BZP16_ARATH
ID BZP16_ARATH Reviewed; 409 AA.
AC Q501B2; O82288;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=bZIP transcription factor 16 {ECO:0000305};
DE Short=AtbZIP16 {ECO:0000303|PubMed:11906833};
GN Name=BZIP16 {ECO:0000303|PubMed:11906833};
GN OrderedLocusNames=At2g35530 {ECO:0000312|Araport:AT2G35530};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF Clones.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Fujita M., Mizukado S., Seki M., Shinozaki K., Mitsuda N., Takiguchi Y.,
RA Takagi M.;
RT "ORF cloning and analysis of Arabidopsis transcription factor genes.";
RL Submitted (MAR-2009) 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, SUBUNIT, INTERACTION WITH BZIP68; 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 IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH BZIP68 AND
RP GBF1/BZIP41, SUBCELLULAR LOCATION, DISULFIDE BOND, AND MUTAGENESIS OF
RP CYS-330 AND CYS-358.
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 repressor in light-
CC regulated expression of LHCB2.4. Binds DNA as monomer. DNA-binding
CC 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 BZIP68 and
CC GBF1/BZIP41 (PubMed:18315949, PubMed:22718771). Heterodimers with
CC GBF2/BZIP54 and GBF3/BZIP55 (PubMed:18315949). Binds DNA as monomer and
CC forms homo- and heterodimers. The monomeric form is redox regulated
CC (PubMed:22718771). Interacts with GIP1 (PubMed:25387999).
CC {ECO:0000269|PubMed:18315949, ECO:0000269|PubMed:22718771,
CC ECO:0000269|PubMed:25387999}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18315949,
CC ECO:0000269|PubMed:22718771}.
CC -!- DOMAIN: The N-terminal region is necessary for its transcriptional
CC activity. {ECO:0000269|PubMed:18315949}.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC36168.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC005314; AAC36168.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC09118.1; -; Genomic_DNA.
DR EMBL; BT022055; AAY25467.1; -; mRNA.
DR EMBL; BT026441; ABH04548.1; -; mRNA.
DR EMBL; AB493577; BAH30415.1; -; mRNA.
DR PIR; G84769; G84769.
DR RefSeq; NP_850248.2; NM_179917.4.
DR AlphaFoldDB; Q501B2; -.
DR SMR; Q501B2; -.
DR IntAct; Q501B2; 4.
DR STRING; 3702.AT2G35530.1; -.
DR iPTMnet; Q501B2; -.
DR PaxDb; Q501B2; -.
DR PRIDE; Q501B2; -.
DR ProteomicsDB; 239130; -.
DR EnsemblPlants; AT2G35530.1; AT2G35530.1; AT2G35530.
DR GeneID; 818118; -.
DR Gramene; AT2G35530.1; AT2G35530.1; AT2G35530.
DR KEGG; ath:AT2G35530; -.
DR Araport; AT2G35530; -.
DR TAIR; locus:2062455; AT2G35530.
DR eggNOG; ENOG502QUJX; Eukaryota.
DR HOGENOM; CLU_036349_0_0_1; -.
DR InParanoid; Q501B2; -.
DR OMA; NMPAMGT; -.
DR OrthoDB; 1090552at2759; -.
DR PhylomeDB; Q501B2; -.
DR PRO; PR:Q501B2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q501B2; 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:0045893; P:positive regulation of transcription, DNA-templated; IDA: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; Nucleus; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..409
FT /note="bZIP transcription factor 16"
FT /id="PRO_0000435633"
FT DOMAIN 305..368
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..326
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 333..368
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 362..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 307..323
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000305|PubMed:22718771"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 330
FT /note="Interchain"
FT /evidence="ECO:0000305|PubMed:22718771"
FT MUTAGEN 330
FT /note="C->L: Greatly enhances DNA binding activity."
FT /evidence="ECO:0000269|PubMed:22718771"
FT MUTAGEN 358
FT /note="C->L: Slightly enhances DNA binding activity."
FT /evidence="ECO:0000269|PubMed:22718771"
SQ SEQUENCE 409 AA; 43109 MW; 5C687D6938077C67 CRC64;
MASNEMEKSS KEKEPKTPPP SSTAPPSSQE PSSAVSAGMA TPDWSGFQAY SPMPPPHGYV
ASSPQPHPYM WGVQHMMPPY GTPPHPYVAM YPPGGMYAHP SMPPGSYPYS PYAMPSPNGM
TEVSGNTTGG TDGDAKQSEV KEKLPIKRSR GSLGSLNMIT GKNNEPGKNS GASANGAYSK
SGESASDGSS EGSDGNSQND SGSGLDGKDA EAASENGGSA NGPQNGSAGT PILPVSQTVP
IMPMTAAGVP GPPTNLNIGM DYWGAPTSAG IPGMHGKVST PVPGVVAPGS RDGGHSQPWL
QDDRELKRQR RKQSNRESAR RSRLRKQAEC DELAQRAEVL NEENTNLRAE INKLKSQCEE
LTTENTSLKD QLSLFPPLEG ISMDNDHQEP DTNQTGAAER KVDSYKDST
