Gene Details:
- Gene ID: AA58G00024
- Gene Family: bZIP Family
- Description: bZIP Family protein
- Species: Aethionema arabicum
- Source: bZIP family gene from PlantTFDB
Protein Features:
- SMART: SM00338
- Gene3D: G3DSA:1.20.5.170
- PROSITE profile: PS50217
- Pfam: PF00170
- SuperFamily: SSF57959
- PROSITE pattern: PS00036
- InterPro: IPR004827
Annotation Proteins:
- Refseq: XP_020871920.1 — basic leucine zipper 1
- Swissprot: Q9FGX2 — BZIP1_ARATH; Basic leucine zipper 1
- TrEMBL: D7MNS4 — D7MNS4_ARALL; BZIP family transcription factor
- STRING: fgenesh2_kg.8__816__AT5G49448.1 — (Arabidopsis lyrata)
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:
- >AA58G00024|Aethionema_arabicum|bZIP|AA58G00024
ATGGCAAACGCAACGCAGACGAGTTCAGGTTCTGATTTAGATGAGAGGAAAAGAAAACGCAAGCTATCAAATCGCGAATCGGCTAGGCGATCGCGTTTGAAGAAACAGAAATTGATGGAAGATACGATTCACGAGATCTCAACTTTGCAAATACGGATCAAAGAGAATAACGAGAGATGCAAAGTGATGAAGCAAAGATTAGACGCGATTGAATCGGAAAACCGGTTTCTTAGATCTGAGAAGAAGCGGCTTTCGACTTACTTTAGCGATTTAGAAGCTATGATTGGAAGCGATCAAAACGCGGAAATAATGGTTGGAGATTGTAGACATAGACCTTTGCAGCTGCTACCAATGGCGTCCTTTGGATTCAAGACA
Protein Sequence:
- >AA58G00024|Aethionema_arabicum|bZIP|AA58G00024
MANATQTSSGSDLDERKRKRKLSNRESARRSRLKKQKLMEDTIHEISTLQIRIKENNERCKVMKQRLDAIESENRFLRSEKKRLSTYFSDLEAMIGSDQNAEIMVGDCRHRPLQLLPMASFGFKT