Gene Details:

  • Gene ID: Bostr.15774s0073.1.p
  • Gene Family: bZIP Family
  • Description: bZIP Family protein
  • Species: Boechera stricta
  • Source: bZIP family gene from PlantTFDB

Protein Features:

Annotation Proteins:

  • Refseq:  XP_010440575.1  — PREDICTED: basic leucine zipper 1-like
  • Swissprot:  Q9FGX2  — BZIP1_ARATH; Basic leucine zipper 1
  • TrEMBL:  A0A178UPE4  — A0A178UPE4_ARATH; Uncharacterized protein
  • STRING:  Bostr.15774s0073.1.p  — (Boechera stricta)

Gene Ontology:

  • GO:0006521  — Biological Process — regulation of cellular amino acid metabolic process
  • GO:0009267  — Biological Process — cellular response to starvation
  • GO:0009617  — Biological Process — response to bacterium
  • GO:0009651  — Biological Process — response to salt stress
  • GO:0009901  — Biological Process — anther dehiscence
  • GO:0010182  — Biological Process — sugar mediated signaling pathway
  • GO:0045893  — Biological Process — positive regulation of transcription, DNA-templated
  • GO:0071333  — Biological Process — cellular response to glucose stimulus
  • GO:0005634  — Cellular Component — nucleus
  • GO:0003700  — Molecular Function — transcription factor activity, sequence-specific DNA binding
  • GO:0043565  — Molecular Function — sequence-specific DNA binding
  • GO:0044212  — Molecular Function — transcription regulatory region DNA binding
  • GO:0046982  — Molecular Function — protein heterodimerization activity

Family Introduction:

  • The bZIP domain consists of two structural features located on a contiguous alpha-helix: first, a basic region of ~ 16 amino acid residues containing a nuclear localization signal followed by an invariant N-x7-R/K motif that contacts the DNA; and, second, a heptad repeat of leucines or other bulky hydrophobic amino acids positioned exactly nine amino acids towards the C-terminus, creating an amphipathic helix. To bind DNA, two subunits adhere via interactions between the hydrophobic sides of their helices, which creates a superimposing coiled-coil structure. The ability to form homo- and heterodimers is influenced by the electrostatic attraction and repulsion of polar residues flanking the hydrophobic interaction surface of the helices.
  • Plant bZIP proteins preferentially bind to DNA sequences with an ACGT core. Binding specificity is regulated by flanking nucleotides. Plant bZIPs preferentially bind to the A-box (TACGTA), C-box (GACGTC) and G-box (CACGTG), but there are also examples of nonpalindromic binding sites.

Literature:

Sequences:

CDS Sequence:
  • >Bostr.15774s0073.1.p|Boechera_stricta|bZIP|Bostr.15774s0073.1.p
    ATGGCAAACGCAGAGAAGACAAGTTCAGGTTCCGACATAGATGAGAAGAAAAGAAAACGCAAATTATCAAACCGCGAATCAGCTAGGAGATCGCGTTTGAAGAAACAGAAGTTAATGGAAGACACGATTCATGAGATCTCGAGTCTTGAACGACGAATCAAAGAGAACAGCGAGAGATGTAGAGCTGTGAAAGAGAGGCTTGACTCGGTTGAATCGGAAAACGCGGTTCTTAGATCGGAGAAAACGTGGCTTTCGAGTTACGTTAGCGATTTAGAGAATATGATTGCTACGACGAGTTTGACGCTGACGCAGAGTGGTGGTGGCGGTGGCGATTGTGATGAGGATCAGAACGCAAACGCGGAAATAGGGGTTGGAGATTGTAGACGACGTAGACCGTGGAAGTTGAGTTGTGATTCTCTAACTACAACCAGTCGCGTCCTTTAA
Protein Sequence:
  • >Bostr.15774s0073.1.p|Boechera_stricta|bZIP|Bostr.15774s0073.1.p
    MANAEKTSSGSDIDEKKRKRKLSNRESARRSRLKKQKLMEDTIHEISSLERRIKENSERCRAVKERLDSVESENAVLRSEKTWLSSYVSDLENMIATTSLTLTQSGGGGGDCDEDQNANAEIGVGDCRRRRPWKLSCDSLTTTSRVL*