DDA1_ARATH
ID DDA1_ARATH Reviewed; 101 AA.
AC Q9FFS4;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=DET1- and DDB1-associated protein 1 {ECO:0000303|PubMed:24563205};
GN Name=DDA1 {ECO:0000303|PubMed:24563205};
GN Synonyms=MBK23.8 {ECO:0000312|EMBL:BAB11462.1};
GN OrderedLocusNames=At5g41560 {ECO:0000312|Araport:AT5G41560};
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=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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 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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, IDENTIFICATION IN CDD COMPLEX WITH COP10; DET1 AND DDB1, AND
RP INTERACTION WITH DDB1A; DDB1B; PYL4; PYL8 AND PYL9.
RX PubMed=24563205; DOI=10.1105/tpc.113.122234;
RA Irigoyen M.L., Iniesto E., Rodriguez L., Puga M.I., Yanagawa Y., Pick E.,
RA Strickland E., Paz-Ares J., Wei N., De Jaeger G., Rodriguez P.L.,
RA Deng X.W., Rubio V.;
RT "Targeted degradation of abscisic acid receptors is mediated by the
RT ubiquitin ligase substrate adaptor DDA1 in Arabidopsis.";
RL Plant Cell 26:712-728(2014).
RN [6]
RP INTERACTION WITH SGF11, AND SUBCELLULAR LOCATION.
RX PubMed=30192741; DOI=10.7554/elife.37892;
RA Nassrallah A., Rougee M., Bourbousse C., Drevensek S., Fonseca S.,
RA Iniesto E., Ait-Mohamed O., Deton-Cabanillas A.F., Zabulon G., Ahmed I.,
RA Stroebel D., Masson V., Lombard B., Eeckhout D., Gevaert K., Loew D.,
RA Genovesio A., Breyton C., de Jaeger G., Bowler C., Rubio V., Barneche F.;
RT "DET1-mediated degradation of a SAGA-like deubiquitination module controls
RT H2Bub homeostasis.";
RL Elife 7:0-0(2018).
CC -!- FUNCTION: Involved in ubiquitination and subsequent proteasomal
CC degradation of target proteins (PubMed:24563205). Associates with the
CC CDD complex and mediates the recognition of specific substrates for
CC CUL4-RING E3 ubiquitin ligase (CRL4) by interacting with ubiquitination
CC targets (PubMed:24563205). Binds to the abscisic acid (ABA) receptor
CC PYL8 (required for ABA-mediated responses) and promotes its proteasomal
CC degradation (PubMed:24563205). Acts as negative regulator of ABA-
CC mediated developmental responses, including inhibition of seed
CC germination, seedling establishment, and root growth (PubMed:24563205).
CC {ECO:0000269|PubMed:24563205}.
CC -!- SUBUNIT: Associates with the CDD complex, formed by COP10, DET1 and
CC DDB1 (PubMed:24563205). Interacts directly with DDB1A and DDB1B
CC (PubMed:24563205). Interacts with PYL4, PYL8, and PYL9
CC (PubMed:24563205). Interacts with SGF11 (PubMed:30192741).
CC {ECO:0000269|PubMed:24563205, ECO:0000269|PubMed:30192741}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:30192741}. Note=Displays a rather patchy
CC distribution forming a punctuated pattern in the euchromatin
CC (PubMed:30192741). Does not localize in the heterochromatic
CC chromocenters or nucleolus (PubMed:30192741).
CC {ECO:0000269|PubMed:30192741}.
CC -!- SIMILARITY: Belongs to the DDA1 family. {ECO:0000305}.
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DR EMBL; AB005233; BAB11462.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94692.1; -; Genomic_DNA.
DR EMBL; BT008331; AAP37690.1; -; mRNA.
DR EMBL; AK228323; BAF00265.1; -; mRNA.
DR RefSeq; NP_198971.1; NM_123520.5.
DR AlphaFoldDB; Q9FFS4; -.
DR IntAct; Q9FFS4; 1.
DR STRING; 3702.AT5G41560.1; -.
DR PaxDb; Q9FFS4; -.
DR PRIDE; Q9FFS4; -.
DR ProteomicsDB; 187863; -.
DR EnsemblPlants; AT5G41560.1; AT5G41560.1; AT5G41560.
DR GeneID; 834158; -.
DR Gramene; AT5G41560.1; AT5G41560.1; AT5G41560.
DR KEGG; ath:AT5G41560; -.
DR Araport; AT5G41560; -.
DR TAIR; locus:2160502; AT5G41560.
DR eggNOG; KOG4816; Eukaryota.
DR HOGENOM; CLU_142525_0_0_1; -.
DR InParanoid; Q9FFS4; -.
DR OMA; YQHAEEK; -.
DR OrthoDB; 1521756at2759; -.
DR PhylomeDB; Q9FFS4; -.
DR PRO; PR:Q9FFS4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FFS4; baseline and differential.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IPI:TAIR.
DR GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; IMP:TAIR.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:TAIR.
DR InterPro; IPR033575; DDA1.
DR InterPro; IPR018276; DDA1_N.
DR PANTHER; PTHR31879; PTHR31879; 1.
DR Pfam; PF10172; DDA1; 1.
PE 1: Evidence at protein level;
KW Nucleus; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..101
FT /note="DET1- and DDB1-associated protein 1"
FT /id="PRO_0000446676"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 101 AA; 11356 MW; EC8A87E2EC199369 CRC64;
MASILGDLPS FDPHNFSQHR PSDPSNPSKM VPTTYRPTHN RTLPPPDQVI TTEVKNILIR
SFYQRAEEKL RPKRPATDHL AAEHVNKHFR AASSSSSTQG L
