BZP19_ARATH
ID BZP19_ARATH Reviewed; 261 AA.
AC Q8VY76; O49611; Q8LD81;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Basic leucine zipper 19 {ECO:0000303|PubMed:11906833};
DE Short=AtbZIP19 {ECO:0000303|PubMed:11906833};
DE Short=bZIP protein 19 {ECO:0000305};
GN Name=BZIP19 {ECO:0000303|PubMed:11906833};
GN OrderedLocusNames=At4g35040 {ECO:0000312|Araport:AT4G35040};
GN ORFNames=M4E13.100 {ECO:0000312|EMBL:CAA17769.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 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 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, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20479230; DOI=10.1073/pnas.1004788107;
RA Assuncao A.G., Herrero E., Lin Y.F., Huettel B., Talukdar S., Smaczniak C.,
RA Immink R.G., van Eldik M., Fiers M., Schat H., Aarts M.G.;
RT "Arabidopsis thaliana transcription factors bZIP19 and bZIP23 regulate the
RT adaptation to zinc deficiency.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:10296-10301(2010).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=26306426; DOI=10.1111/tpj.12996;
RA Inaba S., Kurata R., Kobayashi M., Yamagishi Y., Mori I., Ogata Y.,
RA Fukao Y.;
RT "Identification of putative target genes of bZIP19, a transcription factor
RT essential for Arabidopsis adaptation to Zn deficiency in roots.";
RL Plant J. 84:323-334(2015).
CC -!- FUNCTION: Transcription factor involved in the response to zinc ion
CC deficiency. Binds to the consensus sequence 5'-[AG]TGTCGACA[CT]-3' also
CC called zinc deficiency response element (ZDRE). The ZDRE sequence is
CC conserved in the plant kingdom and present in the promoters of genes
CC that constitute the primary response to zinc deficiency, comprising
CC additional ZIP metal transporter genes (PubMed:20479230,
CC PubMed:26306426). Required for zinc accumulation in roots. Mediates the
CC expression of the zinc transporters ZIP3, ZIP4, ZIP5 and ZIP9 during
CC growth in zinc-deficient conditions. ZIP9 transporter is involved in
CC zinc uptake in roots (PubMed:26306426). {ECO:0000269|PubMed:20479230,
CC ECO:0000269|PubMed:26306426}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978,
CC ECO:0000269|PubMed:26306426}.
CC -!- INDUCTION: Induced by zinc deficiency. {ECO:0000269|PubMed:20479230}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions (PubMed:20479230, PubMed:26306426). Mutant seedlings grown
CC under normal conditions accumulate reduced levels of zinc in roots.
CC Mutant seedlings grown in zinc-depleted medium have reduced root length
CC (PubMed:26306426). {ECO:0000269|PubMed:20479230,
CC ECO:0000269|PubMed:26306426}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA17769.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80221.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL022023; CAA17769.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161586; CAB80221.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86454.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66094.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66095.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66096.1; -; Genomic_DNA.
DR EMBL; AY072386; AAL62378.1; -; mRNA.
DR EMBL; BT000160; AAN15479.1; -; mRNA.
DR EMBL; AY086153; AAM63358.1; -; mRNA.
DR PIR; T05774; T05774.
DR RefSeq; NP_001320139.1; NM_001342321.1.
DR RefSeq; NP_001328011.1; NM_001342323.1.
DR RefSeq; NP_001328012.1; NM_001342322.1.
DR RefSeq; NP_567974.1; NM_119670.5.
DR AlphaFoldDB; Q8VY76; -.
DR SMR; Q8VY76; -.
DR STRING; 3702.AT4G35040.1; -.
DR PaxDb; Q8VY76; -.
DR PRIDE; Q8VY76; -.
DR ProteomicsDB; 239104; -.
DR EnsemblPlants; AT4G35040.1; AT4G35040.1; AT4G35040.
DR EnsemblPlants; AT4G35040.2; AT4G35040.2; AT4G35040.
DR EnsemblPlants; AT4G35040.3; AT4G35040.3; AT4G35040.
DR EnsemblPlants; AT4G35040.4; AT4G35040.4; AT4G35040.
DR GeneID; 829656; -.
DR Gramene; AT4G35040.1; AT4G35040.1; AT4G35040.
DR Gramene; AT4G35040.2; AT4G35040.2; AT4G35040.
DR Gramene; AT4G35040.3; AT4G35040.3; AT4G35040.
DR Gramene; AT4G35040.4; AT4G35040.4; AT4G35040.
DR KEGG; ath:AT4G35040; -.
DR Araport; AT4G35040; -.
DR TAIR; locus:2131626; AT4G35040.
DR eggNOG; ENOG502QVJ4; Eukaryota.
DR HOGENOM; CLU_065260_1_0_1; -.
DR InParanoid; Q8VY76; -.
DR OMA; TGPENTH; -.
DR OrthoDB; 1088448at2759; -.
DR PhylomeDB; Q8VY76; -.
DR PRO; PR:Q8VY76; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8VY76; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0010043; P:response to zinc ion; IEP:TAIR.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR Pfam; PF07716; bZIP_2; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
PE 2: Evidence at transcript level;
KW DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..261
FT /note="Basic leucine zipper 19"
FT /id="PRO_0000435720"
FT DOMAIN 89..155
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..113
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 117..131
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 237..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 127
FT /note="V -> L (in Ref. 4; AAM63358)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 261 AA; 28666 MW; 604975EBEE1E3644 CRC64;
MEDGELDFSN QEVFSSSEMG ELPPSNCSMD SFFDGLLMDT NAACTHTHTC NPTGPENTHT
HTCFHVHTKI LPDESDEKVS TDDTAESCGK KGEKRPLGNR EAVRKYREKK KAKAASLEDE
VARLRAVNQQ LVKRLQNQAT LEAEVSRLKC LLVDLRGRID GEIGSFPYQK PMAANIPSFS
HMMNPCNVQC DDEVYCPQNV FGVNSQEGAS INDQGLSGCD FDQLQCMANQ NLNGNGNGSF
SNVNTSVSNK RKGGHRASRA V
