RGLG2_ARATH
ID RGLG2_ARATH Reviewed; 468 AA.
AC Q9LY87;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=E3 ubiquitin-protein ligase RGLG2 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=RING domain ligase 2 {ECO:0000303|PubMed:17586653};
GN Name=RGLG2 {ECO:0000303|PubMed:17586653}; OrderedLocusNames=At5g14420;
GN ORFNames=F18O22.210;
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 [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=15644464; DOI=10.1104/pp.104.052423;
RA Stone S.L., Hauksdottir H., Troy A., Herschleb J., Kraft E., Callis J.;
RT "Functional analysis of the RING-type ubiquitin ligase family of
RT Arabidopsis.";
RL Plant Physiol. 137:13-30(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
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 [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 IDENTIFICATION, FUNCTION, TISSUE SPECIFICITY, MYRISTOYLATION AT GLY-2,
RP MUTAGENESIS OF GLY-2, INTERACTION WITH UBC35 AND PIN1, AND DISRUPTION
RP 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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [7]
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).
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). Mediates
CC ubiquitination and subsequent proteasomal degradation of ERF053 in
CC response to drought stress. Acts as a negative regulator of drought
CC stress response (PubMed:22095047). {ECO:0000269|PubMed:17586653,
CC ECO:0000269|PubMed:22095047}.
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, UBC35 alone, PIN1,
CC but not with UCB2, UCB9, UEV1B or UEV1C alone (PubMed:17586653).
CC Interacts with ERF053 (PubMed:22095047). {ECO:0000269|PubMed:17586653,
CC ECO:0000269|PubMed:22095047}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}. Nucleus {ECO:0000269|PubMed:22095047}. Note=Translocates
CC to the nucleus under salt stress. {ECO:0000269|PubMed:22095047}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:17586653}.
CC -!- DOMAIN: A C-terminal fragment containing the RING domain interacts with
CC UBC35 while the full-length protein does not.
CC -!- PTM: N-myristoylated. {ECO:0000269|PubMed:17586653}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype; due to the redundancy with
CC RGLG1 (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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ086862; AAZ14078.1; -; mRNA.
DR EMBL; AL163817; CAB87781.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92028.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92029.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92030.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92031.1; -; Genomic_DNA.
DR EMBL; AY099597; AAM20448.1; -; mRNA.
DR EMBL; BT000249; AAN15568.1; -; mRNA.
DR PIR; T48615; T48615.
DR RefSeq; NP_196946.1; NM_121446.5.
DR RefSeq; NP_850818.1; NM_180487.4.
DR RefSeq; NP_974779.1; NM_203050.3.
DR RefSeq; NP_974780.1; NM_203051.3.
DR AlphaFoldDB; Q9LY87; -.
DR SMR; Q9LY87; -.
DR BioGRID; 16570; 3.
DR STRING; 3702.AT5G14420.2; -.
DR iPTMnet; Q9LY87; -.
DR PaxDb; Q9LY87; -.
DR PRIDE; Q9LY87; -.
DR ProteomicsDB; 236236; -.
DR EnsemblPlants; AT5G14420.1; AT5G14420.1; AT5G14420.
DR EnsemblPlants; AT5G14420.2; AT5G14420.2; AT5G14420.
DR EnsemblPlants; AT5G14420.3; AT5G14420.3; AT5G14420.
DR EnsemblPlants; AT5G14420.4; AT5G14420.4; AT5G14420.
DR GeneID; 831293; -.
DR Gramene; AT5G14420.1; AT5G14420.1; AT5G14420.
DR Gramene; AT5G14420.2; AT5G14420.2; AT5G14420.
DR Gramene; AT5G14420.3; AT5G14420.3; AT5G14420.
DR Gramene; AT5G14420.4; AT5G14420.4; AT5G14420.
DR KEGG; ath:AT5G14420; -.
DR Araport; AT5G14420; -.
DR TAIR; locus:2145643; AT5G14420.
DR eggNOG; KOG1327; Eukaryota.
DR HOGENOM; CLU_035766_1_0_1; -.
DR InParanoid; Q9LY87; -.
DR OMA; KENWRQS; -.
DR OrthoDB; 1067545at2759; -.
DR PhylomeDB; Q9LY87; -.
DR BRENDA; 2.3.2.27; 399.
DR PRO; PR:Q9LY87; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LY87; baseline and differential.
DR Genevisible; Q9LY87; 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; IEA:InterPro.
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:0009850; P:auxin metabolic process; IGI:TAIR.
DR GO; GO:0009690; P:cytokinin metabolic process; IGI:TAIR.
DR GO; GO:0080148; P:negative regulation of response to water deprivation; IGI:TAIR.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IEA:InterPro.
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 Abscisic acid signaling pathway; Cell membrane; Lipoprotein; Membrane;
KW Metal-binding; Myristate; Nucleus; Reference proteome; Stress response;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305|PubMed:17586653"
FT CHAIN 2..468
FT /note="E3 ubiquitin-protein ligase RGLG2"
FT /id="PRO_0000344784"
FT DOMAIN 122..342
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT ZN_FING 425..458
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..69
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000305|PubMed:17586653"
FT MUTAGEN 2
FT /note="G->A: Loss of myristoylation."
FT /evidence="ECO:0000269|PubMed:17586653"
SQ SEQUENCE 468 AA; 51578 MW; 2AC6D3FA427FD0B9 CRC64;
MGTGNSKENW RQSSFRSTSA SSASPSSSSW ASQQSYPQYG AESYNYPPPP SYAQPPEYTQ
PPPPLYSTQP YSAPSYSAPP SQSYGSDNKK RLERKYSKIS DDYSSLEQVT EALARAGLES
SNLIVGIDFT KSNEWTGARS FNRKSLHFIG SSPNPYEQAI TIIGRTLAAF DEDNLIPCYG
FGDASTHDQD VFSFNSEDRF CNGFEEVLSR YKEIVPQLKL AGPTSFAPII DMAMTIVEQS
GGQYHVLVII ADGQVTRSVD TENGQLSPQE QKTVDAIVQA SKLPLSIVLV GVGDGPWDMM
REFDDNIPAR AFDNFQFVNF TEIMAKNKAQ SLKETEFALS ALMEIPQQYK ATIELNLLGR
RNGYIPERFP LPPPMRGGSS SYNSPKPSRL PSFKPSVPPH PTEGYHVRSS PVPPPTSSAS
DNQLCPICLS NPKDMAFGCG HQTCCECGPD LQMCPICRAP IQTRIKLY
