BBX20_ARATH
ID BBX20_ARATH Reviewed; 242 AA.
AC Q0IGM7; Q8GWF3; Q9SVI6;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=B-box zinc finger protein 20 {ECO:0000303|PubMed:19920209};
DE AltName: Full=Protein BZR1 SUPPRESSOR 1 {ECO:0000303|PubMed:22535582};
DE AltName: Full=Protein DOUBLE B-BOX 2;
DE AltName: Full=Protein SALT TOLERANCE HOMOLOG 7;
GN Name=BBX20 {ECO:0000303|PubMed:19920209};
GN Synonyms=BZS1 {ECO:0000303|PubMed:22535582}, DBB2, STH7;
GN OrderedLocusNames=At4g39070; ORFNames=F19H22.170;
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;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF Clones.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION.
RX PubMed=18796637; DOI=10.1105/tpc.108.061747;
RA Datta S., Johansson H., Hettiarachchi C., Irigoyen M.L., Desai M.,
RA Rubio V., Holm M.;
RT "LZF1/SALT TOLERANCE HOMOLOG3, an Arabidopsis B-box protein involved in
RT light-dependent development and gene expression, undergoes COP1-mediated
RT ubiquitination.";
RL Plant Cell 20:2324-2338(2008).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19920209; DOI=10.1105/tpc.109.069088;
RA Khanna R., Kronmiller B., Maszle D.R., Coupland G., Holm M., Mizuno T.,
RA Wu S.H.;
RT "The Arabidopsis B-box zinc finger family.";
RL Plant Cell 21:3416-3420(2009).
RN [7]
RP INTERACTION WITH MED25.
RX PubMed=21343311; DOI=10.1093/mp/ssr002;
RA Ou B., Yin K.Q., Liu S.N., Yang Y., Gu T., Wing Hui J.M., Zhang L.,
RA Miao J., Kondou Y., Matsui M., Gu H.Y., Qu L.J.;
RT "A high-throughput screening system for Arabidopsis transcription factors
RT and its application to Med25-dependent transcriptional regulation.";
RL Mol. Plant 4:546-555(2011).
RN [8]
RP FUNCTION, AND INTERACTION WITH COP1.
RX PubMed=22535582; DOI=10.1093/mp/sss041;
RA Fan X.Y., Sun Y., Cao D.M., Bai M.Y., Luo X.M., Yang H.J., Wei C.Q.,
RA Zhu S.W., Sun Y., Chong K., Wang Z.Y.;
RT "BZS1, a B-box protein, promotes photomorphogenesis downstream of both
RT brassinosteroid and light signaling pathways.";
RL Mol. Plant 5:591-600(2012).
CC -!- FUNCTION: Acts as positive regulator of seedling photomorphogenesis.
CC Plays a negative role in brassinosteroid responses.
CC {ECO:0000269|PubMed:22535582}.
CC -!- SUBUNIT: Interacts with MED25 (PubMed:21343311) and COP1
CC (PubMed:22535582). {ECO:0000269|PubMed:21343311,
CC ECO:0000269|PubMed:22535582}.
CC -!- INTERACTION:
CC Q0IGM7; O24646: HY5; NbExp=3; IntAct=EBI-15191597, EBI-301660;
CC Q0IGM7; A8MS70: HYH; NbExp=3; IntAct=EBI-15191597, EBI-15191595;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- PTM: COP1-mediated ubiquitination and subsequent proteasomal
CC degradation of BBX20 occurs in the dark. {ECO:0000303|PubMed:22535582}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB38827.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80570.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL035679; CAB38827.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161594; CAB80570.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE87014.1; -; Genomic_DNA.
DR EMBL; AK118879; BAC43464.1; -; mRNA.
DR EMBL; BT028893; ABI49440.1; -; mRNA.
DR PIR; T06067; T06067.
DR RefSeq; NP_195618.2; NM_120067.7.
DR AlphaFoldDB; Q0IGM7; -.
DR BioGRID; 15342; 14.
DR IntAct; Q0IGM7; 9.
DR STRING; 3702.AT4G39070.1; -.
DR PaxDb; Q0IGM7; -.
DR PRIDE; Q0IGM7; -.
DR EnsemblPlants; AT4G39070.1; AT4G39070.1; AT4G39070.
DR GeneID; 830062; -.
DR Gramene; AT4G39070.1; AT4G39070.1; AT4G39070.
DR KEGG; ath:AT4G39070; -.
DR Araport; AT4G39070; -.
DR TAIR; locus:2120207; AT4G39070.
DR eggNOG; ENOG502QUWE; Eukaryota.
DR HOGENOM; CLU_025298_4_1_1; -.
DR InParanoid; Q0IGM7; -.
DR OMA; GIEENYH; -.
DR OrthoDB; 1160515at2759; -.
DR PhylomeDB; Q0IGM7; -.
DR PRO; PR:Q0IGM7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q0IGM7; baseline and differential.
DR Genevisible; Q0IGM7; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:1900458; P:negative regulation of brassinosteroid mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0009640; P:photomorphogenesis; IBA:GO_Central.
DR GO; GO:2000306; P:positive regulation of photomorphogenesis; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0009741; P:response to brassinosteroid; IEP:TAIR.
DR InterPro; IPR000315; Znf_B-box.
DR Pfam; PF00643; zf-B_box; 1.
DR SMART; SM00336; BBOX; 2.
DR PROSITE; PS50119; ZF_BBOX; 2.
PE 1: Evidence at protein level;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..242
FT /note="B-box zinc finger protein 20"
FT /id="PRO_0000418140"
FT ZN_FING 5..47
FT /note="B box-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 58..100
FT /note="B box-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 112..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 5
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 8
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 28
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT CONFLICT 129
FT /note="T -> A (in Ref. 3; BAC43464)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 242 AA; 26780 MW; D7B7A81C3B6E8AD7 CRC64;
MKIWCAVCDK EEASVFCCAD EAALCNGCDR HVHFANKLAG KHLRFSLTSP TFKDAPLCDI
CGERRALLFC QEDRAILCRE CDIPIHQANE HTKKHNRFLL TGVKISASPS AYPRASNSNS
AAAFGRAKTR PKSVSSEVPS SASNEVFTSS SSTTTSNCYY GIEENYHHVS DSGSGSGCTG
SISEYLMETL PGWRVEDLLE HPSCVSYEDN IITNNNNSES YRVYDGSSQF HHQGFWDHKP
FS
