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Database: UniProt
Entry: Q6NPN9
LinkDB: Q6NPN9
Original site: Q6NPN9 
ID   DWA2_ARATH              Reviewed;         350 AA.
AC   Q6NPN9; Q67YQ8; Q9SFW2; Q9SGQ8;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 132.
DE   RecName: Full=WD repeat-containing protein DWA2;
DE   AltName: Full=Protein DWD HYPERSENSITIVE TO ABA 2;
GN   Name=DWA2; OrderedLocusNames=At1g76260; ORFNames=F15M4.24, T23E18.19;
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;
RA   Kim C.J., Chen H., Cheuk R.F., Shinn P., Carninci P., Hayashizaki Y.,
RA   Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA   Shinozaki K., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION, COMPONENT OF THE CUL4-RBX1-DDB1-DWA1 COMPLEX, INTERACTION WITH
RP   ABI5; DDB1A AND DWA2, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=20525848; DOI=10.1105/tpc.109.073783;
RA   Lee J.H., Yoon H.J., Terzaghi W., Martinez C., Dai M., Li J., Byun M.O.,
RA   Deng X.W.;
RT   "DWA1 and DWA2, two Arabidopsis DWD protein components of CUL4-based E3
RT   ligases, act together as negative regulators in aba signal transduction.";
RL   Plant Cell 22:1716-1732(2010).
CC   -!- FUNCTION: Component of the CUL4-RBX1-DDB1-DWA1/DWA2 E3 ubiquitin-
CC       protein ligase complex that acts as a negative regulator in abscisic
CC       acid (ABA) signaling. May function as the substrate recognition module
CC       within this complex leading to ABI5 degradation. Functionally redundant
CC       with DWA1. {ECO:0000269|PubMed:20525848}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with ABI5 and DDB1A and DWA1.
CC       {ECO:0000269|PubMed:20525848}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20525848}.
CC   -!- DISRUPTION PHENOTYPE: Increased sensitivity to abscisic acid (ABA) and
CC       salt. {ECO:0000269|PubMed:20525848}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF16674.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAF17630.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC009978; AAF17630.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC012394; AAF16674.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE35816.1; -; Genomic_DNA.
DR   EMBL; BT010880; AAR24658.1; -; mRNA.
DR   EMBL; AK176410; BAD44173.1; -; mRNA.
DR   EMBL; AK175439; BAD43202.1; -; mRNA.
DR   EMBL; AK176650; BAD44413.1; -; mRNA.
DR   RefSeq; NP_177753.1; NM_106276.5.
DR   AlphaFoldDB; Q6NPN9; -.
DR   SMR; Q6NPN9; -.
DR   BioGRID; 29178; 5.
DR   STRING; 3702.Q6NPN9; -.
DR   iPTMnet; Q6NPN9; -.
DR   PaxDb; 3702-AT1G76260-1; -.
DR   ProteomicsDB; 222041; -.
DR   DNASU; 843959; -.
DR   EnsemblPlants; AT1G76260.1; AT1G76260.1; AT1G76260.
DR   GeneID; 843959; -.
DR   Gramene; AT1G76260.1; AT1G76260.1; AT1G76260.
DR   KEGG; ath:AT1G76260; -.
DR   Araport; AT1G76260; -.
DR   TAIR; AT1G76260; DWA2.
DR   eggNOG; KOG1007; Eukaryota.
DR   HOGENOM; CLU_050772_0_0_1; -.
DR   InParanoid; Q6NPN9; -.
DR   OMA; AVWRMPE; -.
DR   OrthoDB; 167212at2759; -.
DR   PhylomeDB; Q6NPN9; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q6NPN9; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q6NPN9; baseline and differential.
DR   Genevisible; Q6NPN9; AT.
DR   GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISS:TAIR.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; IMP:UniProtKB.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR040323; EIPR1.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR14205:SF16; WD REPEAT-CONTAINING PROTEIN DWA2; 1.
DR   PANTHER; PTHR14205; WD-REPEAT PROTEIN; 1.
DR   Pfam; PF00400; WD40; 2.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Abscisic acid signaling pathway; Nucleus; Reference proteome; Repeat;
KW   Ubl conjugation pathway; WD repeat.
FT   CHAIN           1..350
FT                   /note="WD repeat-containing protein DWA2"
FT                   /id="PRO_0000396858"
FT   REPEAT          39..79
FT                   /note="WD 1"
FT   REPEAT          118..158
FT                   /note="WD 2"
FT   REPEAT          166..205
FT                   /note="WD 3"
FT   REPEAT          206..246
FT                   /note="WD 4"
FT   REPEAT          250..290
FT                   /note="WD 5"
FT   REPEAT          311..350
FT                   /note="WD 6"
FT   CONFLICT        217
FT                   /note="N -> D (in Ref. 3; BAD44173)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   350 AA;  39054 MW;  8D13197760FABBC6 CRC64;
     MQGGSSGIGY GLKYQARCIS DVKADRDHTS FLTGTLSLKE ENEVHLLRLS SGGSELLCEG
     LFSHPNEIWD LASSPFDQRI FSTVFSTGDS YGAAIWQIPE PYGQSNSSTL ECVASLDAHV
     GKINCVLWCP SGNSDKLISM DEQNLVFWSL DSSKKSAEVL SKESAGMRHS LSGGAWNPHD
     VNSVAATSES SIQFWDLRTM KKNNSIERAH VRNVDYNLKR EHILVSADDE SGIHLWDLRK
     TKFPVQELPG HTHWTWAVRC NPEYEELILS VGTDSAVNLW FASASSEHKT SESPVEASRQ
     RVNPLLNSYT DYEDSVYGLA WSSREPWIFA SLSYDGRVVI ESVKPFLPRR
//
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