ID DRIP1_ARATH Reviewed; 421 AA.
AC Q9M9Y4; Q3EDH5;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 24-JAN-2024, entry version 106.
DE RecName: Full=E3 ubiquitin protein ligase DRIP1;
DE EC=2.3.2.27 {ECO:0000269|PubMed:18552202};
DE AltName: Full=DREB2A-interacting protein 1;
DE AltName: Full=RING-type E3 ubiquitin transferase DRIP1 {ECO:0000305};
GN Name=DRIP1; OrderedLocusNames=At1g06770; ORFNames=F4H5.14;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 115-421.
RC STRAIN=cv. Columbia;
RA De Los Reyes C., Quan R., Chen H., Bautista V.R., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH DREB2A, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, 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 DRIP2.
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 Q9M9Y4; O82132: DREB2A; NbExp=4; IntAct=EBI-1786858, EBI-1786840;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18552202}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9M9Y4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9M9Y4-2; Sequence=VSP_039633;
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves and flowers.
CC {ECO:0000269|PubMed:18552202}.
CC -!- PTM: Autoubiquitinated. {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF63142.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BX815334; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AC011001; AAF63142.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28033.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28034.1; -; Genomic_DNA.
DR EMBL; BX815334; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BT033132; ACF28393.1; -; mRNA.
DR PIR; E86202; E86202.
DR RefSeq; NP_172162.3; NM_100554.5. [Q9M9Y4-1]
DR RefSeq; NP_973775.1; NM_202046.2. [Q9M9Y4-2]
DR PDB; 5Y53; X-ray; 1.60 A; D/F=269-286.
DR PDBsum; 5Y53; -.
DR AlphaFoldDB; Q9M9Y4; -.
DR SMR; Q9M9Y4; -.
DR BioGRID; 22429; 2.
DR IntAct; Q9M9Y4; 1.
DR STRING; 3702.Q9M9Y4; -.
DR iPTMnet; Q9M9Y4; -.
DR PaxDb; 3702-AT1G06770-1; -.
DR ProteomicsDB; 224304; -. [Q9M9Y4-1]
DR EnsemblPlants; AT1G06770.1; AT1G06770.1; AT1G06770. [Q9M9Y4-1]
DR EnsemblPlants; AT1G06770.2; AT1G06770.2; AT1G06770. [Q9M9Y4-2]
DR GeneID; 837188; -.
DR Gramene; AT1G06770.1; AT1G06770.1; AT1G06770. [Q9M9Y4-1]
DR Gramene; AT1G06770.2; AT1G06770.2; AT1G06770. [Q9M9Y4-2]
DR KEGG; ath:AT1G06770; -.
DR Araport; AT1G06770; -.
DR TAIR; AT1G06770; DRIP1.
DR eggNOG; KOG2660; Eukaryota.
DR HOGENOM; CLU_039235_1_0_1; -.
DR InParanoid; Q9M9Y4; -.
DR OMA; SAHYLRI; -.
DR OrthoDB; 445545at2759; -.
DR PhylomeDB; Q9M9Y4; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9M9Y4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9M9Y4; baseline and differential.
DR Genevisible; Q9M9Y4; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
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 CDD; cd16525; RING-HC_PCGF; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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; E3 UBIQUITIN PROTEIN LIGASE DRIP1; 1.
DR PANTHER; PTHR46293:SF1; E3 UBIQUITIN PROTEIN LIGASE DRIP1; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Metal-binding; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..421
FT /note="E3 ubiquitin protein ligase DRIP1"
FT /id="PRO_0000397042"
FT ZN_FING 16..57
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 106..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..114
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_039633"
SQ SEQUENCE 421 AA; 47328 MW; 56F7D797DE944567 CRC64;
MMIKVKKETM RACLSCSICD NILRDATTIS ECLHTFCRKC IYEKITEDEI ETCPVCNIDL
GSTPLEKLRP DHNLQDLRAK IFALKRRKVK APGIVSLPGK RKERSISSLV VSTPMVSAQA
GTTRRRTKAP TRKELRNGSL AERTVKKEES SGDELLESTS SPDTLNKFTQ NKRQSKKSCK
ESISNKENKD GDEPWDSKMD WKPLNFLVEV ANGTKPLKSS ASQGSGSKSE HANVSRNQFQ
GSKTKTKNKK RKCKREDDKS NNGDPTTSET VTPKRMRTTQ RKRSATTLGD SRNLPQPDES
SAKQERRNGP VWFSLVASND QEGGTSLPQI PANFLRIRDG NTTVSFIQKY LMRKLDLESE
NEIEIKCMGE AVIPTLTLYN LVDLWLQKSS NHQRFAALVG SSAKDFTMVL VYARKLPECN
M
//
