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Basic leucine zipper 9 (AtbZIP9) (bZIP protein 9) (Basic leucine zipper OPAQUE 2 homolog 2) (Basic leucine zipper O2 homolog 2)

 BZIP9_ARATH             Reviewed;         277 AA.
Q9FUD3;
18-APR-2012, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
12-SEP-2018, entry version 122.
RecName: Full=Basic leucine zipper 9;
Short=AtbZIP9;
Short=bZIP protein 9;
AltName: Full=Basic leucine zipper OPAQUE 2 homolog 2;
Short=Basic leucine zipper O2 homolog 2;
Name=BZIP9; Synonyms=BZO2H2; OrderedLocusNames=At5g24800;
ORFNames=F6A4.10;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND GENE FAMILY.
STRAIN=cv. Columbia;
PubMed=12569427; DOI=10.1007/s00239-002-2386-1;
Vincentz M., Bandeira-Kobarg C., Gauer L., Schloegl P., Leite A.;
"Evolutionary pattern of angiosperm bZIP factors homologous to the
maize Opaque2 regulatory protein.";
J. Mol. Evol. 56:105-116(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130714; DOI=10.1038/35048507;
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis
thaliana.";
Nature 408:823-826(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
GENE FAMILY, AND NOMENCLATURE.
PubMed=11906833; DOI=10.1016/S1360-1385(01)02223-3;
Jakoby M., Weisshaar B., Droege-Laser W., Vicente-Carbajosa J.,
Tiedemann J., Kroj T., Parcy F.;
"bZIP transcription factors in Arabidopsis.";
Trends Plant Sci. 7:106-111(2002).
[5]
TISSUE SPECIFICITY, AND GENE FAMILY.
STRAIN=cv. Columbia;
PubMed=12657652; DOI=10.1074/jbc.M210538200;
Lara P., Onate-Sanchez L., Abraham Z., Ferrandiz C., Diaz I.,
Carbonero P., Vicente-Carbajosa J.;
"Synergistic activation of seed storage protein gene expression in
Arabidopsis by ABI3 and two bZIPs related to OPAQUE2.";
J. Biol. Chem. 278:21003-21011(2003).
[6]
INTERACTION WITH BZIP53.
PubMed=16810321; DOI=10.1038/sj.emboj.7601206;
Weltmeier F., Ehlert A., Mayer C.S., Dietrich K., Wang X.,
Schuetze K., Alonso R., Harter K., Vicente-Carbajosa J.,
Droege-Laser W.;
"Combinatorial control of Arabidopsis proline dehydrogenase
transcription by specific heterodimerisation of bZIP transcription
factors.";
EMBO J. 25:3133-3143(2006).
[7]
SUBUNIT.
PubMed=16731568; DOI=10.1093/molbev/msl022;
Deppmann C.D., Alvania R.S., Taparowsky E.J.;
"Cross-species annotation of basic leucine zipper factor interactions:
Insight into the evolution of closed interaction networks.";
Mol. Biol. Evol. 23:1480-1492(2006).
[8]
INTERACTION WITH BZIP1; BZIP2; BZIP10; BZIP11; BZIP25; BZIP44; BZIP53
AND BZIP63.
PubMed=16709202; DOI=10.1111/j.1365-313X.2006.02731.x;
Ehlert A., Weltmeier F., Wang X., Mayer C.S., Smeekens S.,
Vicente-Carbajosa J., Droege-Laser W.;
"Two-hybrid protein-protein interaction analysis in Arabidopsis
protoplasts: establishment of a heterodimerization map of group C and
group S bZIP transcription factors.";
Plant J. 46:890-900(2006).
[9]
TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION BY GLUCOSE.
STRAIN=cv. Columbia;
PubMed=18841482; DOI=10.1007/s11103-008-9410-9;
Weltmeier F., Rahmani F., Ehlert A., Dietrich K., Schuetze K.,
Wang X., Chaban C., Hanson J., Teige M., Harter K.,
Vicente-Carbajosa J., Smeekens S., Droege-Laser W.;
"Expression patterns within the Arabidopsis C/S1 bZIP transcription
factor network: availability of heterodimerization partners controls
gene expression during stress response and development.";
Plant Mol. Biol. 69:107-119(2009).
[10]
PHOSPHORYLATION.
PubMed=20047775; DOI=10.1016/j.ejcb.2009.11.023;
Kirchler T., Briesemeister S., Singer M., Schuetze K., Keinath M.,
Kohlbacher O., Vicente-Carbajosa J., Teige M., Harter K., Chaban C.;
"The role of phosphorylatable serine residues in the DNA-binding
domain of Arabidopsis bZIP transcription factors.";
Eur. J. Cell Biol. 89:175-183(2010).
[11]
SUBUNIT.
PubMed=20080816; DOI=10.1093/mp/ssp115;
Kang S.G., Price J., Lin P.-C., Hong J.C., Jang J.-C.;
"The arabidopsis bZIP1 transcription factor is involved in sugar
signaling, protein networking, and DNA binding.";
Mol. Plant 3:361-373(2010).
-!- FUNCTION: Transcription factor. {ECO:0000250}.
-!- SUBUNIT: Homodimer. Interacts with BZIP1, BZIP2, BZIP10, BZIP11,
BZIP25, BZIP44, BZIP53 and BZIP63. {ECO:0000269|PubMed:16709202,
ECO:0000269|PubMed:16731568, ECO:0000269|PubMed:16810321,
ECO:0000269|PubMed:20080816}.
-!- INTERACTION:
Q9FGX2:BZIP1; NbExp=3; IntAct=EBI-942633, EBI-942623;
O65683:BZIP11; NbExp=3; IntAct=EBI-942633, EBI-942769;
Q9SI15:BZIP2; NbExp=3; IntAct=EBI-942633, EBI-942735;
C0Z2L5:BZIP44; NbExp=3; IntAct=EBI-942633, EBI-942804;
Q29PT3:bZIP5; NbExp=3; IntAct=EBI-942633, EBI-15194487;
Q9LZP8:BZIP53; NbExp=5; IntAct=EBI-942633, EBI-942845;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00978}.
-!- TISSUE SPECIFICITY: Expressed in roots, shoots, stems, young
leaves, and flowers, mostly in vascular tissues (e.g. phloem).
{ECO:0000269|PubMed:12657652, ECO:0000269|PubMed:18841482}.
-!- DEVELOPMENTAL STAGE: Present in silique vasculature and funiculi.
In the anthers, restricted to the connective tissue at pre- and
post-dehiscence stages and detected in the vascular tissue of the
stamen filament. {ECO:0000269|PubMed:18841482}.
-!- INDUCTION: Repressed by glucose. {ECO:0000269|PubMed:18841482}.
-!- PTM: Phosphorylated. {ECO:0000269|PubMed:20047775}.
-!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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EMBL; AF310223; AAG25728.1; -; mRNA.
EMBL; AF069716; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CP002688; AED93363.1; -; Genomic_DNA.
RefSeq; NP_568457.1; NM_122389.4.
UniGene; At.25540; -.
UniGene; At.49059; -.
ProteinModelPortal; Q9FUD3; -.
BioGrid; 17824; 13.
IntAct; Q9FUD3; 18.
MINT; Q9FUD3; -.
STRING; 3702.AT5G24800.1; -.
PaxDb; Q9FUD3; -.
EnsemblPlants; AT5G24800.1; AT5G24800.1; AT5G24800.
GeneID; 832549; -.
Gramene; AT5G24800.1; AT5G24800.1; AT5G24800.
KEGG; ath:AT5G24800; -.
Araport; AT5G24800; -.
TAIR; locus:2149403; AT5G24800.
eggNOG; ENOG410IWNP; Eukaryota.
eggNOG; ENOG410YMIG; LUCA.
HOGENOM; HOG000240492; -.
InParanoid; Q9FUD3; -.
OMA; DLMNRDY; -.
OrthoDB; EOG09360IU0; -.
PhylomeDB; Q9FUD3; -.
PRO; PR:Q9FUD3; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q9FUD3; baseline and differential.
Genevisible; Q9FUD3; AT.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
GO; GO:0046982; F:protein heterodimerization activity; IPI:TAIR.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0071333; P:cellular response to glucose stimulus; IEP:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR020983; Basic_leucine-zipper_C.
InterPro; IPR004827; bZIP.
Pfam; PF00170; bZIP_1; 1.
Pfam; PF12498; bZIP_C; 1.
SMART; SM00338; BRLZ; 1.
PROSITE; PS50217; BZIP; 1.
PROSITE; PS00036; BZIP_BASIC; 1.
1: Evidence at protein level;
Complete proteome; DNA-binding; Nucleus; Phosphoprotein;
Reference proteome; Transcription; Transcription regulation.
CHAIN 1 277 Basic leucine zipper 9.
/FTId=PRO_0000416559.
DOMAIN 120 183 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 122 141 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 148 162 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
MOTIF 124 131 Nuclear localization signal.
{ECO:0000250}.
MOD_RES 100 100 Phosphoserine.
{ECO:0000250|UniProtKB:Q9M1G6}.
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


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