DET1_ARATH
ID DET1_ARATH Reviewed; 543 AA.
AC P48732; Q66GQ4;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Light-mediated development protein DET1;
DE AltName: Full=Protein DEETIOLATED 1;
GN Name=DET1; OrderedLocusNames=At4g10180; ORFNames=F28M11.100, T9A4.13;
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 [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=8033202; DOI=10.1016/0092-8674(94)90577-0;
RA Pepper A., Delaney T., Washburn T., Poole D., Chory J.;
RT "DET1, a negative regulator of light-mediated development and gene
RT expression in Arabidopsis, encodes a novel nuclear-localized protein.";
RL Cell 78:109-116(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Zidanic M., McQuerry Y., Smith A.;
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION.
RX PubMed=9681024; DOI=10.1046/j.1365-313x.1998.00078.x;
RA Christopher D.A., Hoffer P.H.;
RT "DET1 represses a chloroplast blue light-responsive promoter in a
RT developmental and tissue-specific manner in Arabidopsis thaliana.";
RL Plant J. 14:1-11(1998).
RN [7]
RP INTERACTION WITH DDB1A.
RX PubMed=12225661; DOI=10.1016/s0960-9822(02)01106-5;
RA Schroeder D.F., Gahrtz M., Maxwell B.B., Cook R.K., Kan J.M., Alonso J.M.,
RA Ecker J.R., Chory J.;
RT "De-etiolated 1 and damaged DNA binding protein 1 interact to regulate
RT Arabidopsis photomorphogenesis.";
RL Curr. Biol. 12:1462-1472(2002).
RN [8]
RP INTERACTION WITH HISTONE H2B.
RX PubMed=12225670; DOI=10.1016/s0960-9822(02)01105-3;
RA Benvenuto G., Formiggini F., Laflamme P., Malakhov M., Bowler C.;
RT "The photomorphogenesis regulator DET1 binds the amino-terminal tail of
RT histone H2B in a nucleosome context.";
RL Curr. Biol. 12:1529-1534(2002).
RN [9]
RP FUNCTION, AND COMPONENT OF CDD COMPLEX WITH COP10 AND DDB1A.
RX PubMed=15342494; DOI=10.1101/gad.1229504;
RA Yanagawa Y., Sullivan J.A., Komatsu S., Gusmaroli G., Suzuki G., Yin J.,
RA Ishibashi T., Saijo Y., Rubio V., Kimura S., Wang J., Deng X.-W.;
RT "Arabidopsis COP10 forms a complex with DDB1 and DET1 in vivo and enhances
RT the activity of ubiquitin conjugating enzymes.";
RL Genes Dev. 18:2172-2181(2004).
RN [10]
RP IDENTIFICATION IN CDD COMPLEX WITH COP10 AND DDB1A.
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 [11]
RP FUNCTION, 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: Component of light signal transduction machinery. Involved in
CC repression of photomorphogenesis in darkness by participating in the
CC CDD complex, a complex probably required to regulate the activity of
CC ubiquitin conjugating enzymes (E2s). Involved in repression of
CC deetiolation in the developing seedling. Repression of
CC photomorphogenesis is probably mediated by ubiquitination and
CC subsequent degradation of photomorphogenesis-promoting factors such as
CC HY5, HYH and LAF1. Involved in the repression of blue light responsive
CC promoter in chloroplasts. May be required to stabilize the CDD complex.
CC Its association with histone tail suggests a role in remodeling of
CC chromatin (PubMed:9681024, PubMed:15342494). Required for the
CC regulation of histone H2B monoubiquitination (H2Bub) over most genes by
CC controlling the stability of the deubiquitination module (DUB module)
CC (PubMed:30192741). {ECO:0000269|PubMed:15342494,
CC ECO:0000269|PubMed:30192741, ECO:0000269|PubMed:9681024}.
CC -!- SUBUNIT: Component of the CDD complex, at least composed of COP10, DET1
CC and DDB1A (PubMed:15342494, PubMed:24563205). Interacts with DDB1A
CC (PubMed:12225661). Interacts with non-acetylated N-terminal tail of
CC histone H2B in a nucleosome context (PubMed:12225670).
CC {ECO:0000269|PubMed:12225661, ECO:0000269|PubMed:12225670,
CC ECO:0000269|PubMed:15342494, ECO:0000269|PubMed:24563205}.
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 DET1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB59299.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAC62814.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB39770.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78141.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; L33695; AAB59299.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF096373; AAC62814.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL049487; CAB39770.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161516; CAB78141.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82852.1; -; Genomic_DNA.
DR EMBL; BT015348; AAU05471.1; -; mRNA.
DR EMBL; BT020454; AAW30032.1; -; mRNA.
DR PIR; A54841; A54841.
DR RefSeq; NP_192756.2; NM_117086.4.
DR AlphaFoldDB; P48732; -.
DR BioGRID; 11908; 24.
DR IntAct; P48732; 2.
DR STRING; 3702.AT4G10180.1; -.
DR PaxDb; P48732; -.
DR PRIDE; P48732; -.
DR ProteomicsDB; 224206; -.
DR EnsemblPlants; AT4G10180.1; AT4G10180.1; AT4G10180.
DR GeneID; 826609; -.
DR Gramene; AT4G10180.1; AT4G10180.1; AT4G10180.
DR KEGG; ath:AT4G10180; -.
DR Araport; AT4G10180; -.
DR TAIR; locus:2005505; AT4G10180.
DR eggNOG; KOG2558; Eukaryota.
DR HOGENOM; CLU_036725_1_0_1; -.
DR InParanoid; P48732; -.
DR OMA; AFSYVFF; -.
DR OrthoDB; 603320at2759; -.
DR PhylomeDB; P48732; -.
DR PRO; PR:P48732; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P48732; baseline and differential.
DR Genevisible; P48732; AT.
DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IMP:TAIR.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0009585; P:red, far-red light phototransduction; IEA:UniProtKB-KW.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR019138; De-etiolated_protein_1_Det1.
DR PANTHER; PTHR13374; PTHR13374; 1.
DR Pfam; PF09737; Det1; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phytochrome signaling pathway; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..543
FT /note="Light-mediated development protein DET1"
FT /id="PRO_0000129028"
FT REGION 246..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 421..436
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 492..510
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
SQ SEQUENCE 543 AA; 62492 MW; D38354984D5F646A CRC64;
MFTSGNVTAR VFERQIRTPP PGASVNRARH FYENLVPSYT LYDVESPDHC FRKFTEDGLF
LISFSRNHQE LIVYRPSWLT YSTTDDSTTT LPPLPRRASK FDSFFTQLYS VNLASSNELI
CKDFFLYHQT RRFGLFATST AQIHDSSSPS NDAVPGVPSI DKITFVLLRL DDGVVLDERV
FLHDFVNLAH NMGVFLYDDL LAILSLRYQR IHLLQIRDSG HLVDARAIGY FCREDDELFL
NSSSQAMMSQ DKSKQQSLSG SKEDDTGENG LRHSLSQPSG SNSFLSGVKQ RLLSFIFREI
WNEESDNVMR VQSLKKKFYF HFQDYVDLII WKVQFLDRQH LLIKFGSVDG GVTRSADHHP
AFFAVYNMET TDIVAFYQNS AEDLYQLFEQ FSDHFTVSSS TPFMNFVTSH SNNVYALEQL
KYTKNKSNSF SQFVKKMLLS LPFSCQSQSP SPYFDQSLFR FDEKLISAAD RHRQSSDNPI
KFISRRQPQT LKFKIKPGPE CGTADGRSKK ICSFLFHPHL PLAISIQQTL FMPPSVVNIH
FRR
