BZIP9_ARATH
ID BZIP9_ARATH Reviewed; 277 AA.
AC Q9FUD3;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Basic leucine zipper 9;
DE Short=AtbZIP9;
DE Short=bZIP protein 9;
DE AltName: Full=Basic leucine zipper OPAQUE 2 homolog 2;
DE Short=Basic leucine zipper O2 homolog 2;
GN Name=BZIP9; Synonyms=BZO2H2; OrderedLocusNames=At5g24800; ORFNames=F6A4.10;
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], AND GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=12569427; DOI=10.1007/s00239-002-2386-1;
RA Vincentz M., Bandeira-Kobarg C., Gauer L., Schloegl P., Leite A.;
RT "Evolutionary pattern of angiosperm bZIP factors homologous to the maize
RT Opaque2 regulatory protein.";
RL J. Mol. Evol. 56:105-116(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 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 [5]
RP TISSUE SPECIFICITY, AND GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=12657652; DOI=10.1074/jbc.m210538200;
RA Lara P., Onate-Sanchez L., Abraham Z., Ferrandiz C., Diaz I., Carbonero P.,
RA Vicente-Carbajosa J.;
RT "Synergistic activation of seed storage protein gene expression in
RT Arabidopsis by ABI3 and two bZIPs related to OPAQUE2.";
RL J. Biol. Chem. 278:21003-21011(2003).
RN [6]
RP INTERACTION WITH BZIP53.
RX PubMed=16810321; DOI=10.1038/sj.emboj.7601206;
RA Weltmeier F., Ehlert A., Mayer C.S., Dietrich K., Wang X., Schuetze K.,
RA Alonso R., Harter K., Vicente-Carbajosa J., Droege-Laser W.;
RT "Combinatorial control of Arabidopsis proline dehydrogenase transcription
RT by specific heterodimerisation of bZIP transcription factors.";
RL EMBO J. 25:3133-3143(2006).
RN [7]
RP SUBUNIT.
RX PubMed=16731568; DOI=10.1093/molbev/msl022;
RA Deppmann C.D., Alvania R.S., Taparowsky E.J.;
RT "Cross-species annotation of basic leucine zipper factor interactions:
RT Insight into the evolution of closed interaction networks.";
RL Mol. Biol. Evol. 23:1480-1492(2006).
RN [8]
RP INTERACTION WITH BZIP1; BZIP2; BZIP10; BZIP11; BZIP25; BZIP44; BZIP53 AND
RP BZIP63.
RX PubMed=16709202; DOI=10.1111/j.1365-313x.2006.02731.x;
RA Ehlert A., Weltmeier F., Wang X., Mayer C.S., Smeekens S.,
RA Vicente-Carbajosa J., Droege-Laser W.;
RT "Two-hybrid protein-protein interaction analysis in Arabidopsis
RT protoplasts: establishment of a heterodimerization map of group C and group
RT S bZIP transcription factors.";
RL Plant J. 46:890-900(2006).
RN [9]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION BY GLUCOSE.
RC STRAIN=cv. Columbia;
RX PubMed=18841482; DOI=10.1007/s11103-008-9410-9;
RA Weltmeier F., Rahmani F., Ehlert A., Dietrich K., Schuetze K., Wang X.,
RA Chaban C., Hanson J., Teige M., Harter K., Vicente-Carbajosa J.,
RA Smeekens S., Droege-Laser W.;
RT "Expression patterns within the Arabidopsis C/S1 bZIP transcription factor
RT network: availability of heterodimerization partners controls gene
RT expression during stress response and development.";
RL Plant Mol. Biol. 69:107-119(2009).
RN [10]
RP PHOSPHORYLATION.
RX PubMed=20047775; DOI=10.1016/j.ejcb.2009.11.023;
RA Kirchler T., Briesemeister S., Singer M., Schuetze K., Keinath M.,
RA Kohlbacher O., Vicente-Carbajosa J., Teige M., Harter K., Chaban C.;
RT "The role of phosphorylatable serine residues in the DNA-binding domain of
RT Arabidopsis bZIP transcription factors.";
RL Eur. J. Cell Biol. 89:175-183(2010).
RN [11]
RP SUBUNIT.
RX PubMed=20080816; DOI=10.1093/mp/ssp115;
RA Kang S.G., Price J., Lin P.-C., Hong J.C., Jang J.-C.;
RT "The arabidopsis bZIP1 transcription factor is involved in sugar signaling,
RT protein networking, and DNA binding.";
RL Mol. Plant 3:361-373(2010).
CC -!- FUNCTION: Transcription factor. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with BZIP1, BZIP2, BZIP10, BZIP11,
CC BZIP25, BZIP44, BZIP53 and BZIP63. {ECO:0000269|PubMed:16709202,
CC ECO:0000269|PubMed:16731568, ECO:0000269|PubMed:16810321,
CC ECO:0000269|PubMed:20080816}.
CC -!- INTERACTION:
CC Q9FUD3; Q9FGX2: BZIP1; NbExp=3; IntAct=EBI-942633, EBI-942623;
CC Q9FUD3; O65683: BZIP11; NbExp=3; IntAct=EBI-942633, EBI-942769;
CC Q9FUD3; Q9SI15: BZIP2; NbExp=3; IntAct=EBI-942633, EBI-942735;
CC Q9FUD3; C0Z2L5: BZIP44; NbExp=3; IntAct=EBI-942633, EBI-942804;
CC Q9FUD3; Q29PT3: bZIP5; NbExp=3; IntAct=EBI-942633, EBI-15194487;
CC Q9FUD3; Q9LZP8: BZIP53; NbExp=5; IntAct=EBI-942633, EBI-942845;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, shoots, stems, young leaves,
CC and flowers, mostly in vascular tissues (e.g. phloem).
CC {ECO:0000269|PubMed:12657652, ECO:0000269|PubMed:18841482}.
CC -!- DEVELOPMENTAL STAGE: Present in silique vasculature and funiculi. In
CC the anthers, restricted to the connective tissue at pre- and post-
CC dehiscence stages and detected in the vascular tissue of the stamen
CC filament. {ECO:0000269|PubMed:18841482}.
CC -!- INDUCTION: Repressed by glucose. {ECO:0000269|PubMed:18841482}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:20047775}.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR EMBL; AF310223; AAG25728.1; -; mRNA.
DR EMBL; AF069716; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED93363.1; -; Genomic_DNA.
DR RefSeq; NP_568457.1; NM_122389.4.
DR AlphaFoldDB; Q9FUD3; -.
DR SMR; Q9FUD3; -.
DR BioGRID; 17824; 24.
DR IntAct; Q9FUD3; 19.
DR MINT; Q9FUD3; -.
DR STRING; 3702.AT5G24800.1; -.
DR PaxDb; Q9FUD3; -.
DR PRIDE; Q9FUD3; -.
DR ProteomicsDB; 240558; -.
DR EnsemblPlants; AT5G24800.1; AT5G24800.1; AT5G24800.
DR GeneID; 832549; -.
DR Gramene; AT5G24800.1; AT5G24800.1; AT5G24800.
DR KEGG; ath:AT5G24800; -.
DR Araport; AT5G24800; -.
DR TAIR; locus:2149403; AT5G24800.
DR eggNOG; ENOG502QV87; Eukaryota.
DR HOGENOM; CLU_057781_1_0_1; -.
DR InParanoid; Q9FUD3; -.
DR OMA; FNDASQH; -.
DR OrthoDB; 1446419at2759; -.
DR PhylomeDB; Q9FUD3; -.
DR PRO; PR:Q9FUD3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FUD3; baseline and differential.
DR Genevisible; Q9FUD3; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEP:UniProtKB.
DR CDD; cd14702; bZIP_plant_GBF1; 1.
DR InterPro; IPR020983; Basic_leucine-zipper_C.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR045314; bZIP_plant_GBF1.
DR InterPro; IPR046347; bZIP_sf.
DR Pfam; PF00170; bZIP_1; 1.
DR Pfam; PF12498; bZIP_C; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..277
FT /note="Basic leucine zipper 9"
FT /id="PRO_0000416559"
FT DOMAIN 120..183
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 73..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..141
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 148..162
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT MOTIF 124..131
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 118..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9M1G6"
SQ SEQUENCE 277 AA; 30409 MW; 003617E73298544F CRC64;
MDNHTAKDIG MKRSASELAL QEYLTTSPLD PCFDLMNRDY TCELRDSLLW SEGLFPAGPF
RDAQSSICEN LSADSPVSAN KPEVRGGVRR TTSGSSHVNS DDEDAETEAG QSEMTNDPND
LKRIRRMNSN RESAKRSRRR KQEYLVDLET QVDSLKGDNS TLYKQLIDAT QQFRSAGTNN
RVLKSDVETL RVKVKLAEDL VARGSLTSSL NQLLQTHLSP PSHSISSLHY TGNTSPAITV
HSDQSLFPGM TLSGQNSSPG LGNVSSEAVS CVSDIWP
