BBX24_ARATH
ID BBX24_ARATH Reviewed; 248 AA.
AC Q96288;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=B-box zinc finger protein 24 {ECO:0000303|PubMed:19920209};
DE AltName: Full=Salt tolerance protein;
GN Name=BBX24 {ECO:0000303|PubMed:19920209}; Synonyms=STO;
GN OrderedLocusNames=At1g06040; ORFNames=T21E18.8, T21E18.9;
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 [MRNA].
RC TISSUE=Aerial part;
RX PubMed=8662738; DOI=10.1074/jbc.271.22.12859;
RA Lippuner V., Cyert M.S., Gasser C.S.;
RT "Two classes of plant cDNA clones differentially complement yeast
RT calcineurin mutants and increase salt tolerance of wild-type yeast.";
RL J. Biol. Chem. 271:12859-12866(1996).
RN [2]
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 [3]
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 [4]
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 [5]
RP INTERACTION WITH RCD1.
RX PubMed=11018516; DOI=10.1016/s0014-5793(00)02016-0;
RA Belles-Boix E., Babiychuk E., Van Montagu M., Inze D., Kushnir S.;
RT "CEO1, a new protein from Arabidopsis thaliana, protects yeast against
RT oxidative damage.";
RL FEBS Lett. 482:19-24(2000).
RN [6]
RP INTERACTION WITH COP1.
RC TISSUE=Etiolated seedling;
RX PubMed=11226162; DOI=10.1093/emboj/20.1.118;
RA Holm M., Hardtke C.S., Gaudet R., Deng X.-W.;
RT "Identification of a structural motif that confers specific interaction
RT with the WD40 repeat domain of Arabidopsis COP1.";
RL EMBO J. 20:118-127(2001).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND INTERACTION WITH TRP4.
RX PubMed=12909688; DOI=10.1093/jxb/erg241;
RA Nagaoka S., Takano T.;
RT "Salt tolerance-related protein STO binds to a Myb transcription factor
RT homologue and confers salt tolerance in Arabidopsis.";
RL J. Exp. Bot. 54:2231-2237(2003).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17605755; DOI=10.1111/j.1365-313x.2007.03162.x;
RA Indorf M., Cordero J., Neuhaus G., Rodriguez-Franco M.;
RT "Salt tolerance (STO), a stress-related protein, has a major role in light
RT signalling.";
RL Plant J. 51:563-574(2007).
RN [9]
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 [10]
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 [11]
RP FUNCTION, INTERACTION WITH COP1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP LYS-226 AND 244-VAL-PRO-245.
RX PubMed=21685177; DOI=10.1104/pp.111.180208;
RA Yan H., Marquardt K., Indorf M., Jutt D., Kircher S., Neuhaus G.,
RA Rodriguez-Franco M.;
RT "Nuclear localization and interaction with COP1 are required for STO/BBX24
RT function during photomorphogenesis.";
RL Plant Physiol. 156:1772-1782(2011).
RN [12]
RP FUNCTION, INTERACTION WITH COP1 AND HY5, AND DISRUPTION PHENOTYPE.
RX PubMed=22410790; DOI=10.1038/cr.2012.34;
RA Jiang L., Wang Y., Li Q.F., Bjorn L.O., He J.X., Li S.S.;
RT "Arabidopsis STO/BBX24 negatively regulates UV-B signaling by interacting
RT with COP1 and repressing HY5 transcriptional activity.";
RL Cell Res. 22:1046-1057(2012).
RN [13]
RP FUNCTION.
RX PubMed=23624715; DOI=10.1105/tpc.113.109751;
RA Gangappa S.N., Crocco C.D., Johansson H., Datta S., Hettiarachchi C.,
RA Holm M., Botto J.F.;
RT "The Arabidopsis B-BOX protein BBX25 interacts with HY5, negatively
RT regulating BBX22 expression to suppress seedling photomorphogenesis.";
RL Plant Cell 25:1243-1257(2013).
RN [14]
RP INTERACTION WITH HY5 AND HYH.
RX PubMed=23733077; DOI=10.4161/psb.25208;
RA Gangappa S.N., Holm M., Botto J.F.;
RT "Molecular interactions of BBX24 and BBX25 with HYH, HY5 HOMOLOG, to
RT modulate Arabidopsis seedling development.";
RL Plant Signal. Behav. 8:0-0(2013).
CC -!- FUNCTION: Acts as negative regulator of seedling photomorphogenesis and
CC light-regulated inhibition of hypocotyl elongation (PubMed:17605755,
CC PubMed:18540109, PubMed:21685177). BBX24/STO and BBX25/STH function as
CC transcriptional corepressors of HY5 activity, leading to the down-
CC regulation of BBX22 expression. BBX24/STO acts additively with
CC BBX25/STH during de-etiolation and the hypocotyl shade avoidance
CC response (PubMed:23624715). Functions as negative regulator of
CC photomorphogenic UV-B responses by interacting with both COP1 and HY5
CC (PubMed:22410790). May act as a transcription factor in the salt-stress
CC response (PubMed:12909688). {ECO:0000269|PubMed:12909688,
CC ECO:0000269|PubMed:17605755, ECO:0000269|PubMed:18540109,
CC ECO:0000269|PubMed:21685177, ECO:0000269|PubMed:22410790,
CC ECO:0000269|PubMed:23624715}.
CC -!- SUBUNIT: Interacts with COP1 WD40 domain (PubMed:11226162,
CC PubMed:21685177, PubMed:22410790). Interacts with HY5 (PubMed:22410790,
CC PubMed:23733077) and HYH (PubMed:23733077). Interacts with RCD1 and
CC TRP4 (PubMed:11018516, PubMed:12909688). {ECO:0000269|PubMed:11018516,
CC ECO:0000269|PubMed:11226162, ECO:0000269|PubMed:12909688,
CC ECO:0000269|PubMed:21685177, ECO:0000269|PubMed:22410790,
CC ECO:0000269|PubMed:23733077}.
CC -!- INTERACTION:
CC Q96288; O82617: BBX23; NbExp=3; IntAct=EBI-631943, EBI-15191793;
CC Q96288; Q6NLH4: BBX29; NbExp=4; IntAct=EBI-631943, EBI-15192709;
CC Q96288; Q8RY59: RCD1; NbExp=4; IntAct=EBI-631943, EBI-2118043;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12909688,
CC ECO:0000269|PubMed:17605755, ECO:0000269|PubMed:21685177}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q96288-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: High expression in leaves and lower in roots and
CC flowers.
CC -!- INDUCTION: Circadian regulation with a peak before dawn.
CC {ECO:0000269|PubMed:17605755}.
CC -!- PTM: COP1-mediated ubiquitination and subsequent proteasomal
CC degradation of BBX24/STO occurs in the dark.
CC {ECO:0000303|PubMed:21685177}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant seedlings show reduction of hypocotyls length
CC when grown under continuous blue light and a short primary root
CC phenotype under UV-B radiation. {ECO:0000269|PubMed:17605755,
CC ECO:0000269|PubMed:22410790}.
CC -!- MISCELLANEOUS: BBX24/STO expression is not changed in plants treated
CC with increasing salt concentrations. {ECO:0000269|PubMed:12909688}.
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DR EMBL; X95572; CAA64819.1; -; mRNA.
DR EMBL; AC024174; AAF80128.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27933.1; -; Genomic_DNA.
DR EMBL; AY079377; AAL85108.1; -; mRNA.
DR EMBL; AY045794; AAK76468.1; -; mRNA.
DR PIR; E86195; E86195.
DR RefSeq; NP_172094.1; NM_100484.4. [Q96288-1]
DR PDB; 6QTU; X-ray; 1.30 A; B=240-248.
DR PDBsum; 6QTU; -.
DR AlphaFoldDB; Q96288; -.
DR SMR; Q96288; -.
DR BioGRID; 22355; 15.
DR IntAct; Q96288; 12.
DR MINT; Q96288; -.
DR STRING; 3702.AT1G06040.1; -.
DR PaxDb; Q96288; -.
DR PRIDE; Q96288; -.
DR ProteomicsDB; 240849; -. [Q96288-1]
DR EnsemblPlants; AT1G06040.1; AT1G06040.1; AT1G06040. [Q96288-1]
DR GeneID; 837113; -.
DR Gramene; AT1G06040.1; AT1G06040.1; AT1G06040. [Q96288-1]
DR KEGG; ath:AT1G06040; -.
DR Araport; AT1G06040; -.
DR TAIR; locus:2198841; AT1G06040.
DR eggNOG; ENOG502QQIU; Eukaryota.
DR HOGENOM; CLU_025298_3_0_1; -.
DR InParanoid; Q96288; -.
DR OrthoDB; 1378371at2759; -.
DR PhylomeDB; Q96288; -.
DR PRO; PR:Q96288; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q96288; baseline and differential.
DR Genevisible; Q96288; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; ISS:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0003712; F:transcription coregulator activity; IDA:TAIR.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009640; P:photomorphogenesis; IBA:GO_Central.
DR GO; GO:0048573; P:photoperiodism, flowering; IMP:TAIR.
DR GO; GO:1902448; P:positive regulation of shade avoidance; IGI:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0009416; P:response to light stimulus; IEP:TAIR.
DR GO; GO:0090351; P:seedling development; IGI:TAIR.
DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP: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 3D-structure; Alternative splicing; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..248
FT /note="B-box zinc finger protein 24"
FT /id="PRO_0000113295"
FT ZN_FING 5..47
FT /note="B box-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 57..99
FT /note="B box-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 115..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..248
FT /note="Interaction with COP1"
FT /evidence="ECO:0000269|PubMed:11226162"
FT MOTIF 226..229
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:21685177"
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 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
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 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MUTAGEN 226
FT /note="K->N: Prevents nuclear import."
FT /evidence="ECO:0000269|PubMed:21685177"
FT MUTAGEN 244..245
FT /note="VP->AA: Abolishes interaction with COP1."
FT /evidence="ECO:0000269|PubMed:21685177"
SQ SEQUENCE 248 AA; 27641 MW; 4E7A960D56741B0A CRC64;
MKIQCDVCEK APATVICCAD EAALCPQCDI EIHAANKLAS KHQRLHLNSL STKFPRCDIC
QEKAAFIFCV EDRALLCRDC DESIHVANSR SANHQRFLAT GIKVALTSTI CSKEIEKNQP
EPSNNQQKAN QIPAKSTSQQ QQQPSSATPL PWAVDDFFHF SDIESTDKKG QLDLGAGELD
WFSDMGFFGD QINDKALPAA EVPELSVSHL GHVHSYKPMK SNVSHKKPRF ETRYDDDDEE
HFIVPDLG
