DRIP2_ARATH
ID DRIP2_ARATH Reviewed; 420 AA.
AC Q94AY3; O04337;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=E3 ubiquitin protein ligase DRIP2;
DE EC=2.3.2.27 {ECO:0000269|PubMed:18552202};
DE AltName: Full=DREB2A-interacting protein 2;
DE AltName: Full=RING-type E3 ubiquitin transferase DRIP2 {ECO:0000305};
GN Name=DRIP2; OrderedLocusNames=At2g30580; ORFNames=T6B20.7;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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, CATALYTIC ACTIVITY, INTERACTION WITH DREB2A, TISSUE SPECIFICITY,
RP AUTOUBIQUITINATION, AND DISRUPTION PHENOTYPE.
RX PubMed=18552202; DOI=10.1105/tpc.107.057380;
RA Qin F., Sakuma Y., Tran L.-S.H., Maruyama K., Kidokoro S., Fujita Y.,
RA Fujita M., Umezawa T., Sawano Y., Miyazono K., Tanokura M., Shinozaki K.,
RA Yamaguchi-Shinozaki K.;
RT "Arabidopsis DREB2A-interacting proteins function as RING E3 ligases and
RT negatively regulate plant drought stress-responsive gene expression.";
RL Plant Cell 20:1693-1707(2008).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that acts as a negative regulator
CC of the response to water stress. Mediates ubiquitination and subsequent
CC proteasomal degradation of the drought-induced transcriptional
CC activator DREB2A. Functionally redundant with DRIP1.
CC {ECO:0000269|PubMed:18552202}.
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:0000269|PubMed:18552202};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with DREB2A. {ECO:0000269|PubMed:18552202}.
CC -!- INTERACTION:
CC Q94AY3; Q38829: IAA11; NbExp=3; IntAct=EBI-1787347, EBI-2367923;
CC Q94AY3; Q5CCK4: VAL2; NbExp=3; IntAct=EBI-1787347, EBI-15193683;
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves and flowers.
CC {ECO:0000269|PubMed:18552202}.
CC -!- PTM: Auto-ubiquitinated. {ECO:0000269|PubMed:18552202}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Drip1 and drip2 double
CC mutant shows delayed growth and development, but increased tolerance to
CC drought stress, compared to wild-type. {ECO:0000269|PubMed:18552202}.
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DR EMBL; U93215; AAB63079.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC08411.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61597.1; -; Genomic_DNA.
DR EMBL; AY045618; AAK73976.1; -; mRNA.
DR EMBL; BT000505; AAN18074.1; -; mRNA.
DR PIR; B84710; B84710.
DR RefSeq; NP_001323803.1; NM_001336273.1.
DR RefSeq; NP_565702.1; NM_128610.3.
DR AlphaFoldDB; Q94AY3; -.
DR SMR; Q94AY3; -.
DR BioGRID; 2957; 16.
DR IntAct; Q94AY3; 22.
DR STRING; 3702.AT2G30580.1; -.
DR PaxDb; Q94AY3; -.
DR PRIDE; Q94AY3; -.
DR ProteomicsDB; 224305; -.
DR EnsemblPlants; AT2G30580.1; AT2G30580.1; AT2G30580.
DR EnsemblPlants; AT2G30580.2; AT2G30580.2; AT2G30580.
DR GeneID; 817608; -.
DR Gramene; AT2G30580.1; AT2G30580.1; AT2G30580.
DR Gramene; AT2G30580.2; AT2G30580.2; AT2G30580.
DR KEGG; ath:AT2G30580; -.
DR Araport; AT2G30580; -.
DR TAIR; locus:2064392; AT2G30580.
DR eggNOG; KOG2660; Eukaryota.
DR HOGENOM; CLU_039235_1_0_1; -.
DR InParanoid; Q94AY3; -.
DR OMA; SKHQRVA; -.
DR OrthoDB; 530390at2759; -.
DR PhylomeDB; Q94AY3; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q94AY3; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q94AY3; baseline and differential.
DR Genevisible; Q94AY3; AT.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IGI:TAIR.
DR CDD; cd17087; RAWUL_DRIP_like; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR044768; DRIP-like_RAWUL.
DR InterPro; IPR044807; DRIP1-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR46293; PTHR46293; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Reference proteome; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..420
FT /note="E3 ubiquitin protein ligase DRIP2"
FT /id="PRO_0000397043"
FT ZN_FING 20..61
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 113..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 420 AA; 47190 MW; CA82BBBA58C7C801 CRC64;
MEGDMVAKVK RETVVACMTC PLCDKLLRDA TTISECLHTF CRKCIYEKIT EDEIESCPVC
DIDLGGTPLE KLRPDHILQD LRAKLFPLKR KKERAPEVVS SISLPAKRKE RSISSLVVST
PRVSAQAGTT GKRTKAATRK DVRGSGSFTK RTVKKEEEFG DDHVESASSP ETLKKFTQNK
RQSSYANPNQ SLSNRRNKDV DEPWDSKLHL WKPLNFLVDV ANGTKDPKSE LGNASHNDVQ
GSKTKTKDHK RKCKLEEEIS NNGDPTTSET ATLKRTRRTR RKRSSTFGDS RIPLLPGAAS
LKQERRNGHV WFSLVASSNQ EGEASLPQIP ANYLRIRDGN IPVSFIQKYL MRKLDLKSED
EVEITCMGEP VIPTLQLHSL VDLWLETTSK HQRVAASIGS SAKEFVMVLV YSRKLPECNN
