DRIPH_ARATH
ID DRIPH_ARATH Reviewed; 480 AA.
AC Q9LS86;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Probable E3 ubiquitin protein ligase DRIPH;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q9M9Y4};
DE AltName: Full=DREB2A-interacting protein homolog;
DE AltName: Full=RING-type E3 ubiquitin transferase DRIPH {ECO:0000305};
GN OrderedLocusNames=At3g23060; ORFNames=MXC7.9;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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).
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:0000250|UniProtKB:Q9M9Y4};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- INTERACTION:
CC Q9LS86; Q9LEZ3: BIM1; NbExp=3; IntAct=EBI-4445671, EBI-617095;
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DR EMBL; AB026655; BAB02097.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76711.1; -; Genomic_DNA.
DR EMBL; AY099845; AAM20696.1; -; mRNA.
DR EMBL; BT006623; AAP31967.1; -; mRNA.
DR RefSeq; NP_188946.2; NM_113206.5.
DR AlphaFoldDB; Q9LS86; -.
DR SMR; Q9LS86; -.
DR BioGRID; 7212; 6.
DR IntAct; Q9LS86; 6.
DR STRING; 3702.AT3G23060.1; -.
DR iPTMnet; Q9LS86; -.
DR PaxDb; Q9LS86; -.
DR PRIDE; Q9LS86; -.
DR ProteomicsDB; 224306; -.
DR EnsemblPlants; AT3G23060.1; AT3G23060.1; AT3G23060.
DR GeneID; 821880; -.
DR Gramene; AT3G23060.1; AT3G23060.1; AT3G23060.
DR KEGG; ath:AT3G23060; -.
DR Araport; AT3G23060; -.
DR TAIR; locus:2094608; AT3G23060.
DR eggNOG; KOG2660; Eukaryota.
DR HOGENOM; CLU_039235_1_0_1; -.
DR InParanoid; Q9LS86; -.
DR OMA; ISNAYIR; -.
DR OrthoDB; 969344at2759; -.
DR PhylomeDB; Q9LS86; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9LS86; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LS86; baseline and differential.
DR Genevisible; Q9LS86; AT.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
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 pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..480
FT /note="Probable E3 ubiquitin protein ligase DRIPH"
FT /id="PRO_0000397044"
FT ZN_FING 16..57
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 93..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 480 AA; 53664 MW; 4E656E20E7A01E7E CRC64;
MLTKVLSKEV KPCLACPICT NPFKDATTIS ECLHTFCRSC IRNKFINERV NACPVCNVNL
GVFPLEKLRS DCTWQDLKLK IYRAMMESLK KAGPKTVAAS VKSSKKKRKS RTSLRVSSSR
VSSSPDTPLE PANVVVEPPN VVVEEKHRET VLALQSTRKP IITFQKRGRK ASLPKKIDSK
PEPELPPKEP KIKNLFDLNN EPEDNGLDEA EGSTFQEVVP KEKDLCKPIF SLSVTLNIND
TPPDIVEPEI SSDDDTEESV EPIQNKCVVN RETKEVPVQV NQNSLLISSD RDREDNSGQK
LKTNGAATSR SRKKKGKKPV EKSYSLRPRI GRRTVNPAAG TTTPEAPVSV EEEMKVEEGR
NNNPVWFSLK PSKTQNIEML LPPITACCIR VKDSNMTVSY LKKYLMVKLG LESEDQVEIW
LRDEPVCSSL TLHNLVDWWV QTTPLPERQS AMVGSSAAEF IMDLYYSFKS DASDSGSASE
