RDUF2_ARATH
ID RDUF2_ARATH Reviewed; 407 AA.
AC Q940T5; Q9LTH6;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=E3 ubiquitin-protein ligase RDUF2 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=RING and DUF1117 domain-containing protein 2 {ECO:0000305};
DE Short=AtRDUF2 {ECO:0000303|PubMed:22405823};
DE AltName: Full=RING-type E3 ubiquitin transferase RDUF2 {ECO:0000305};
GN Name=DURF2 {ECO:0000303|PubMed:22405823};
GN OrderedLocusNames=At5g59550 {ECO:0000312|Araport:AT5G59550};
GN ORFNames=F2O15.22 {ECO:0000312|EMBL:BAA97489.1};
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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-239, 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).
CC -!- FUNCTION: E3 ubiquitin-protein ligase involved in the positive
CC regulation of abscisic acid-dependent drought stress responses.
CC Possesses E3 ubiquitin ligase activity in vitro.
CC {ECO:0000269|PubMed:22405823}.
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
CC {ECO:0000250|UniProtKB:Q9SNB6}.
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, but mutant plants have decreased sensitivity to abscisic
CC acid (ABA) and reduced tolerance to drought stress.
CC {ECO:0000269|PubMed:22405823}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA97489.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB025604; BAA97489.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED97204.1; -; Genomic_DNA.
DR EMBL; AY052711; AAK96615.1; -; mRNA.
DR EMBL; AY063719; AAL36069.1; -; mRNA.
DR RefSeq; NP_001331469.1; NM_001345358.1.
DR RefSeq; NP_568910.1; NM_125347.3.
DR AlphaFoldDB; Q940T5; -.
DR SMR; Q940T5; -.
DR STRING; 3702.AT5G59550.1; -.
DR PaxDb; Q940T5; -.
DR PRIDE; Q940T5; -.
DR EnsemblPlants; AT5G59550.1; AT5G59550.1; AT5G59550.
DR GeneID; 836074; -.
DR Gramene; AT5G59550.1; AT5G59550.1; AT5G59550.
DR KEGG; ath:AT5G59550; -.
DR Araport; AT5G59550; -.
DR TAIR; locus:2148318; AT5G59550.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_040377_0_0_1; -.
DR InParanoid; Q940T5; -.
DR OMA; MSSTYWC; -.
DR OrthoDB; 1249953at2759; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q940T5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q940T5; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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;
KW Reference proteome; Stress response; Transferase; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..407
FT /note="E3 ubiquitin-protein ligase RDUF2"
FT /id="PRO_0000436413"
FT ZN_FING 199..240
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 316..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 239
FT /note="C->S: Loss of E3 ubiquitin ligase activity."
FT /evidence="ECO:0000269|PubMed:22405823"
SQ SEQUENCE 407 AA; 44381 MW; 15CB10DE31EB0494 CRC64;
MPSTPTTPTT TTPITASYWC YSCTRFVSVW ADQGTTTVGS VACPHCDGGF IEQINDSSSA
ATELTIPAST EVRSINNNRR SVIRRRRSGR RPSFNPVIVL QGGAGEREEG EEGDAARDRR
AFEFYYDDGS GSGLRPLPDS VSEILMGSGF ERLLEQLSQI EASATGIGRS GNPPASKSAI
ESLPRVEISD CHIGSEANCA VCTEIFETET EAREMPCKHL FHDDCIVPWL SIRNSCPVCR
FELPSEPNRR SNNNEEDNAV GMTIWRLPGG GFAVGRFNAA MRDGERVLPV VLTEMDGGGI
GNSQDGPRRI SWVRSHGTLE SDSNGTGSGS GSGGRLRRMV RGMVSLMRRV RPNRSSSSSS
AAISTSSDNL DLNIEVESRV LDRSNSVMRR YFRRNRSNRD SSSSVLH
