BBX21_ARATH
ID BBX21_ARATH Reviewed; 331 AA.
AC Q9LQZ7; C0SV33;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=B-box zinc finger protein 21 {ECO:0000303|PubMed:19920209};
DE Short=AtBBX21;
DE AltName: Full=Protein LONG HYPOCOTYL UNDER SHADE {ECO:0000303|PubMed:21070414};
DE AltName: Full=Protein SALT TOLERANCE HOMOLOG 2;
GN Name=BBX21 {ECO:0000303|PubMed:19920209};
GN Synonyms=LHUS {ECO:0000303|PubMed:21070414}, STH2;
GN OrderedLocusNames=At1g75540; ORFNames=F10A5.24;
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].
RA Fujita M., Mizukado S., Seki M., Shinozaki K., Mitsuda N., Takiguchi Y.,
RA Takagi M.;
RT "ORF cloning and analysis of Arabidopsis transcription factor genes.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, INTERACTION WITH COP1 AND HY5, SUBCELLULAR LOCATION, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF ASP-20; ASP-75 AND ASP-84.
RX PubMed=17965270; DOI=10.1105/tpc.107.054791;
RA Datta S., Hettiarachchi C., Johansson H., Holm M.;
RT "SALT TOLERANCE HOMOLOG2, a B-box protein in Arabidopsis that activates
RT transcription and positively regulates light-mediated development.";
RL Plant Cell 19:3242-3255(2007).
RN [5]
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 [6]
RP FUNCTION.
RX PubMed=21070414; DOI=10.1111/j.1365-313x.2010.04360.x;
RA Crocco C.D., Holm M., Yanovsky M.J., Botto J.F.;
RT "AtBBX21 and COP1 genetically interact in the regulation of shade
RT avoidance.";
RL Plant J. 64:551-562(2010).
RN [7]
RP FUNCTION, AND INTERACTION WITH BBX32 AND HY5.
RX PubMed=21632973; DOI=10.1104/pp.111.177139;
RA Holtan H.E., Bandong S., Marion C.M., Adam L., Tiwari S., Shen Y.,
RA Maloof J.N., Maszle D.R., Ohto M.A., Preuss S., Meister R., Petracek M.,
RA Repetti P.P., Reuber T.L., Ratcliffe O.J., Khanna R.;
RT "BBX32, an Arabidopsis B-Box protein, functions in light signaling by
RT suppressing HY5-regulated gene expression and interacting with
RT STH2/BBX21.";
RL Plant Physiol. 156:2109-2123(2011).
RN [8]
RP INTERACTION WITH FLZ1.
RX PubMed=24901469; DOI=10.1371/journal.pone.0099074;
RA Jamsheer K M., Laxmi A.;
RT "DUF581 is plant specific FCS-like zinc finger involved in protein-protein
RT interaction.";
RL PLoS ONE 9:E99074-E99074(2014).
CC -!- FUNCTION: Transcription activator that acts as positive regulator of
CC seedling photomorphogenesis (PubMed:17965270). Acts downstream of COP1
CC and play an important role in early and long-term adjustment of the
CC shade avoidance syndrome (SAS) responses in natural environments
CC (PubMed:21070414). {ECO:0000269|PubMed:17965270,
CC ECO:0000269|PubMed:21070414}.
CC -!- SUBUNIT: Interacts with COP1, HY5 and BBX32. Interacts with FLZ1
CC (PubMed:24901469). {ECO:0000269|PubMed:17965270,
CC ECO:0000269|PubMed:21632973, ECO:0000269|PubMed:24901469}.
CC -!- INTERACTION:
CC Q9LQZ7; O24646: HY5; NbExp=4; IntAct=EBI-1994459, EBI-301660;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17965270}.
CC -!- DISRUPTION PHENOTYPE: Enhanced number of emerged lateral roots.
CC {ECO:0000269|PubMed:17965270}.
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DR EMBL; AC006434; AAF87126.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35731.1; -; Genomic_DNA.
DR EMBL; AB493536; BAH30374.1; -; mRNA.
DR PIR; G96785; G96785.
DR RefSeq; NP_177686.1; NM_106207.4.
DR AlphaFoldDB; Q9LQZ7; -.
DR SMR; Q9LQZ7; -.
DR BioGRID; 29109; 7.
DR IntAct; Q9LQZ7; 5.
DR STRING; 3702.AT1G75540.1; -.
DR iPTMnet; Q9LQZ7; -.
DR PaxDb; Q9LQZ7; -.
DR PRIDE; Q9LQZ7; -.
DR ProteomicsDB; 241208; -.
DR EnsemblPlants; AT1G75540.1; AT1G75540.1; AT1G75540.
DR GeneID; 843890; -.
DR Gramene; AT1G75540.1; AT1G75540.1; AT1G75540.
DR KEGG; ath:AT1G75540; -.
DR Araport; AT1G75540; -.
DR TAIR; locus:2005624; AT1G75540.
DR eggNOG; ENOG502QUWE; Eukaryota.
DR HOGENOM; CLU_025298_4_0_1; -.
DR InParanoid; Q9LQZ7; -.
DR OMA; DICQDKK; -.
DR OrthoDB; 1160515at2759; -.
DR PhylomeDB; Q9LQZ7; -.
DR PRO; PR:Q9LQZ7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LQZ7; baseline and differential.
DR Genevisible; Q9LQZ7; 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:0009640; P:photomorphogenesis; IBA:GO_Central.
DR GO; GO:0010117; P:photoprotection; IMP:TAIR.
DR GO; GO:1905157; P:positive regulation of photosynthesis; IMP:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:TAIR.
DR GO; GO:0009641; P:shade avoidance; IMP:TAIR.
DR InterPro; IPR000315; Znf_B-box.
DR Pfam; PF00643; zf-B_box; 2.
DR SMART; SM00336; BBOX; 2.
DR PROSITE; PS50119; ZF_BBOX; 2.
PE 1: Evidence at protein level;
KW Activator; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..331
FT /note="B-box zinc finger protein 21"
FT /id="PRO_0000113297"
FT ZN_FING 5..47
FT /note="B box-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 60..102
FT /note="B box-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 115..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..241
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 34
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MUTAGEN 20
FT /note="D->A: Abolishes interaction with HY5."
FT /evidence="ECO:0000269|PubMed:17965270"
FT MUTAGEN 75
FT /note="D->A: Abolishes interaction with HY5."
FT /evidence="ECO:0000269|PubMed:17965270"
FT MUTAGEN 84
FT /note="D->A: Abolishes interaction with HY5."
FT /evidence="ECO:0000269|PubMed:17965270"
SQ SEQUENCE 331 AA; 36634 MW; 6C2C5A4707976DEA CRC64;
MKIRCDVCDK EEASVFCTAD EASLCGGCDH QVHHANKLAS KHLRFSLLYP SSSNTSSPLC
DICQDKKALL FCQQDRAILC KDCDSSIHAA NEHTKKHDRF LLTGVKLSAT SSVYKPTSKS
SSSSSSNQDF SVPGSSISNP PPLKKPLSAP PQSNKIQPFS KINGGDASVN QWGSTSTISE
YLMDTLPGWH VEDFLDSSLP TYGFSKSGDD DGVLPYMEPE DDNNTKRNNN NNNNNNNNTV
SLPSKNLGIW VPQIPQTLPS SYPNQYFSQD NNIQFGMYNK ETSPEVVSFA PIQNMKQQGQ
NNKRWYDDGG FTVPQITPPP LSSNKKFRSF W
