GBF3_ARATH
ID GBF3_ARATH Reviewed; 382 AA.
AC P42776;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 25-MAY-2022, entry version 157.
DE RecName: Full=G-box-binding factor 3;
DE AltName: Full=bZIP transcription factor 55;
DE Short=AtbZIP55;
GN Name=GBF3; Synonyms=BZIP55; OrderedLocusNames=At2g46270; ORFNames=T3F17.8;
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], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=8672884; DOI=10.2307/3870287;
RA Lu G.H., Paul A.L., McCarty D.R., Ferl R.J.;
RT "Transcription factor veracity: is GBF3 responsible for ABA-regulated
RT expression of Arabidopsis Adh?";
RL Plant Cell 8:847-857(1996).
RN [2]
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 [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 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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 59-382.
RC STRAIN=cv. Columbia; TISSUE=Leaf, and Stem;
RX PubMed=1373374; DOI=10.1002/j.1460-2075.1992.tb05170.x;
RA Schindler U., Menkens A.E., Beckmann H., Ecker J.R., Cashmore A.R.;
RT "Heterodimerization between light-regulated and ubiquitously expressed
RT Arabidopsis GBF bZIP proteins.";
RL EMBO J. 11:1261-1273(1992).
RN [6]
RP INTERACTION WITH GBF4.
RC STRAIN=cv. Columbia;
RX PubMed=8146148; DOI=10.1073/pnas.91.7.2522;
RA Menkens A.E., Cashmore A.R.;
RT "Isolation and characterization of a fourth Arabidopsis thaliana G-box-
RT binding factor, which has similarities to Fos oncoprotein.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:2522-2526(1994).
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 BZIP16 AND BZIP68.
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).
CC -!- FUNCTION: Binds to the G-box motif (5'-CCACGTGG-3') of the rbcS-1A gene
CC promoter. G-box and G-box-like motifs are cis-acting elements defined
CC in promoters of certain plant genes which are regulated by such diverse
CC stimuli as light-induction or hormone control.
CC {ECO:0000269|PubMed:8672884}.
CC -!- SUBUNIT: DNA-binding heterodimer. Interacts with GBF4 (PubMed:8146148).
CC Interacts with BZIP16 and BZIP68 (PubMed:18315949).
CC {ECO:0000269|PubMed:18315949, ECO:0000269|PubMed:8146148}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978,
CC ECO:0000269|PubMed:8672884}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=P42776-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Present only in dark grown leaves and roots.
CC {ECO:0000269|PubMed:8672884}.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR EMBL; U17891; AAA90947.1; -; mRNA.
DR EMBL; U51850; AAB06611.1; -; mRNA.
DR EMBL; AC005397; AAC62879.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10667.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61227.1; -; Genomic_DNA.
DR EMBL; AF370307; AAK44122.1; -; mRNA.
DR EMBL; AY063093; AAL34267.1; -; mRNA.
DR EMBL; X63896; CAA45358.1; -; mRNA.
DR PIR; G84900; G84900.
DR PIR; S20885; S20885.
DR RefSeq; NP_001323457.1; NM_001337182.1. [P42776-1]
DR RefSeq; NP_182150.1; NM_130190.3. [P42776-1]
DR AlphaFoldDB; P42776; -.
DR SMR; P42776; -.
DR BioGRID; 4570; 6.
DR IntAct; P42776; 5.
DR STRING; 3702.AT2G46270.1; -.
DR iPTMnet; P42776; -.
DR PaxDb; P42776; -.
DR PRIDE; P42776; -.
DR ProteomicsDB; 222180; -. [P42776-1]
DR EnsemblPlants; AT2G46270.1; AT2G46270.1; AT2G46270. [P42776-1]
DR EnsemblPlants; AT2G46270.3; AT2G46270.3; AT2G46270. [P42776-1]
DR GeneID; 819235; -.
DR Gramene; AT2G46270.1; AT2G46270.1; AT2G46270. [P42776-1]
DR Gramene; AT2G46270.3; AT2G46270.3; AT2G46270. [P42776-1]
DR KEGG; ath:AT2G46270; -.
DR Araport; AT2G46270; -.
DR TAIR; locus:2063020; AT2G46270.
DR eggNOG; ENOG502QRCN; Eukaryota.
DR InParanoid; P42776; -.
DR OMA; PASAHMK; -.
DR OrthoDB; 1121126at2759; -.
DR PhylomeDB; P42776; -.
DR PRO; PR:P42776; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P42776; baseline and differential.
DR Genevisible; P42776; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
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 GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
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 Alternative splicing; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..382
FT /note="G-box-binding factor 3"
FT /id="PRO_0000076567"
FT DOMAIN 259..322
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..280
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 287..322
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 329..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 75
FT /note="Y -> S (in Ref. 1; AAA90947/AAB06611)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="L -> F (in Ref. 1; AAA90947/AAB06611)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 382 AA; 41114 MW; 48B31762CDCD977C CRC64;
MGNSSEEPKP PTKSDKPSSP PVDQTNVHVY PDWAAMQAYY GPRVAMPPYY NSAMAASGHP
PPPYMWNPQH MMSPYGAPYA AVYPHGGGVY AHPGIPMGSL PQGQKDPPLT TPGTLLSIDT
PTKSTGNTDN GLMKKLKEFD GLAMSLGNGN PENGADEHKR SRNSSETDGS TDGSDGNTTG
ADEPKLKRSR EGTPTKDGKQ LVQASSFHSV SPSSGDTGVK LIQGSGAILS PGVSANSNPF
MSQSLAMVPP ETWLQNEREL KRERRKQSNR ESARRSRLRK QAETEELARK VEALTAENMA
LRSELNQLNE KSDKLRGANA TLLDKLKCSE PEKRVPANML SRVKNSGAGD KNKNQGDNDS
NSTSKLHQLL DTKPRAKAVA AG
