ID BZP24_ARATH Reviewed; 227 AA.
AC Q8GTS1; Q9SV08;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 144.
DE RecName: Full=Basic leucine zipper 24 {ECO:0000303|PubMed:11906833};
DE Short=AtbZIP24 {ECO:0000303|PubMed:11906833};
DE Short=bZIP protein 24 {ECO:0000305};
GN Name=BZIP24 {ECO:0000303|PubMed:11906833};
GN OrderedLocusNames=At3g51960 {ECO:0000312|Araport:AT3G51960};
GN ORFNames=F4F15.70 {ECO:0000312|EMBL:CAB41316.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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 GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11906833; DOI=10.1016/s1360-1385(01)02223-3;
RA Jakoby M., Weisshaar B., Droege-Laser W., Vicente-Carbajosa J.,
RA Tiedemann J., Kroj T., Parcy F.;
RT "bZIP transcription factors in Arabidopsis.";
RL Trends Plant Sci. 7:106-111(2002).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION BY SALT STRESS.
RX PubMed=18703123; DOI=10.1016/j.gene.2008.07.017;
RA Popova O.V., Yang O., Dietz K.J., Golldack D.;
RT "Differential transcript regulation in Arabidopsis thaliana and the
RT halotolerant Lobularia maritima indicates genes with potential function in
RT plant salt adaptation.";
RL Gene 423:142-148(2008).
RN [7]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=19248824; DOI=10.1016/j.gene.2009.02.010;
RA Yang O., Popova O.V., Suethoff U., Lueking I., Dietz K.J., Golldack D.;
RT "The Arabidopsis basic leucine zipper transcription factor AtbZIP24
RT regulates complex transcriptional networks involved in abiotic stress
RT resistance.";
RL Gene 436:45-55(2009).
CC -!- FUNCTION: Transcription factor involved in the regulation of salt
CC stress response. Functions as a negative transcriptional regulator of
CC salt stress acclimation response by regulating cation homeostasis
CC (PubMed:18703123, PubMed:19248824). Negatively regulates the expression
CC of genes contributing to ion and osmotic homeostasis during salt
CC stress, such as the Na(+) transporter HKT1, the Na(+)/H(+) antiporter
CC SOS1, the aquaporin PIP2-1 and the glutamine synthetase GLN1-3. In
CC addition, targets genes with functions in plant growth and development,
CC such as argonaute 4 (AGO4) and cyclophilin 19 (CYP19)
CC (PubMed:19248824). {ECO:0000269|PubMed:18703123,
CC ECO:0000269|PubMed:19248824}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19248824}.
CC -!- INTERACTION:
CC Q8GTS1; Q8LBK6: GRXS15; NbExp=2; IntAct=EBI-2292496, EBI-4427398;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978,
CC ECO:0000269|PubMed:18703123, ECO:0000269|PubMed:19248824}. Cytoplasm
CC {ECO:0000269|PubMed:18703123, ECO:0000269|PubMed:19248824}.
CC Note=Targeted to the nucleus in salt stress conditions.
CC {ECO:0000269|PubMed:19248824}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=Q8GTS1-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in young leaves and cauline leaves.
CC {ECO:0000269|PubMed:19248824}.
CC -!- INDUCTION: Induced by salt stress (PubMed:18703123, PubMed:19248824).
CC Induced by osmotic stress (PubMed:19248824).
CC {ECO:0000269|PubMed:18703123, ECO:0000269|PubMed:19248824}.
CC -!- MISCELLANEOUS: Plants silencing BZIP24 show enhanced tolerance to salt
CC stress (PubMed:18703123, PubMed:19248824). Enhanced salt stress
CC tolerance in silencing plants is characterized by enhanced root and
CC leaves development and reduced sodium accumulation in plants
CC (PubMed:19248824). {ECO:0000269|PubMed:18703123,
CC ECO:0000269|PubMed:19248824}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB41316.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL049711; CAB41316.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE78869.1; -; Genomic_DNA.
DR EMBL; AK117629; BAC42285.1; -; mRNA.
DR EMBL; BT005422; AAO63842.1; -; mRNA.
DR PIR; T49075; T49075.
DR RefSeq; NP_850680.1; NM_180349.1. [Q8GTS1-1]
DR AlphaFoldDB; Q8GTS1; -.
DR SMR; Q8GTS1; -.
DR IntAct; Q8GTS1; 8.
DR STRING; 3702.Q8GTS1; -.
DR PaxDb; 3702-AT3G51960-2; -.
DR ProteomicsDB; 240443; -. [Q8GTS1-1]
DR EnsemblPlants; AT3G51960.1; AT3G51960.1; AT3G51960. [Q8GTS1-1]
DR GeneID; 824359; -.
DR Gramene; AT3G51960.1; AT3G51960.1; AT3G51960. [Q8GTS1-1]
DR KEGG; ath:AT3G51960; -.
DR Araport; AT3G51960; -.
DR TAIR; AT3G51960; BZIP24.
DR eggNOG; ENOG502R3UK; Eukaryota.
DR InParanoid; Q8GTS1; -.
DR PhylomeDB; Q8GTS1; -.
DR PRO; PR:Q8GTS1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8GTS1; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR GO; GO:1901001; P:negative regulation of response to salt stress; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd14686; bZIP; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR031106; C/EBP.
DR PANTHER; PTHR23334; CCAAT/ENHANCER BINDING PROTEIN; 1.
DR PANTHER; PTHR23334:SF20; CCAAT_ENHANCER-BINDING PROTEIN-RELATED; 1.
DR Pfam; PF07716; bZIP_2; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; Leucine zipper domain; 1.
DR PROSITE; PS50217; BZIP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; DNA-binding; Nucleus; Reference proteome;
KW Repressor; Stress response; Transcription; Transcription regulation.
FT CHAIN 1..227
FT /note="Basic leucine zipper 24"
FT /id="PRO_0000435722"
FT DOMAIN 94..160
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 44..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..118
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 122..129
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
SQ SEQUENCE 227 AA; 26091 MW; D977B43B7A10AB18 CRC64;
MFCCCKDCRG NQRVSNFDSL TGVFFGDLEF GPQNQRYIKM NEEEDKDQDR VTRGCSHTHS
CNPPGPEDAS HSHTCFHAHT HLIISDQQEN DHSDSSNKKR LCGNREAVRK YREKKKARTA
YLEDEVMRLQ SLNEQFLRKL QSQEMVETEL IRLRALLVEM QGKIEVELCS FSFQKQCNGS
GFVFKEDGCN LATSNMMCEA ARVECEEGQT LHDPIQSFVP QPPPFSR
//
