ID   BZP1B_WHEAT             Reviewed;         388 AA.
AC   B6E107;
DT   03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=bZIP transcription factor 1-B {ECO:0000305};
DE            Short=TabZIP1-B {ECO:0000305};
GN   Name=BZIP1-B {ECO:0000305}; Synonyms=BZIP1 {ECO:0000303|Ref.1};
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND INDUCTION.
RC   TISSUE=Leaf;
RX   DOI=10.1016/j.pmpp.2009.02.002;
RA   Zhang Y., Zhang G., Xia N., Wang X.J., Huang L.L., Kang Z.S.;
RT   "Cloning and characterization of a bZIP transcription factor gene in wheat
RT   and its expression in response to stripe rust pathogen infection and
RT   abiotic stresses.";
RL   Physiol. Mol. Plant Pathol. 73:88-94(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Chinese Spring;
RX   PubMed=30115783; DOI=10.1126/science.aar7191;
RG   International wheat genome sequencing consortium (IWGSC);
RT   "Shifting the limits in wheat research and breeding using a fully annotated
RT   reference genome.";
RL   Science 361:EAAR7191-EAAR7191(2018).
CC   -!- FUNCTION: Probable transcription factor that may be involved in
CC       responses to fungal pathogen infection and abiotic stresses.
CC       {ECO:0000269|Ref.1}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978,
CC       ECO:0000269|Ref.1}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in roots and at lower levels in
CC       stems and leaves. {ECO:0000269|Ref.1}.
CC   -!- INDUCTION: Induced during incompatible interaction with the fungal
CC       pathogen Puccinia striiformis (Ref.1). Induced by abscisic acid (ABA),
CC       ethylene, cold stress, salt stress and wounding (Ref.1).
CC       {ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR   EMBL; FJ194457; ACI28287.1; -; mRNA.
DR   AlphaFoldDB; B6E107; -.
DR   SMR; B6E107; -.
DR   STRING; 4565.Traes_5BL_A5532B750.1; -.
DR   EnsemblPlants; TraesCS5B02G122000.2; TraesCS5B02G122000.2; TraesCS5B02G122000.
DR   Gramene; TraesCS5B02G122000.2; TraesCS5B02G122000.2; TraesCS5B02G122000.
DR   HOGENOM; CLU_036349_0_1_1; -.
DR   OMA; NMPAMGT; -.
DR   Proteomes; UP000019116; Unplaced.
DR   ExpressionAtlas; B6E107; baseline.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   DNA-binding; Nucleus; Plant defense; Reference proteome; Stress response;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..388
FT                   /note="bZIP transcription factor 1-B"
FT                   /id="PRO_0000447481"
FT   DOMAIN          293..356
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          126..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          261..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          295..314
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          321..356
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          348..388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..202
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..249
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   388 AA;  41323 MW;  96A019D21D013F21 CRC64;
     MGSSEAETPA KANKASAPQE QQPPATSSTA TPTVYPDWTS FQGYPPIPPH GFFPSPVVSN
     PQGHPYMWGP QPMMPPYGTP PYVIYPPGGI YAHPSMRPGA HPFAPYTMTS PNGNPDAAGT
     TITAATAGGE TNGKSSEGKE KSPIKRSKGS LGSLNMITGK NCVEHGKTSG ASANGTISQS
     GESGSESSSE GSEANSQNDS QHKESGQEQD GDVRSSQNGV SPSPSQAQLK QTLAIMQMPS
     SGPVPGPTTN LNIGMDYWAN TASSSPALHG KVTPTAIPGA VAPTEPWMQD ERELKRQKRK
     QSNRDSARRS RLRKQAECEE LAQRAEVLKQ ENASLKDEVS RIRKEYDELL SKNSSLKDNV
     GDKQHKTDEA GLDNKLQHSG DDSQKDTN