GBF1_ARATH
ID GBF1_ARATH Reviewed; 315 AA.
AC P42774; Q940I9; Q944J1; Q96263;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=G-box-binding factor 1;
DE Short=AtGBF1;
DE AltName: Full=bZIP transcription factor 41;
DE Short=AtbZIP41;
GN Name=GBF1; Synonyms=BZIP41; OrderedLocusNames=At4g36730;
GN ORFNames=C7A10_630;
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] (ISOFORM 1), AND FUNCTION.
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 Terryn N., Villarroel R., Neyt P., de Clercq R., Ardiles W., de Keyser A.,
RA van den Daele H., Rouze P., Gielen J., van Montagu M.;
RT "Nucleotide sequence of the Arabidopsis thaliana gene encoding the G-box-
RT binding factor 1 (GBF1).";
RL (er) Plant Gene Register PGR96-111(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 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., 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 [7]
RP PHOSPHORYLATION.
RX PubMed=7696877; DOI=10.2307/3869841;
RA Klimczak L.J., Collinge M.A., Farini D., Giuliano G., Walker J.C.,
RA Cashmore A.R.;
RT "Reconstitution of Arabidopsis casein kinase II from recombinant subunits
RT and phosphorylation of transcription factor GBF1.";
RL Plant Cell 7:105-115(1995).
RN [8]
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 [9]
RP SUBUNIT, AND 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).
RN [10]
RP FUNCTION, DISULFIDE BOND, AND MUTAGENESIS OF CYS-247 AND CYS-275.
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 [11]
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: Binds to the G-box motif (5'-CCACGTGG-3') of the rbcS-1A gene
CC promoter (PubMed:1373374). 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
CC control. Binds to the G-box motif 5'-CACGTG-3' of LHCB2.4 (At3g27690)
CC promoter. May act as transcriptional activator in light-regulated
CC expression of LHCB2.4. Probably binds DNA as monomer. DNA-binding
CC activity is redox-dependent (PubMed:22718771).
CC {ECO:0000269|PubMed:1373374, ECO:0000269|PubMed:22718771}.
CC -!- SUBUNIT: Monomer and heterodimers with BZIP16 and BZIP68
CC (PubMed:18315949). Interacts with GIP1 (PubMed:25387999).
CC {ECO:0000269|PubMed:18315949, ECO:0000269|PubMed:25387999}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P42774-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P42774-2; Sequence=VSP_009191;
CC -!- TISSUE SPECIFICITY: Found in both light and dark grown leaves.
CC -!- PTM: Phosphorylated by CK2. {ECO:0000269|PubMed:7696877}.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR EMBL; X63894; CAA45356.1; -; mRNA.
DR EMBL; X99941; CAA68197.1; -; Genomic_DNA.
DR EMBL; Z99708; CAB16806.1; -; Genomic_DNA.
DR EMBL; AL161589; CAB80339.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86694.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86695.1; -; Genomic_DNA.
DR EMBL; AY054574; AAK96765.1; -; mRNA.
DR EMBL; AY064670; AAL47377.1; -; mRNA.
DR EMBL; AF428382; AAL16150.1; -; mRNA.
DR PIR; G85433; G85433.
DR PIR; S20883; S20883.
DR RefSeq; NP_195391.1; NM_119837.4. [P42774-1]
DR RefSeq; NP_849510.1; NM_179179.3. [P42774-2]
DR AlphaFoldDB; P42774; -.
DR SMR; P42774; -.
DR BioGRID; 15107; 10.
DR IntAct; P42774; 6.
DR STRING; 3702.AT4G36730.1; -.
DR PaxDb; P42774; -.
DR PRIDE; P42774; -.
DR ProteomicsDB; 222178; -. [P42774-1]
DR EnsemblPlants; AT4G36730.1; AT4G36730.1; AT4G36730. [P42774-1]
DR EnsemblPlants; AT4G36730.2; AT4G36730.2; AT4G36730. [P42774-2]
DR GeneID; 829826; -.
DR Gramene; AT4G36730.1; AT4G36730.1; AT4G36730. [P42774-1]
DR Gramene; AT4G36730.2; AT4G36730.2; AT4G36730. [P42774-2]
DR KEGG; ath:AT4G36730; -.
DR Araport; AT4G36730; -.
DR TAIR; locus:2115250; AT4G36730.
DR eggNOG; ENOG502QVYY; Eukaryota.
DR InParanoid; P42774; -.
DR OMA; TRFCGPE; -.
DR PhylomeDB; P42774; -.
DR PRO; PR:P42774; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P42774; baseline and differential.
DR Genevisible; P42774; AT.
DR GO; GO:0005737; C:cytoplasm; 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 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; Disulfide bond; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..315
FT /note="G-box-binding factor 1"
FT /id="PRO_0000076565"
FT DOMAIN 222..285
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..243
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 250..285
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COMPBIAS 1..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 247
FT /note="Interchain"
FT /evidence="ECO:0000305|PubMed:22718771"
FT VAR_SEQ 161..162
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_009191"
FT MUTAGEN 247
FT /note="C->L: Significantly increases DNA binding activity."
FT /evidence="ECO:0000269|PubMed:22718771"
FT MUTAGEN 275
FT /note="C->L: Slightly increases DNA binding activity."
FT /evidence="ECO:0000269|PubMed:22718771"
FT CONFLICT 43
FT /note="T -> S (in Ref. 1; CAA45356)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="S -> A (in Ref. 6; AAK96765/AAL47377)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="Q -> R (in Ref. 6; AAK96765/AAL47377)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 315 AA; 33932 MW; 8585EF0249C91C21 CRC64;
MGTSEDKMPF KTTKPTSSAQ EVPPTPYPDW QNSMQAYYGG GGTPNPFFPS PVGSPSPHPY
MWGAQHHMMP PYGTPVPYPA MYPPGAVYAH PSMPMPPNSG PTNKEPAKDQ ASGKKSKGNS
KKKAEGGDKA LSGSGNDGAS HSDESVTAGS SDENDENANQ QEQGSIRKPS FGQMLADASS
QSTTGEIQGS VPMKPVAPGT NLNIGMDLWS SQAGVPVKDE RELKRQKRKQ SNRESARRSR
LRKQAECEQL QQRVESLSNE NQSLRDELQR LSSECDKLKS ENNSIQDELQ RVLGAEAVAN
LEQNAAGSKD GEGTN
