ID   DDB1B_ARATH             Reviewed;        1088 AA.
AC   O49552; Q0WML4; Q570Q9;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 2.
DT   25-MAY-2022, entry version 152.
DE   RecName: Full=DNA damage-binding protein 1b {ECO:0000303|PubMed:12225661};
DE   AltName: Full=UV-damaged DNA-binding protein 1b {ECO:0000303|PubMed:12225661};
DE            Short=DDB1b {ECO:0000303|PubMed:12225661};
GN   Name=DDB1B {ECO:0000303|PubMed:12225661};
GN   OrderedLocusNames=At4g21100 {ECO:0000312|Araport:AT4G21100};
GN   ORFNames=F7J7.40 {ECO:0000312|EMBL:CAA17529.1};
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=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   [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   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   [4]
RP   IDENTIFICATION, AND POSSIBLE FUNCTION.
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   [5]
RP   INTERACTION WITH KTN80.2/DWA3.
RC   STRAIN=cv. Columbia;
RX   PubMed=21421380; DOI=10.1016/j.plantsci.2010.10.008;
RA   Lee J.-H., Terzaghi W., Deng X.W.;
RT   "DWA3, an Arabidopsis DWD protein, acts as a negative regulator in ABA
RT   signal transduction.";
RL   Plant Sci. 180:352-357(2011).
RN   [6]
RP   INTERACTION WITH HTD1.
RX   PubMed=25358503; DOI=10.14348/molcells.2014.0224;
RA   Kim S.-H., Lee J.-H., Seo K.-I., Ryu B., Sung Y., Chung T., Deng X.W.,
RA   Lee J.-H.;
RT   "Characterization of a novel DWD protein that participates in heat stress
RT   response in Arabidopsis.";
RL   Mol. Cells 37:833-840(2014).
RN   [7]
RP   INTERACTION WITH DDA1.
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).
CC   -!- FUNCTION: Component of light signal transduction machinery. Involved in
CC       repression of photomorphogenesis in darkness (By similarity). Plays a
CC       role in DNA repair by forming with DDB2 the UV-damaged DNA-binding
CC       protein complex (UV-DDB) (By similarity). {ECO:0000250}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with DDA1 (PubMed:24563205). Binds to KTN80.2/DWA3
CC       (PubMed:21421380). Interacts with HTD1 (PubMed:25358503).
CC       {ECO:0000269|PubMed:21421380, ECO:0000269|PubMed:24563205,
CC       ECO:0000269|PubMed:25358503}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DDB1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA17529.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB79110.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL021960; CAA17529.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161554; CAB79110.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE84401.1; -; Genomic_DNA.
DR   EMBL; AK220648; BAD95136.1; -; mRNA.
DR   EMBL; AK229805; BAF01636.1; -; mRNA.
DR   PIR; T04941; T04941.
DR   RefSeq; NP_193842.1; NM_118228.4.
DR   AlphaFoldDB; O49552; -.
DR   SMR; O49552; -.
DR   BioGRID; 13148; 55.
DR   DIP; DIP-46981N; -.
DR   IntAct; O49552; 2.
DR   STRING; 3702.AT4G21100.1; -.
DR   PaxDb; O49552; -.
DR   PRIDE; O49552; -.
DR   ProteomicsDB; 224662; -.
DR   EnsemblPlants; AT4G21100.1; AT4G21100.1; AT4G21100.
DR   GeneID; 827857; -.
DR   Gramene; AT4G21100.1; AT4G21100.1; AT4G21100.
DR   KEGG; ath:AT4G21100; -.
DR   Araport; AT4G21100; -.
DR   TAIR; locus:2127368; AT4G21100.
DR   eggNOG; KOG1897; Eukaryota.
DR   HOGENOM; CLU_002893_0_1_1; -.
DR   InParanoid; O49552; -.
DR   OMA; EMKGITH; -.
DR   OrthoDB; 146622at2759; -.
DR   PhylomeDB; O49552; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:O49552; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; O49552; baseline and differential.
DR   Genevisible; O49552; AT.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009585; P:red, far-red light phototransduction; IEA:UniProtKB-KW.
DR   Gene3D; 2.130.10.10; -; 3.
DR   InterPro; IPR004871; Cleavage/polyA-sp_fac_asu_C.
DR   InterPro; IPR018846; Cleavage/polyA-sp_fac_asu_N.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF03178; CPSF_A; 1.
DR   Pfam; PF10433; MMS1_N; 1.
DR   SUPFAM; SSF50978; SSF50978; 2.
PE   1: Evidence at protein level;
KW   DNA damage; DNA repair; DNA-binding; Nucleus;
KW   Phytochrome signaling pathway; Reference proteome.
FT   CHAIN           1..1088
FT                   /note="DNA damage-binding protein 1b"
FT                   /id="PRO_0000079838"
FT   CONFLICT        666
FT                   /note="N -> S (in Ref. 3; BAD95136)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        914
FT                   /note="T -> A (in Ref. 3; BAD95136)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1088 AA;  121179 MW;  11724075C9D5C7C3 CRC64;
     MSVWNYAVTA QKPTCVTHSC VGNFTSPQEL NLIVAKSTRI EIHLLSPQGL QTILDVPLYG
     RIATMELFRP HGEAQDFLFV ATERYKFCVL QWDYESSELI TRAMGDVSDR IGRPTDNGQI
     GIIDPDCRVI GLHLYDGLFK VIPFDNKGQL KEAFNIRLEE LQVLDIKFLY GCTKPTIAVL
     YQDNKDARHV KTYEVSLKDK NFVEGPWSQN NLDNGADLLI PVPSPLCGVL IIGEETIVYC
     SANAFKAIPI RPSITKAYGR VDLDGSRYLL GDHAGLIHLL VITHEKEKVT GLKIELLGET
     SIASSISYLD NAVVFVGSSY GDSQLIKLNL QPDAKGSYVE ILEKYVNLGP IVDFCVVDLE
     RQGQGQVVTC SGAYKDGSLR IVRNGIGINE QASVELQGIK GMWSLKSSID EAFDTFLVVS
     FISETRILAM NIEDELEETE IEGFLSEVQT LFCHDAVYNQ LVQVTSNSVR LVSSTTRELR
     NKWDAPAGFS VNVATANASQ VLLATGGGHL VYLEIGDGTL TEVKHVLLEY EVSCLDINPI
     GDNPNYSQLA AVGMWTDISV RIFVLPDLTL ITKEELGGEI IPRSVLLCAF EGISYLLCAL
     GDGHLLNFQL DTSCGKLRDR KKVSLGTRPI TLRTFSSKSA THVFAASDRP AVIYSNNKKL
     LYSNVNLKEV SHMCPFNSAA FPDSLAIARE GELTIGTIDD IQKLHIRTIP IGEHARRICH
     QEQTRTFAIS CLRNEPSAEE SESHFVRLLD AQSFEFLSSY PLDAFECGCS ILSCSFTDDK
     NVYYCVGTAY VLPEENEPTK GRILVFIVEE GRLQLITEKE TKGAVYSLNA FNGKLLASIN
     QKIQLYKWML RDDGTRELQS ECGHHGHILA LYVQTRGDFI AVGDLMKSIS LLIYKHEEGA
     IEERARDYNA NWMTAVEILN DDIYLGTDNC FNIFTVKKNN EGATDEERAR MEVVGEYHIG
     EFVNRFRHGS LVMKLPDSDI GQIPTVIFGT VSGMIGVIAS LPQEQYAFLE KLQTSLRKVI
     KGVGGLSHEQ WRSFNNEKRT AEAKGYLDGD LIESFLDLSR GKMEEISKGM DVQVEELCKR
     VEELTRLH