GBF2_ARATH
ID GBF2_ARATH Reviewed; 360 AA.
AC P42775;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 162.
DE RecName: Full=G-box-binding factor 2;
DE AltName: Full=bZIP transcription factor 54;
DE Short=AtbZIP54;
GN Name=GBF2; Synonyms=BZIP54; OrderedLocusNames=At4g01120; ORFNames=F2N1.12;
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; 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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Jarillo J.A., Cashmore A.R.;
RT "Cloning and identification of the nucleotide sequence of the Arabidopsis
RT thaliana gene encoding G-box binding factor 2 (GBF2).";
RL (er) Plant Gene Register PGR98-101(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [4]
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 [5]
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 [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. GBF2 is found to bind
CC asymmetrically to the G-box. {ECO:0000269|PubMed:1373374}.
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:1373374}.
CC -!- TISSUE SPECIFICITY: Found in both light and dark grown leaves.
CC {ECO:0000269|PubMed:1373374}.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR EMBL; X63895; CAA45357.1; -; mRNA.
DR EMBL; AF053228; AAC26198.1; -; Genomic_DNA.
DR EMBL; AL161491; CAB80921.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE81984.1; -; Genomic_DNA.
DR EMBL; AY062667; AAL32745.1; -; mRNA.
DR EMBL; AY093316; AAM13315.1; -; mRNA.
DR PIR; G85014; G85014.
DR RefSeq; NP_192021.1; NM_116342.3.
DR AlphaFoldDB; P42775; -.
DR SMR; P42775; -.
DR BioGRID; 11804; 9.
DR IntAct; P42775; 9.
DR STRING; 3702.AT4G01120.1; -.
DR iPTMnet; P42775; -.
DR PaxDb; P42775; -.
DR PRIDE; P42775; -.
DR ProteomicsDB; 222179; -.
DR EnsemblPlants; AT4G01120.1; AT4G01120.1; AT4G01120.
DR GeneID; 826505; -.
DR Gramene; AT4G01120.1; AT4G01120.1; AT4G01120.
DR KEGG; ath:AT4G01120; -.
DR Araport; AT4G01120; -.
DR TAIR; locus:2124938; AT4G01120.
DR eggNOG; ENOG502QRCN; Eukaryota.
DR HOGENOM; CLU_036349_1_0_1; -.
DR InParanoid; P42775; -.
DR OMA; RHGAPHE; -.
DR OrthoDB; 1121126at2759; -.
DR PhylomeDB; P42775; -.
DR PRO; PR:P42775; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P42775; baseline and differential.
DR Genevisible; P42775; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IDA:TAIR.
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:0019760; P:glucosinolate metabolic process; IMP:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0009637; P:response to blue light; IDA: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 DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..360
FT /note="G-box-binding factor 2"
FT /id="PRO_0000076566"
FT DOMAIN 249..312
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 150..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..270
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 277..312
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 335..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 360 AA; 38789 MW; 060EEFCB168BBB17 CRC64;
MGSNEEGNPT NNSDKPSQAA APEQSNVHVY HHDWAAMQAY YGPRVGIPQY YNSNLAPGHA
PPPYMWASPS PMMAPYGAPY PPFCPPGGVY AHPGVQMGSQ PQGPVSQSAS GVTTPLTIDA
PANSAGNSDH GFMKKLKEFD GLAMSISNNK VGSAEHSSSE HRSSQSSEND GSSNGSDGNT
TGGEQSRRKR RQQRSPSTGE RPSSQNSLPL RGENEKPDVT MGTPVMPTAM SFQNSAGMNG
VPQPWNEKEV KREKRKQSNR ESARRSRLRK QAETEQLSVK VDALVAENMS LRSKLGQLNN
ESEKLRLENE AILDQLKAQA TGKTENLISR VDKNNSVSGS KTVQHQLLNA SPITDPVAAS
