BBX18_ARATH
ID BBX18_ARATH Reviewed; 172 AA.
AC Q9SJU5; Q8W4S1;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=B-box zinc finger protein 18 {ECO:0000303|PubMed:19920209};
DE AltName: Full=Protein DOUBLE B-BOX 1A {ECO:0000303|PubMed:20872270};
DE AltName: Full=Protein SALT TOLERANCE HOMOLOG 4;
GN Name=BBX18 {ECO:0000303|PubMed:19920209};
GN Synonyms=DBB1A {ECO:0000303|PubMed:20872270}, STH4;
GN OrderedLocusNames=At2g21320 {ECO:0000312|Araport:AT2G21320};
GN ORFNames=F3K23.8;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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=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 FUNCTION.
RX PubMed=18540109; DOI=10.1271/bbb.80041;
RA Kumagai T., Ito S., Nakamichi N., Niwa Y., Murakami M., Yamashino T.,
RA Mizuno T.;
RT "The common function of a novel subfamily of B-Box zinc finger proteins
RT with reference to circadian-associated events in Arabidopsis thaliana.";
RL Biosci. Biotechnol. Biochem. 72:1539-1549(2008).
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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION BY BLUE
RP LIGHT.
RX PubMed=20872270; DOI=10.1007/s00425-010-1274-y;
RA Wang Q., Zeng J., Deng K., Tu X., Zhao X., Tang D., Liu X.;
RT "DBB1a, involved in gibberellin homeostasis, functions as a negative
RT regulator of blue light-mediated hypocotyl elongation in Arabidopsis.";
RL Planta 233:13-23(2011).
RN [7]
RP FUNCTION, AND INDUCTION BY HEAT SHOCK.
RX PubMed=23238922; DOI=10.1007/s11033-012-2354-9;
RA Wang Q., Tu X., Zhang J., Chen X., Rao L.;
RT "Heat stress-induced BBX18 negatively regulates the thermotolerance in
RT Arabidopsis.";
RL Mol. Biol. Rep. 40:2679-2688(2013).
CC -!- FUNCTION: Acts as negative regulator of seedling photomorphogenesis
CC (PubMed:18540109). Acts as a negative regulator of blue light-mediated
CC inhibition of hypocotyl elongation through increase of bioactive
CC gibberellin levels (PubMed:20872270). Acts as a repressor of
CC thermotolerance by modulating expression of a set of heat shock-
CC responsive genes (PubMed:23238922). {ECO:0000269|PubMed:18540109,
CC ECO:0000269|PubMed:20872270, ECO:0000269|PubMed:23238922}.
CC -!- INTERACTION:
CC Q9SJU5; Q8L500: APRR9; NbExp=3; IntAct=EBI-15192077, EBI-7920168;
CC Q9SJU5; C0SV91: At2g46670; NbExp=3; IntAct=EBI-15192077, EBI-15192193;
CC Q9SJU5; O22800-2: COL14; NbExp=3; IntAct=EBI-15192077, EBI-15192033;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20872270}.
CC -!- TISSUE SPECIFICITY: Expressed in vasculature of leaves and petioles.
CC {ECO:0000269|PubMed:20872270}.
CC -!- INDUCTION: By blue light (PubMed:20872270) and heat shock (at protein
CC level) (PubMed:23238922). {ECO:0000269|PubMed:20872270,
CC ECO:0000269|PubMed:23238922}.
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DR EMBL; AC006841; AAD23680.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC07159.1; -; Genomic_DNA.
DR EMBL; AY060570; AAL31199.1; -; mRNA.
DR EMBL; AY125573; AAM78083.1; -; mRNA.
DR PIR; H84599; H84599.
DR RefSeq; NP_565507.1; NM_127704.3.
DR AlphaFoldDB; Q9SJU5; -.
DR BioGRID; 2024; 14.
DR IntAct; Q9SJU5; 13.
DR STRING; 3702.AT2G21320.1; -.
DR PaxDb; Q9SJU5; -.
DR PRIDE; Q9SJU5; -.
DR ProteomicsDB; 240852; -.
DR EnsemblPlants; AT2G21320.1; AT2G21320.1; AT2G21320.
DR GeneID; 816671; -.
DR Gramene; AT2G21320.1; AT2G21320.1; AT2G21320.
DR KEGG; ath:AT2G21320; -.
DR Araport; AT2G21320; -.
DR TAIR; locus:2050130; AT2G21320.
DR eggNOG; ENOG502QZEK; Eukaryota.
DR HOGENOM; CLU_113487_0_0_1; -.
DR InParanoid; Q9SJU5; -.
DR OMA; HDHNMID; -.
DR OrthoDB; 1198657at2759; -.
DR PhylomeDB; Q9SJU5; -.
DR PRO; PR:Q9SJU5; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SJU5; baseline and differential.
DR Genevisible; Q9SJU5; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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:0070370; P:cellular heat acclimation; IMP:UniProtKB.
DR GO; GO:0071483; P:cellular response to blue light; IDA:UniProtKB.
DR GO; GO:0010100; P:negative regulation of photomorphogenesis; IDA:UniProtKB.
DR GO; GO:0009640; P:photomorphogenesis; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
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; Repressor;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..172
FT /note="B-box zinc finger protein 18"
FT /id="PRO_0000430585"
FT ZN_FING 5..47
FT /note="B box-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 56..96
FT /note="B box-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 119..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..151
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 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
SQ SEQUENCE 172 AA; 18891 MW; 90774B714E352633 CRC64;
MRILCDACES AAAIVFCAAD EAALCCSCDE KVHKCNKLAS RHLRVGLADP SNAPSCDICE
NAPAFFYCEI DGSSLCLQCD MVVHVGGKRT HRRFLLLRQR IEFPGDKPNH ADQLGLRCQK
ASSGRGQESN GNGDHDHNMI DLNSNPQRVH EPGSHNQEEG IDVNNANNHE HE
