ID   BZP63_ARATH             Reviewed;         314 AA.
AC   B9DGI8; F4KA11; Q712P1; Q940U4; Q9FUD2; Q9LKT9;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   05-JUL-2017, entry version 76.
DE   RecName: Full=Basic leucine zipper 63;
DE            Short=AtbZIP63;
DE            Short=bZIP protein 63;
DE   AltName: Full=Basic leucine zipper OPAQUE 2 homolog 3;
DE            Short=Basic leucine zipper O2 homolog 3;
GN   Name=BZIP63; Synonyms=BZO2H3; OrderedLocusNames=At5g28770;
GN   ORFNames=T32B20.4;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
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.,
RA   Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
RA   Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
RA   Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
RA   Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
RA   Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
RA   Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
RA   Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
RA   Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
RA   Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
RA   Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
RA   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.,
RA   Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
RA   Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
RA   van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
RA   Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
RA   Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
RA   Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:823-826(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Portal (Araport);
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., 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] (ISOFORM 1).
RC   STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX   PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA   Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M.,
RA   Seki M., Shinozaki K.;
RT   "Analysis of multiple occurrences of alternative splicing events in
RT   Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL   DNA Res. 16:155-164(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-191 (ISOFORM 1/3), 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
RT   maize Opaque2 regulatory protein.";
RL   J. Mol. Evol. 56:105-116(2003).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 6-314 (ISOFORM 1), TISSUE SPECIFICITY,
RP   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.,
RA   Carbonero P., 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   [7]
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   [8]
RP   INTERACTION WITH LSD1.
RX   PubMed=15469500; DOI=10.1111/j.1365-313X.2004.02219.x;
RA   Walter M., Chaban C., Schuetze K., Batistic O., Weckermann K.,
RA   Naeke C., Blazevic D., Grefen C., Schumacher K., Oecking C.,
RA   Harter K., Kudla J.;
RT   "Visualization of protein interactions in living plant cells using
RT   bimolecular fluorescence complementation.";
RL   Plant J. 40:428-438(2004).
RN   [9]
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.,
RA   Schuetze K., Alonso R., Harter K., Vicente-Carbajosa J.,
RA   Droege-Laser W.;
RT   "Combinatorial control of Arabidopsis proline dehydrogenase
RT   transcription by specific heterodimerisation of bZIP transcription
RT   factors.";
RL   EMBO J. 25:3133-3143(2006).
RN   [10]
RP   SUBCELLULAR LOCATION.
RX   PubMed=16957775; DOI=10.1038/sj.emboj.7601312;
RA   Kaminaka H., Naeke C., Epple P., Dittgen J., Schuetze K., Chaban C.,
RA   Holt B.F. III, Merkle T., Schaefer E., Harter K., Dangl J.L.;
RT   "bZIP10-LSD1 antagonism modulates basal defense and cell death in
RT   Arabidopsis following infection.";
RL   EMBO J. 25:4400-4411(2006).
RN   [11]
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   [12]
RP   INTERACTION WITH BZIP1; BZIP2; BZIP9; BZIP10; BZIP11; BZIP44 AND
RP   BZIP53.
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
RT   group S bZIP transcription factors.";
RL   Plant J. 46:890-900(2006).
RN   [13]
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.,
RA   Wang X., Chaban C., Hanson J., Teige M., Harter K.,
RA   Vicente-Carbajosa J., Smeekens S., Droege-Laser W.;
RT   "Expression patterns within the Arabidopsis C/S1 bZIP transcription
RT   factor network: availability of heterodimerization partners controls
RT   gene expression during stress response and development.";
RL   Plant Mol. Biol. 69:107-119(2009).
RN   [14]
RP   PHOSPHORYLATION, AND MUTAGENESIS OF SER-160; SER-164 AND SER-168.
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
RT   domain of Arabidopsis bZIP transcription factors.";
RL   Eur. J. Cell Biol. 89:175-183(2010).
RN   [15]
RP   INTERACTION WITH BZIP1; BZIP10 AND BZIP25, AND 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
RT   signaling, protein networking, and DNA binding.";
RL   Mol. Plant 3:361-373(2010).
CC   -!- FUNCTION: Transcription factor. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Forms a heterodimer with LSD1, BZIP1, BZIP2,
CC       BZIP9, BZIP10, BZIP11, BZIP25, BZIP44 and BZIP53.
CC       {ECO:0000269|PubMed:16709202, ECO:0000269|PubMed:16731568,
CC       ECO:0000269|PubMed:16810321, ECO:0000269|PubMed:20080816}.
CC   -!- INTERACTION:
CC       Self; NbExp=2; IntAct=EBI-942713, EBI-942713;
CC       Q9FGX2:BZIP1; NbExp=4; IntAct=EBI-942713, EBI-942623;
CC       O65683:BZIP11; NbExp=4; IntAct=EBI-942713, EBI-942769;
CC       Q9SI15:BZIP2; NbExp=4; IntAct=EBI-942713, EBI-942735;
CC       C0Z2L5:BZIP44; NbExp=4; IntAct=EBI-942713, EBI-942804;
CC       Q9LZP8:BZIP53; NbExp=8; IntAct=EBI-942713, EBI-942845;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
CC       ProRule:PRU00978, ECO:0000269|PubMed:16957775}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=B9DGI8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=B9DGI8-2; Sequence=VSP_042641;
CC         Note=No experimental confirmation available.;
CC       Name=3;
CC         IsoId=B9DGI8-3; Sequence=VSP_042642, VSP_042643;
CC         Note=Derived from EST data. No experimental confirmation
CC         available.;
CC   -!- TISSUE SPECIFICITY: Expressed in roots, shoots, young leaves,
CC       pollen, and flowers. {ECO:0000269|PubMed:12657652,
CC       ECO:0000269|PubMed:18841482}.
CC   -!- DEVELOPMENTAL STAGE: Present in silique valves, vasculature and
CC       funiculi. {ECO:0000269|PubMed:18841482}.
CC   -!- INDUCTION: Strongly repressed by glucose.
CC       {ECO:0000269|PubMed:18841482}.
CC   -!- PTM: Phosphorylated. {ECO:0000269|PubMed:20047775}.
CC   -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF67360.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAC79656.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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DR   EMBL; AF262041; AAF67360.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED93832.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED93833.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED93834.1; -; Genomic_DNA.
DR   EMBL; AF446876; AAL38609.1; -; mRNA.
DR   EMBL; AY052688; AAK96592.1; -; mRNA.
DR   EMBL; AK317169; BAH19855.1; -; mRNA.
DR   EMBL; AF310224; AAG25729.1; -; mRNA.
DR   EMBL; AJ010858; CAC79656.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001031962.1; NM_001036885.2. [B9DGI8-3]
DR   RefSeq; NP_568508.2; NM_122760.4. [B9DGI8-1]
DR   RefSeq; NP_851088.1; NM_180757.3. [B9DGI8-2]
DR   UniGene; At.15754; -.
DR   ProteinModelPortal; B9DGI8; -.
DR   SMR; B9DGI8; -.
DR   BioGrid; 18262; 12.
DR   IntAct; B9DGI8; 10.
DR   STRING; 3702.AT5G28770.2; -.
DR   iPTMnet; B9DGI8; -.
DR   PaxDb; B9DGI8; -.
DR   EnsemblPlants; AT5G28770.2; AT5G28770.2; AT5G28770. [B9DGI8-1]
DR   GeneID; 832990; -.
DR   Gramene; AT5G28770.2; AT5G28770.2; AT5G28770. [B9DGI8-1]
DR   KEGG; ath:AT5G28770; -.
DR   Araport; AT5G28770; -.
DR   TAIR; locus:2184251; AT5G28770.
DR   eggNOG; ENOG410IIE6; Eukaryota.
DR   eggNOG; ENOG4111S51; LUCA.
DR   HOGENOM; HOG000240492; -.
DR   InParanoid; B9DGI8; -.
DR   OMA; GNAMNRC; -.
DR   OrthoDB; EOG09360JUP; -.
DR   PhylomeDB; B9DGI8; -.
DR   PRO; PR:B9DGI8; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   Genevisible; B9DGI8; AT.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR   GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; ISS:TAIR.
DR   GO; GO:0071215; P:cellular response to abscisic acid stimulus; IEP:TAIR.
DR   GO; GO:0071333; P:cellular response to glucose stimulus; IEP:UniProtKB.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   InterPro; IPR020983; Basic_leucine-zipper_C.
DR   InterPro; IPR004827; bZIP.
DR   Pfam; PF00170; bZIP_1; 1.
DR   Pfam; PF12498; bZIP_C; 2.
DR   SMART; SM00338; BRLZ; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Complete proteome; DNA-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    314       Basic leucine zipper 63.
FT                                /FTId=PRO_0000416560.
FT   DOMAIN      151    214       bZIP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00978}.
FT   REGION      153    172       Basic motif. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00978}.
FT   REGION      179    193       Leucine-zipper. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00978}.
FT   MOTIF       155    162       Nuclear localization signal 1.
FT                                {ECO:0000250}.
FT   MOTIF       295    302       Nuclear localization signal 2.
FT                                {ECO:0000250}.
FT   VAR_SEQ      90     96       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14593172}.
FT                                /FTId=VSP_042641.
FT   VAR_SEQ     227    250       MAEETVKRLTGFNPMFHNMPQIVS -> YFLLSLCLPKLAI
FT                                EACLFLAGENG (in isoform 3).
FT                                {ECO:0000305}.
FT                                /FTId=VSP_042642.
FT   VAR_SEQ     251    314       Missing (in isoform 3). {ECO:0000305}.
FT                                /FTId=VSP_042643.
FT   MUTAGEN     160    160       S->A: Normal DNA-binding.
FT                                {ECO:0000269|PubMed:20047775}.
FT   MUTAGEN     160    160       S->D: Reduced DNA-binding to C-box motif.
FT                                {ECO:0000269|PubMed:20047775}.
FT   MUTAGEN     164    164       S->A: Normal DNA-binding.
FT                                {ECO:0000269|PubMed:20047775}.
FT   MUTAGEN     164    164       S->D: Impaired DNA-binding to C-box
FT                                motif. {ECO:0000269|PubMed:20047775}.
FT   MUTAGEN     168    168       S->A: Normal DNA-binding.
FT                                {ECO:0000269|PubMed:20047775}.
FT   MUTAGEN     168    168       S->D: Impaired DNA-binding to C-box
FT                                motif. {ECO:0000269|PubMed:20047775}.
SQ   SEQUENCE   314 AA;  34311 MW;  37B85F20425DFF8B CRC64;
     MEKVFSDEEI SGNHHWSVNG MTSLNRSASE WAFNRFIQES SAAADDGEST TACGVSVSSP
     PNVPVDSEEY RAFLKSKLNL ACAAVAMKRG TFIKPQDTSG RSDNGGANES EQASLASSKA
     TPMMSSAITS GSELSGDEEE ADGETNMNPT NVKRVKRMLS NRESARRSRR RKQAHLSELE
     TQVSQLRVEN SKLMKGLTDV TQTFNDASVE NRVLKANIET LRAKVKMAEE TVKRLTGFNP
     MFHNMPQIVS TVSLPSETSN SPDTTSSQVT TPEIISSGNK GKALIGCKMN RTASMRRVES
     LEHLQKRIRS VGDQ
//