RDUF1_ARATH
ID RDUF1_ARATH Reviewed; 395 AA.
AC Q9SNB6;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=E3 ubiquitin-protein ligase RDUF1 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=RING and DUF1117 domain-containing protein 1 {ECO:0000305};
DE Short=AtRDUF1 {ECO:0000303|PubMed:22405823};
DE AltName: Full=RING-type E3 ubiquitin transferase RDUF1 {ECO:0000305};
GN Name=RDUF1 {ECO:0000303|PubMed:22405823};
GN OrderedLocusNames=At3g46620 {ECO:0000312|Araport:AT3G46620};
GN ORFNames=F12A12.140 {ECO:0000312|EMBL:CAB62332.1};
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=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=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, INDUCTION, MUTAGENESIS OF CYS-255, AND DISRUPTION PHENOTYPE.
RX PubMed=22405823; DOI=10.1016/j.bbrc.2012.02.131;
RA Kim S.J., Ryu M.Y., Kim W.T.;
RT "Suppression of Arabidopsis RING-DUF1117 E3 ubiquitin ligases, AtRDUF1 and
RT AtRDUF2, reduces tolerance to ABA-mediated drought stress.";
RL Biochem. Biophys. Res. Commun. 420:141-147(2012).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23951086; DOI=10.1371/journal.pone.0071078;
RA Li J., Han Y., Zhao Q., Li C., Xie Q., Chong K., Xu Y.;
RT "The E3 ligase AtRDUF1 positively regulates salt stress responses in
RT Arabidopsis thaliana.";
RL PLoS ONE 8:E71078-E71078(2013).
CC -!- FUNCTION: E3 ubiquitin-protein ligase involved in the positive
CC regulation of abscisic acid-dependent drought stress responses
CC (PubMed:22405823). Involved in the positive regulation of responses to
CC salt and osmotic stresses during seed germination and early seedling
CC development (PubMed:23951086). Possesses E3 ubiquitin ligase activity
CC in vitro (PubMed:22405823, PubMed:23951086).
CC {ECO:0000269|PubMed:22405823, ECO:0000269|PubMed:23951086}.
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 -!- PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:23951086}.
CC Nucleus {ECO:0000269|PubMed:23951086}.
CC -!- TISSUE SPECIFICITY: Expressed in root tips, leaf tips, junction of
CC carpels and pedicels, stigma, anthers, pollen, vasculature of sepals
CC and petals, immature seeds and embryos. {ECO:0000269|PubMed:23951086}.
CC -!- INDUCTION: Induced by abscisic acid (ABA), and drought and salt
CC stresses. {ECO:0000269|PubMed:22405823}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions (PubMed:22405823, PubMed:23951086). Mutant plants have
CC decreased sensitivity to abscisic acid (ABA) and reduced tolerance to
CC drought stress (PubMed:22405823). {ECO:0000269|PubMed:22405823,
CC ECO:0000269|PubMed:23951086}.
CC -!- MISCELLANEOUS: Plants over-expressing RDUF1 display decreased
CC sensitivity to salt and osmotic stresses.
CC {ECO:0000269|PubMed:23951086}.
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; AL133314; CAB62332.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78184.1; -; Genomic_DNA.
DR EMBL; AY093203; AAM13202.1; -; mRNA.
DR EMBL; BT008859; AAP68298.1; -; mRNA.
DR PIR; T45599; T45599.
DR RefSeq; NP_190246.1; NM_114529.6.
DR AlphaFoldDB; Q9SNB6; -.
DR SMR; Q9SNB6; -.
DR STRING; 3702.AT3G46620.1; -.
DR PaxDb; Q9SNB6; -.
DR PRIDE; Q9SNB6; -.
DR ProteomicsDB; 235013; -.
DR EnsemblPlants; AT3G46620.1; AT3G46620.1; AT3G46620.
DR GeneID; 823815; -.
DR Gramene; AT3G46620.1; AT3G46620.1; AT3G46620.
DR KEGG; ath:AT3G46620; -.
DR Araport; AT3G46620; -.
DR TAIR; locus:2075175; AT3G46620.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_040377_0_0_1; -.
DR InParanoid; Q9SNB6; -.
DR OMA; GASSYWC; -.
DR OrthoDB; 1249953at2759; -.
DR PhylomeDB; Q9SNB6; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9SNB6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SNB6; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
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:0051865; P:protein autoubiquitination; IDA:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR010543; DUF1117.
DR InterPro; IPR039525; RNF126-like_zinc-ribbon.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF06547; DUF1117; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR Pfam; PF14369; zinc_ribbon_9; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Cytoplasm; Metal-binding; Nucleus;
KW Reference proteome; Stress response; Transferase; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..395
FT /note="E3 ubiquitin-protein ligase RDUF1"
FT /id="PRO_0000436412"
FT ZN_FING 215..256
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 255
FT /note="C->S: Loss of E3 ubiquitin ligase activity."
FT /evidence="ECO:0000269|PubMed:22405823"
SQ SEQUENCE 395 AA; 43151 MW; 1AD9BAE031C7ABA1 CRC64;
MMPNSRSATI TPTTESTTTT TTTTTTLTTS YWCYSCTRFI SVWEDQDANA GVLCPYCNGG
FIEEIEDSSN STVAAIPAST PEVRSVEETH RSIIRRRRSN RRTSFNPVIV LHGGGGGGAG
ERVENEEGDG ATRERRAYEF YYDDGSGSGL RPLPDSVSEI LMGSGFERLL EQLSQIEASG
NGIGRSGNPP ASKSAIESLP RVEISDCHTK AEANCAVCTE VFEAGIEGRE MPCKHIFHGD
CIVPWLSIRN SCPVCRFELP SDPIQRSNEE EHAVGMTIWR LPGGGFAVGR FNAGVREGER
ILPVVLTEMD GGGLGSNEGP RRISWVRAHE TPEMSRNGGR SGNGGRLRRA VRGMVSFMRR
VRPSRGSSNS NVIDLDSDGE TRVMNRSTSL IRRFF
