BZP68_ARATH
ID BZP68_ARATH Reviewed; 389 AA.
AC Q84LG2; Q9FVR0;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=bZIP transcription factor 68 {ECO:0000305};
DE Short=AtbZIP68 {ECO:0000303|PubMed:11906833};
GN Name=BZIP68 {ECO:0000303|PubMed:11906833};
GN OrderedLocusNames=At1g32150 {ECO:0000312|Araport:AT1G32150};
GN ORFNames=F3C3.7 {ECO:0000312|EMBL:AAG23442.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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=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 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 UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-154, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [6]
RP FUNCTION, SUBUNIT, INTERACTION WITH BZIP16; GBF1/BZIP41; GBF2/BZIP54 AND
RP GBF3/BZIP55, AND SUBCELLULAR LOCATION.
RX PubMed=18315949; DOI=10.5483/bmbrep.2008.41.2.132;
RA Shen H., Cao K., Wang X.;
RT "AtbZIP16 and AtbZIP68, two new members of GBFs, can interact with other G
RT group bZIPs in Arabidopsis thaliana.";
RL BMB Rep. 41:132-138(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [8]
RP FUNCTION, INTERACTION WITH BZIP16, DISULFIDE BOND, AND MUTAGENESIS OF
RP CYS-182 AND CYS-320.
RX PubMed=22718771; DOI=10.1074/jbc.m112.361394;
RA Shaikhali J., Noren L., de Dios Barajas-Lopez J., Srivastava V., Koenig J.,
RA Sauer U.H., Wingsle G., Dietz K.J., Strand A.;
RT "Redox-mediated mechanisms regulate DNA binding activity of the G-group of
RT basic region leucine zipper (bZIP) transcription factors in Arabidopsis.";
RL J. Biol. Chem. 287:27510-27525(2012).
RN [9]
RP INTERACTION WITH GIP1.
RX PubMed=25387999; DOI=10.1007/s00709-014-0726-9;
RA Shaikhali J.;
RT "GIP1 protein is a novel cofactor that regulates DNA-binding affinity of
RT redox-regulated members of bZIP transcription factors involved in the early
RT stages of Arabidopsis development.";
RL Protoplasma 252:867-883(2015).
CC -!- FUNCTION: Transcriptional activator that binds to the G-box motif (5'-
CC CACGTG-3') and other cis-acting elements with 5'-ACGT-3' core, such as
CC Hex, C-box and as-1 motifs. Possesses high binding affinity to G-box,
CC much lower affinity to Hex and C-box, and little affinity to as-1
CC element (PubMed:18315949). G-box and G-box-like motifs are cis-acting
CC elements defined in promoters of certain plant genes which are
CC regulated by such diverse stimuli as light-induction or hormone control
CC (Probable). Binds to the G-box motif 5'-CACGTG-3' of LHCB2.4
CC (At3g27690) promoter. May act as transcriptional activator in light-
CC regulated expression of LHCB2.4. Probably binds DNA as monomer. DNA-
CC binding activity is redox-dependent (PubMed:22718771).
CC {ECO:0000269|PubMed:18315949, ECO:0000269|PubMed:22718771,
CC ECO:0000305|PubMed:18315949}.
CC -!- SUBUNIT: Monomer, homodimer and heterodimers with GBF1/BZIP41,
CC GBF2/BZIP54 and GBF3/BZIP55 (PubMed:18315949). Heterodimers with BZIP16
CC (PubMed:18315949, PubMed:22718771). Interacts with GIP1
CC (PubMed:25387999). {ECO:0000269|PubMed:18315949,
CC ECO:0000269|PubMed:22718771, ECO:0000269|PubMed:25387999}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18315949}.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG23442.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC084165; AAG23442.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31441.1; -; Genomic_DNA.
DR EMBL; BT004147; AAO42168.1; -; mRNA.
DR PIR; H86445; H86445.
DR RefSeq; NP_174494.2; NM_102948.4.
DR AlphaFoldDB; Q84LG2; -.
DR SMR; Q84LG2; -.
DR IntAct; Q84LG2; 4.
DR STRING; 3702.AT1G32150.1; -.
DR iPTMnet; Q84LG2; -.
DR PaxDb; Q84LG2; -.
DR PRIDE; Q84LG2; -.
DR ProteomicsDB; 240446; -.
DR EnsemblPlants; AT1G32150.1; AT1G32150.1; AT1G32150.
DR GeneID; 840107; -.
DR Gramene; AT1G32150.1; AT1G32150.1; AT1G32150.
DR KEGG; ath:AT1G32150; -.
DR Araport; AT1G32150; -.
DR TAIR; locus:2031705; AT1G32150.
DR eggNOG; ENOG502QUJX; Eukaryota.
DR HOGENOM; CLU_036349_0_0_1; -.
DR InParanoid; Q84LG2; -.
DR OMA; IMPMSAV; -.
DR OrthoDB; 1090552at2759; -.
DR PhylomeDB; Q84LG2; -.
DR PRO; PR:Q84LG2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q84LG2; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:TAIR.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd14702; bZIP_plant_GBF1; 1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR045314; bZIP_plant_GBF1.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR044827; GBF-like.
DR InterPro; IPR012900; MFMR.
DR PANTHER; PTHR45967; PTHR45967; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR Pfam; PF07777; MFMR; 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 Activator; Disulfide bond; DNA-binding; Isopeptide bond; Nucleus;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..389
FT /note="bZIP transcription factor 68"
FT /id="PRO_0000435634"
FT DOMAIN 295..358
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..316
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 323..358
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 356..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 320
FT /note="Interchain"
FT /evidence="ECO:0000305|PubMed:22718771"
FT CROSSLNK 154
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:17272265"
FT MUTAGEN 182
FT /note="C->L: Slightly increases DNA binding activity."
FT /evidence="ECO:0000269|PubMed:22718771"
FT MUTAGEN 320
FT /note="C->L: Significantly increases DNA binding activity."
FT /evidence="ECO:0000269|PubMed:22718771"
SQ SEQUENCE 389 AA; 40868 MW; CDFBD3E348BE04CC CRC64;
MGSSEMEKSG KEKEPKTTPP STSSSAPATV VSQEPSSAVS AGVAVTQDWS GFQAYSPMPP
HGYVASSPQP HPYMWGVQHM MPPYGTPPHP YVTMYPPGGM YAHPSLPPGS YPYSPYAMPS
PNGMAEASGN TGSVIEGDGK PSDGKEKLPI KRSKGSLGSL NMIIGKNNEA GKNSGASANG
ACSKSAESGS DGSSDGSDAN SQNDSGSRHN GKDGETASES GGSAHGPPRN GSNLPVNQTV
AIMPVSATGV PGPPTNLNIG MDYWSGHGNV SGAVPGVVVD GSQSQPWLQV SDEREIKRQR
RKQSNRESAR RSRLRKQAEC DELAQRAEVL NGENSSLRAE INKLKSQYEE LLAENSSLKN
KFSSAPSLEG GDLDKNEQEP QRSTRQDVA
