Gene Details:

• Gene ID: Gh_A08G2092
• Gene Family: bZIP Family
• Description: bZIP Family protein
• Species: Gossypium hirsutum
• 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_016692136.1  — PREDICTED: protein OVEREXPRESSOR OF CATIONIC PEROXIDASE 3-like isoform X1
• Refseq:  XP_016692139.1  — PREDICTED: protein OVEREXPRESSOR OF CATIONIC PEROXIDASE 3-like isoform X3
• Refseq:  XP_016692140.1  — PREDICTED: protein OVEREXPRESSOR OF CATIONIC PEROXIDASE 3-like isoform X3
• TrEMBL:  A0A1U8JPD5  — A0A1U8JPD5_GOSHI; protein OVEREXPRESSOR OF CATIONIC PEROXIDASE 3-like isoform X1
• TrEMBL:  A0A1U8JV42  — A0A1U8JV42_GOSHI; protein OVEREXPRESSOR OF CATIONIC PEROXIDASE 3-like isoform X3
• STRING:  Gorai.004G274200.1  — (Gossypium raimondii)

Gene Ontology:

• GO:0002229  — Biological Process — defense response to oomycetes
• GO:0006355  — Biological Process — regulation of transcription, DNA-templated
• GO:0009414  — Biological Process — response to water deprivation
• GO:0009682  — Biological Process — induced systemic resistance
• GO:0009787  — Biological Process — regulation of abscisic acid-activated signaling pathway
• GO:0010118  — Biological Process — stomatal movement
• GO:0050832  — Biological Process — defense response to fungus
• GO:2000022  — Biological Process — regulation of jasmonic acid mediated signaling pathway
• GO:2000071  — Biological Process — regulation of defense response by callose deposition
• GO:0005634  — Cellular Component — nucleus
• GO:0003700  — Molecular Function — transcription factor activity, sequence-specific DNA binding
• GO:0043565  — Molecular Function — sequence-specific DNA binding

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:

• bZIP transcription factors in Arabidopsis.   DOI:  10.1016/s1360-1385(01)02223-3 ;  PMID:  11906833

Sequences: