ID   BZP1A_WHEAT             Reviewed;         388 AA.
AC   A0A3B6KF13;
DT   03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT   05-DEC-2018, sequence version 1.
DT   25-MAY-2022, entry version 12.
DE   RecName: Full=bZIP transcription factor 1-A {ECO:0000305};
DE            Short=TabZIP1-A {ECO:0000305};
GN   Name=BZIP1-A {ECO:0000305}; Synonyms=BZIP1 {ECO:0000303|Ref.2};
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 [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).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE 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).
CC   -!- FUNCTION: Probable transcription factor that may be involved in
CC       responses to fungal pathogen infection and abiotic stresses.
CC       {ECO:0000269|Ref.2}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978,
CC       ECO:0000269|Ref.2}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in roots and at lower levels in
CC       stems and leaves. {ECO:0000269|Ref.2}.
CC   -!- INDUCTION: Induced during incompatible interaction with the fungal
CC       pathogen Puccinia striiformis (Ref.2). Induced by abscisic acid (ABA),
CC       ethylene, cold stress, salt stress and wounding (Ref.2).
CC       {ECO:0000269|Ref.2}.
CC   -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; A0A3B6KF13; -.
DR   SMR; A0A3B6KF13; -.
DR   STRING; 4565.Traes_5AS_3A85F1C2C.3; -.
DR   EnsemblPlants; TraesCS5A02G115300.2; TraesCS5A02G115300.2; TraesCS5A02G115300.
DR   Gramene; TraesCS5A02G115300.2; TraesCS5A02G115300.2; TraesCS5A02G115300.
DR   Proteomes; UP000019116; Unplaced.
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-A"
FT                   /id="PRO_0000447480"
FT   DOMAIN          293..356
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          103..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        107..133
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..270
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   388 AA;  41351 MW;  AE402441089AD447 CRC64;
     MGSSEAETPA KANKASAPQE QQPPATSSIA TPTVYPDWTS FQGYPPIPPH GFFPSPVVSN
     PQGHPYMWGP QPMMPPYGTP PYVIYPPGGI YAHPSMRPGA HPFAPYTMTS PNGNPDAAGT
     TTTAATAGGE TNGKSSEGKE KSPIKRSKGS LGSLNMITGK NCVEHGKTSG ASVNGTISQS
     GESGSESSSE GSEANSQNDS QHKESGQEQD GDVRSSQNGV SPSPSQAQLK QTLAIMQMPS
     SGPVPGPTTN LNIGMDYWAN TASSSPALHG KVTPTAIPGA VAPTEPWMQD ERELKRQKRK
     QSNRDSARRS RLRKQAECEE LAQRAEVLKQ ENASLKDEVS RIRKEYDELL SKNSSLKDNV
     GDKQHKTDEA GLDNKLQHSG DDSQKDTN