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DRIP1_ARATH
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   25-MAY-2022, entry version 99.
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.AT1G06770.1; -.
DR   iPTMnet; Q9M9Y4; -.
DR   PaxDb; Q9M9Y4; -.
DR   PRIDE; Q9M9Y4; -.
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; locus:2033103; AT1G06770.
DR   eggNOG; KOG2660; Eukaryota.
DR   HOGENOM; CLU_039235_1_0_1; -.
DR   InParanoid; Q9M9Y4; -.
DR   OMA; SAKEYMM; -.
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   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   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
 
 
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