BBX25_ARATH
ID BBX25_ARATH Reviewed; 238 AA.
AC Q9SID1; Q9C558;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=B-box zinc finger protein 25 {ECO:0000303|PubMed:19920209};
DE AltName: Full=Protein SALT TOLERANCE HOMOLOG 1;
DE AltName: Full=Salt tolerance-like protein;
GN Name=BBX25 {ECO:0000303|PubMed:19920209}; Synonyms=STH, STH1;
GN OrderedLocusNames=At2g31380; ORFNames=T28P16.13;
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], INTERACTION WITH COP1, AND MUTAGENESIS OF
RP 234-VAL-PRO-235.
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 [2]
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 [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 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 [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 FUNCTION, INTERACTION WITH HY5, SUBCELLULAR LOCATION, DEGRADATION BY THE
RP PROTEASOME, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ASP-20 AND ASP-72.
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 [8]
RP INTERACTION WITH 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
CC (PubMed:18540109). BBX25/STH and BBX24/STO function as transcriptional
CC corepressors of HY5 activity, leading to the down-regulation of BBX22
CC expression. BBX25/STH acts additively with BBX24/STO during de-
CC etiolation and the hypocotyl shade avoidance response
CC (PubMed:23624715). {ECO:0000269|PubMed:18540109,
CC ECO:0000269|PubMed:23624715}.
CC -!- SUBUNIT: Interacts with COP1 WD40 domain (PubMed:11226162). Interacts
CC with HY5 (PubMed:23624715) and HYH (PubMed:23733077).
CC {ECO:0000269|PubMed:11226162, ECO:0000269|PubMed:23624715,
CC ECO:0000269|PubMed:23733077}.
CC -!- INTERACTION:
CC Q9SID1; P43254: COP1; NbExp=3; IntAct=EBI-631960, EBI-301649;
CC Q9SID1; O24646: HY5; NbExp=3; IntAct=EBI-631960, EBI-301660;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23624715}.
CC -!- PTM: COP1-mediated ubiquitination and subsequent proteasomal
CC degradation of BBX25/STH occurs in the dark.
CC {ECO:0000269|PubMed:23624715}.
CC -!- DISRUPTION PHENOTYPE: Reduced length of hypocotyls.
CC {ECO:0000269|PubMed:23624715}.
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DR EMBL; AF323666; AAK01658.1; -; mRNA.
DR EMBL; AC007169; AAD26481.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC08540.1; -; Genomic_DNA.
DR EMBL; AF325077; AAK17145.1; -; mRNA.
DR EMBL; AF370311; AAK44126.1; -; mRNA.
DR EMBL; AY063097; AAL34271.1; -; mRNA.
DR PIR; A84720; A84720.
DR RefSeq; NP_565722.1; NM_128695.4.
DR AlphaFoldDB; Q9SID1; -.
DR BioGRID; 3043; 8.
DR IntAct; Q9SID1; 7.
DR MINT; Q9SID1; -.
DR STRING; 3702.AT2G31380.1; -.
DR PaxDb; Q9SID1; -.
DR PRIDE; Q9SID1; -.
DR EnsemblPlants; AT2G31380.1; AT2G31380.1; AT2G31380.
DR GeneID; 817696; -.
DR Gramene; AT2G31380.1; AT2G31380.1; AT2G31380.
DR KEGG; ath:AT2G31380; -.
DR Araport; AT2G31380; -.
DR TAIR; locus:2061330; AT2G31380.
DR eggNOG; ENOG502QQIU; Eukaryota.
DR HOGENOM; CLU_025298_3_0_1; -.
DR InParanoid; Q9SID1; -.
DR OMA; SKEVKMN; -.
DR OrthoDB; 1378371at2759; -.
DR PhylomeDB; Q9SID1; -.
DR PRO; PR:Q9SID1; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SID1; baseline and differential.
DR Genevisible; Q9SID1; 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:0008270; F:zinc ion binding; IEA:InterPro.
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; 2.
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; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..238
FT /note="B-box zinc finger protein 25"
FT /id="PRO_0000113296"
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..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..238
FT /note="Interaction with COP1"
FT /evidence="ECO:0000269|PubMed:11226162"
FT COMPBIAS 115..133
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 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 20
FT /note="D->A: Abolishes interaction with HY5."
FT /evidence="ECO:0000269|PubMed:23624715"
FT MUTAGEN 72
FT /note="D->A: Abolishes interaction with HY5."
FT /evidence="ECO:0000269|PubMed:23624715"
FT MUTAGEN 234..235
FT /note="VP->AA: Abolishes interaction with COP1."
FT /evidence="ECO:0000269|PubMed:11226162"
SQ SEQUENCE 238 AA; 26657 MW; 1088617F55A003AF CRC64;
MKIQCDVCEK APATLICCAD EAALCAKCDV EVHAANKLAS KHQRLFLDSL STKFPPCDIC
LEKAAFIFCV EDRALLCRDC DEATHAPNTR SANHQRFLAT GIRVALSSTS CNQEVEKNHF
DPSNQQSLSK PPTQQPAAPS PLWATDEFFS YSDLDCSNKE KEQLDLGELD WLAEMGLFGD
QPDQEALPVA EVPELSFSHL AHAHSYNRPM KSNVPNKKQR LEYRYDDEEE HFLVPDLG
