a major inhibitor of ABA signaling
CC (PubMed:27577789). Acts as a negative regulator of drought stress
CC response (PubMed:22095047). {ECO:0000269|PubMed:17586653,
CC ECO:0000269|PubMed:22095047, ECO:0000269|PubMed:27577789}.
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 the heterodimer UBC35/UEV1B (PubMed:17586653).
CC Interacts with ERF053 (PubMed:22095047). Interacts with PP2CA
CC (PubMed:27577789). {ECO:0000269|PubMed:17586653,
CC ECO:0000269|PubMed:22095047, ECO:0000269|PubMed:27577789}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}. Nucleus {ECO:0000269|PubMed:22095047}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:17586653}.
CC -!- PTM: N-myristoylated. {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype; due to the redundancy with
CC RGLG2 (PubMed:17586653, PubMed:22095047). Rglg1 and rglg2 double
CC mutants show a complete loss of apical dominance (PubMed:17586653). The
CC double mutant seedlings rglg1 and rglg2 exhibit a dehydration-tolerant
CC phenotype (PubMed:22095047). {ECO:0000269|PubMed:17586653,
CC ECO:0000269|PubMed:22095047}.
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DR EMBL; AC009325; AAF01562.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73699.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63886.1; -; Genomic_DNA.
DR EMBL; BX824117; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001325948.1; NM_001337352.1.
DR RefSeq; NP_186814.1; NM_111031.4.
DR PDB; 6K82; X-ray; 1.40 A; B=129-419.
DR PDB; 6K83; X-ray; 2.39 A; A/B/C/D/E/F/G/H=129-419.
DR PDB; 6K85; X-ray; 1.61 A; B=129-419.
DR PDB; 6K86; X-ray; 1.59 A; B=129-419.
DR PDB; 6K87; X-ray; 1.50 A; B=129-419.
DR PDB; 6K88; X-ray; 1.79 A; A/B=133-383.
DR PDB; 6K89; X-ray; 1.69 A; B=129-419.
DR PDB; 6K8A; X-ray; 2.40 A; A/B=129-419.
DR PDB; 6K8B; X-ray; 2.21 A; A/B=129-419.
DR PDBsum; 6K82; -.
DR PDBsum; 6K83; -.
DR PDBsum; 6K85; -.
DR PDBsum; 6K86; -.
DR PDBsum; 6K87; -.
DR PDBsum; 6K88; -.
DR PDBsum; 6K89; -.
DR PDBsum; 6K8A; -.
DR PDBsum; 6K8B; -.
DR AlphaFoldDB; Q9SS90; -.
DR SMR; Q9SS90; -.
DR BioGRID; 5246; 2.
DR STRING; 3702.AT3G01650.1; -.
DR PaxDb; Q9SS90; -.
DR PRIDE; Q9SS90; -.
DR ProteomicsDB; 236888; -.
DR EnsemblPlants; AT3G01650.1; AT3G01650.1; AT3G01650.
DR EnsemblPlants; AT3G01650.2; AT3G01650.2; AT3G01650.
DR GeneID; 819911; -.
DR Gramene; AT3G01650.1; AT3G01650.1; AT3G01650.
DR Gramene; AT3G01650.2; AT3G01650.2; AT3G01650.
DR KEGG; ath:AT3G01650; -.
DR Araport; AT3G01650; -.
DR TAIR; locus:2084218; AT3G01650.
DR eggNOG; KOG1327; Eukaryota.
DR HOGENOM; CLU_035766_1_0_1; -.
DR InParanoid; Q9SS90; -.
DR OMA; QYSQEGY; -.
DR OrthoDB; 1067545at2759; -.
DR PhylomeDB; Q9SS90; -.
DR PRO; PR:Q9SS90; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SS90; baseline and differential.
DR Genevisible; Q9SS90; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:TAIR.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0080148; P:negative regulation of response to water deprivation; IGI:TAIR.
DR GO; GO:0009789; P:positive regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IDA:UniProtKB.
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; SM00327; VWA; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Abscisic acid signaling pathway; Cell membrane; Lipoprotein;
KW Membrane; Metal-binding; Myristate; Nucleus; Reference proteome;
KW Stress response; Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..489
FT /note="E3 ubiquitin-protein ligase RGLG1"
FT /id="PRO_0000344783"
FT DOMAIN 156..376
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT ZN_FING 446..479
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..59
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
FT CONFLICT 404
FT /note="P -> L (in Ref. 3; BX824117)"
FT /evidence="ECO:0000305"
FT HELIX 130..134
FT /evidence="ECO:0007829|PDB:6K82"
FT HELIX 140..149
FT /evidence="ECO:0007829|PDB:6K82"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:6K82"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:6K82"
FT TURN 169..177
FT /evidence="ECO:0007829|PDB:6K82"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:6K82"
FT HELIX 189..201
FT /evidence="ECO:0007829|PDB:6K82"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:6K82"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:6K88"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:6K82"
FT TURN 218..223
FT /evidence="ECO:0007829|PDB:6K82"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:6K82"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:6K82"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:6K82"
FT HELIX 238..248
FT /evidence="ECO:0007829|PDB:6K82"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:6K82"
FT HELIX 261..273
FT /evidence="ECO:0007829|PDB:6K82"
FT STRAND 279..287
FT /evidence="ECO:0007829|PDB:6K82"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:6K82"
FT HELIX 302..314
FT /evidence="ECO:0007829|PDB:6K82"
FT STRAND 317..325
FT /evidence="ECO:0007829|PDB:6K82"
FT HELIX 334..339
FT /evidence="ECO:0007829|PDB:6K82"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:6K8B"
FT STRAND 349..353
FT /evidence="ECO:0007829|PDB:6K82"
FT HELIX 354..358
FT /evidence="ECO:0007829|PDB:6K82"
FT STRAND 360..362
FT /evidence="ECO:0007829|PDB:6K82"
FT HELIX 364..376
FT /evidence="ECO:0007829|PDB:6K82"
FT HELIX 379..388
FT /evidence="ECO:0007829|PDB:6K82"
SQ SEQUENCE 489 AA; 53312 MW; C677530E1B20B518 CRC64;
MGGGNSKEES SSPSSSSWAS HQSYPQYGPD SYNYPPPPTY APAPSPAPAP APVPAPSPAS
SYGPQYSQEG YASQPNNPPP PTYAPAPSPA SSYGHQYSQE GYASAASQPN YPPPPSQSQV
ADRKKFDRRY SKISDNYSSL LQVSEALGRA GLESSNLIVG IDFTKSNEWT GAKSFNRKSL
HHLSNTPNPY EQAITIIGRT LAAFDEDNLI PCYGFGDAST HDQDVFSFYP EGRFCNGFEE
VLARYREIVP QLKLAGPTSF APIIEMAMTV VEQSSGQYHV LVIIADGQVT RSVDTEHGRL
SPQEQKTVDA IVKASTLPLS IVLVGVGDGP WDMMQEFDDN IPARAFDNFQ FVNFTEIMSK
NKDQSRKETE FALSALMEIP PQYKATIELN LLGVRNGNIP QRIPLPPPVQ SGSSFSSSRI
PNFEPSVPPY PFESKQMSSA DDIQLCPICL SNPKNMAFGC GHQTCCECGP DLKVCPICRA
PIQTRIKLY
