GBF4_ARATH
ID GBF4_ARATH Reviewed; 270 AA.
AC P42777;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 151.
DE RecName: Full=G-box-binding factor 4;
DE AltName: Full=bZIP transcription factor 40;
DE Short=AtbZIP40;
GN Name=GBF4; Synonyms=BZIP40; OrderedLocusNames=At1g03970;
GN ORFNames=F21M11.10;
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, FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP GBF2 AND GBF3.
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 [2]
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 [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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) 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).
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:8146148}.
CC -!- SUBUNIT: DNA-binding heterodimer with GBF2 and GBF3; non DNA-binding
CC homodimer.
CC -!- INTERACTION:
CC P42777; Q7XJS0: ASHR1; NbExp=3; IntAct=EBI-15192551, EBI-15192553;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978,
CC ECO:0000269|PubMed:8146148}.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR EMBL; U01823; AAA18414.1; -; Unassigned_DNA.
DR EMBL; AC003027; AAD10673.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27640.1; -; Genomic_DNA.
DR EMBL; AY087603; AAM65145.1; -; mRNA.
DR PIR; F86170; F86170.
DR RefSeq; NP_171893.1; NM_100278.3.
DR AlphaFoldDB; P42777; -.
DR SMR; P42777; -.
DR BioGRID; 24591; 10.
DR IntAct; P42777; 7.
DR STRING; 3702.AT1G03970.1; -.
DR iPTMnet; P42777; -.
DR PaxDb; P42777; -.
DR PRIDE; P42777; -.
DR ProteomicsDB; 222181; -.
DR EnsemblPlants; AT1G03970.1; AT1G03970.1; AT1G03970.
DR GeneID; 839356; -.
DR Gramene; AT1G03970.1; AT1G03970.1; AT1G03970.
DR KEGG; ath:AT1G03970; -.
DR Araport; AT1G03970; -.
DR TAIR; locus:2024224; AT1G03970.
DR eggNOG; ENOG502RXGY; Eukaryota.
DR HOGENOM; CLU_043238_2_2_1; -.
DR InParanoid; P42777; -.
DR OMA; HADHSRI; -.
DR OrthoDB; 1206106at2759; -.
DR PhylomeDB; P42777; -.
DR PRO; PR:P42777; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P42777; baseline and differential.
DR Genevisible; P42777; AT.
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:0045893; P:positive regulation of transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR043452; BZIP46-like.
DR InterPro; IPR046347; bZIP_sf.
DR PANTHER; PTHR22952; PTHR22952; 1.
DR Pfam; PF00170; bZIP_1; 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; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..270
FT /note="G-box-binding factor 4"
FT /id="PRO_0000076568"
FT DOMAIN 187..250
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..208
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 215..229
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 250..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LES3"
SQ SEQUENCE 270 AA; 30586 MW; 36BC37F954EFF11E CRC64;
MASFKLMSSS NSDLSRRNSS SASSSPSIRS SHHLRPNPHA DHSRISFAYG GGVNDYTFAS
DSKPFEMAID VDRSIGDRNS VNNGKSVDDV WKEIVSGEQK TIMMKEEEPE DIMTLEDFLA
KAEMDEGASD EIDVKIPTER LNNDGSYTFD FPMQRHSSFQ MVEGSMGGGV TRGKRGRVMM
EAMDKAAAQR QKRMIKNRES AARSRERKQA YQVELETLAA KLEEENEQLL KEIEESTKER
YKKLMEVLIP VDEKPRPPSR PLSRSHSLEW
