BBX22_ARATH
ID BBX22_ARATH Reviewed; 299 AA.
AC Q9SYM2; Q8RWG4;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=B-box zinc finger protein 22 {ECO:0000303|PubMed:19920209};
DE AltName: Full=Protein DOUBLE B-BOX 3 {ECO:0000303|PubMed:18540109};
DE AltName: Full=Protein LIGHT-REGULATED ZINC FINGER PROTEIN 1 {ECO:0000303|PubMed:18796637};
DE AltName: Full=Protein SALT TOLERANCE HOMOLOG 3;
GN Name=BBX22 {ECO:0000303|PubMed:19920209};
GN Synonyms=DBB3 {ECO:0000303|PubMed:18540109},
GN LZF1 {ECO:0000303|PubMed:18796637}, STH3; OrderedLocusNames=At1g78600;
GN ORFNames=T30F21.7;
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].
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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 FUNCTION, INTERACTION WITH HY5, SUBCELLULAR LOCATION, UBIQUITINATION BY
RP COP1, MUTAGENESIS OF ASP-20; ASP-72 AND ASP-81, AND DISRUPTION PHENOTYPE.
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 [7]
RP FUNCTION, INDUCTION BY LIGHT, AND DISRUPTION PHENOTYPE.
RX PubMed=18182030; DOI=10.1111/j.1365-313x.2008.03401.x;
RA Chang C.S., Li Y.H., Chen L.T., Chen W.C., Hsieh W.P., Shin J., Jane W.N.,
RA Chou S.J., Choi G., Hu J.M., Somerville S., Wu S.H.;
RT "LZF1, a HY5-regulated transcriptional factor, functions in Arabidopsis de-
RT etiolation.";
RL Plant J. 54:205-219(2008).
RN [8]
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 [9]
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 [10]
RP FUNCTION, AND DEGRADATION BY THE PROTEASOME.
RX PubMed=21427283; DOI=10.1104/pp.111.175042;
RA Chang C.S., Maloof J.N., Wu S.H.;
RT "COP1-mediated degradation of BBX22/LZF1 optimizes seedling development in
RT Arabidopsis.";
RL Plant Physiol. 156:228-239(2011).
CC -!- FUNCTION: Acts as positive regulator of seedling photomorphogenesis and
CC light-regulated inhibition of hypocotyl elongation, independently and
CC in concert with HY5 and BBX21 (PubMed:18540109, PubMed:18796637,
CC PubMed:18182030, PubMed:21427283). Acts as a positive regulator of de-
CC etiolation and influences chloroplast biogenesis and function through
CC regulation of genes encoding chloroplast proteins (PubMed:18182030).
CC Acts downstream of COP1 and plays an important role in early and long-
CC term adjustment of the shade avoidance syndrome (SAS) responses in
CC natural environments (PubMed:21070414). Regulates the expression of
CC genes responsive to light hormone signals which may contribute to
CC optimal seedling development (PubMed:21427283).
CC {ECO:0000269|PubMed:18182030, ECO:0000269|PubMed:18540109,
CC ECO:0000269|PubMed:18796637, ECO:0000269|PubMed:21070414,
CC ECO:0000269|PubMed:21427283}.
CC -!- SUBUNIT: Interacts with HY5. {ECO:0000269|PubMed:18796637}.
CC -!- INTERACTION:
CC Q9SYM2; O24646: HY5; NbExp=3; IntAct=EBI-1994217, EBI-301660;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18796637}.
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=Q9SYM2-1; Sequence=Displayed;
CC -!- INDUCTION: By light. {ECO:0000269|PubMed:18182030}.
CC -!- PTM: Ubiquitinated by COP1 in vitro (PubMed:18796637). COP1-mediated
CC degradation of BBX22 by the proteasome occurs in the dark and is
CC important for a precise skotomorphogenesis process and optimization of
CC seedling growth under short days conditions (PubMed:21427283).
CC {ECO:0000269|PubMed:18796637, ECO:0000269|PubMed:21427283}.
CC -!- DISRUPTION PHENOTYPE: Increased hypocotyl length under short day
CC conditions (PubMed:18796637). Delayed chloroplast development
CC (PubMed:18182030). {ECO:0000269|PubMed:18182030}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD30576.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007260; AAD30576.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE36125.1; -; Genomic_DNA.
DR EMBL; AY093108; AAM13107.1; -; mRNA.
DR EMBL; BT006324; AAP13432.1; -; mRNA.
DR EMBL; AY087387; AAM64937.1; -; mRNA.
DR PIR; F96814; F96814.
DR RefSeq; NP_565183.1; NM_106507.4. [Q9SYM2-1]
DR AlphaFoldDB; Q9SYM2; -.
DR SMR; Q9SYM2; -.
DR IntAct; Q9SYM2; 5.
DR PRIDE; Q9SYM2; -.
DR EnsemblPlants; AT1G78600.1; AT1G78600.1; AT1G78600. [Q9SYM2-1]
DR GeneID; 844196; -.
DR Gramene; AT1G78600.1; AT1G78600.1; AT1G78600. [Q9SYM2-1]
DR KEGG; ath:AT1G78600; -.
DR Araport; AT1G78600; -.
DR eggNOG; ENOG502QT4C; Eukaryota.
DR InParanoid; Q9SYM2; -.
DR OMA; FVPDISC; -.
DR PhylomeDB; Q9SYM2; -.
DR PRO; PR:Q9SYM2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SYM2; baseline and differential.
DR Genevisible; Q9SYM2; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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 Activator; Alternative splicing; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..299
FT /note="B-box zinc finger protein 22"
FT /id="PRO_0000113298"
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 143..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..290
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: No effect on the interaction with HY5."
FT MUTAGEN 72
FT /note="D->A: Abolishes interaction with HY5."
FT /evidence="ECO:0000269|PubMed:18796637"
FT MUTAGEN 81
FT /note="D->A: Abolishes interaction with HY5."
FT /evidence="ECO:0000269|PubMed:18796637"
SQ SEQUENCE 299 AA; 32864 MW; 0FDF266FE3CA451A CRC64;
MKIQCNVCEA AEATVLCCAD EAALCWACDE KIHAANKLAG KHQRVPLSAS ASSIPKCDIC
QEASGFFFCL QDRALLCRKC DVAIHTVNPH VSAHQRFLLT GIKVGLESID TGPSTKSSPT
NDDKTMETKP FVQSIPEPQK MAFDHHHHQQ QQEQQEGVIP GTKVNDQTST KLPLVSSGST
TGSIPQWQIE EIFGLTDFDQ SYEYMENNGS SKADTSRRGD SDSSSMMRSA EEDGEDNNNC
LGGETSWAVP QIQSPPTASG LNWPKHFHHH SVFVPDITSS TPYTGSSPNQ RVGKRRRRF
