Gene Details:

Protein Features:

Annotation Proteins:

  • Refseq:  NP_001151391.2  — transcription factor RF2b
  • Swissprot:  Q9MA75  — VIP1_ARATH; Transcription factor VIP1
  • TrEMBL:  A0A1D6EHU0  — A0A1D6EHU0_MAIZE; Transcription factor VIP1
  • TrEMBL:  A0A3L6FZV1  — A0A3L6FZV1_MAIZE; Transcription factor VIP1
  • STRING:  Pavir.Ha01827.1.p  — (Panicum virgatum)
  • STRING:  GRMZM5G821024_P01  — (Zea mays)

Gene Ontology:

  • GO:0006355  — Biological Process — regulation of transcription, DNA-templated
  • GO:0007231  — Biological Process — osmosensory signaling pathway
  • GO:0008272  — Biological Process — sulfate transport
  • GO:0009294  — Biological Process — DNA mediated transformation
  • GO:0009652  — Biological Process — thigmotropism
  • GO:0009970  — Biological Process — cellular response to sulfate starvation
  • GO:0045596  — Biological Process — negative regulation of cell differentiation
  • GO:0051170  — Biological Process — nuclear import
  • GO:0005634  — Cellular Component — nucleus
  • GO:0005829  — Cellular Component — cytosol
  • GO:0003682  — Molecular Function — chromatin binding
  • GO:0003700  — Molecular Function — transcription factor activity, sequence-specific DNA binding
  • GO:0043565  — Molecular Function — sequence-specific DNA binding
  • GO:0043621  — Molecular Function — protein self-association
  • GO:0051019  — Molecular Function — mitogen-activated protein kinase 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:

Sequences:

CDS Sequence:
  • >Oropetium_20150105_14977A|Oropetium_thomaeum|bZIP|Oropetium_20150105_14977A
    ATGAGGAGCCTCTCTCTCGACGCGGCCCTGTTCGACGGCCTCTCCCTGCAGCAGGGAGTGGCGGGAGGGAGCGGCGCCGTGGCGGGCCATAAGAGGAGCGGCTCCATGGACGGGCCGACCTCGCCGTTCGAGGGCGAGTCCGCGCTGTCGGGCGGGCTTCCGGAATACGCCAAGAAGGCGGTGCCCTCCGAGAGGCTCGCTGAGCTCGCGCTGCTCGACCCCAAGCGCGCAAAGAGGATTCTGGCAAACAGACAGTCGGCGGCGAGGTCTAAGGAGAGGAAGATCAAGTACACCAGTGAGCTTGAGCGGAAGGTGCAGACGCTGCAGACAGAGGCCACCACGCTTTCGGCACAGCTCACGCTTCTTCAGAGGGACACTTCTGGTCTAACTGCGGAGAACAGGGAGCTCAAACTCCGGTTGCAATCCATGGAAGAACAAGCTAAACTCCGAGATGCGCTGAACGATGCCCTTAGAGAAGAGGTTCAGCGGCTTAAGATAGCCGCAGGCCAAGTCCCGAACATGAACAGGAACCCTTTTAACGGCGGGCTACCACAGCAGCGGCAGCAGCAGCAGCAACAGCAGCAGCAGATGGCATCCTACTTCTCACAACCGCAGCAGATGCAGTACTTTGGCAGTAACCAGGTTCAGCATCACCGCCCGAATCAGCCCCAGAACTCTTCAAACGGTGGTGGGCGGTGCCTGAACGACTCCATGGATTTCATGTGA
Protein Sequence:
  • >Oropetium_20150105_14977A|Oropetium_thomaeum|bZIP|Oropetium_20150105_14977A
    MRSLSLDAALFDGLSLQQGVAGGSGAVAGHKRSGSMDGPTSPFEGESALSGGLPEYAKKAVPSERLAELALLDPKRAKRILANRQSAARSKERKIKYTSELERKVQTLQTEATTLSAQLTLLQRDTSGLTAENRELKLRLQSMEEQAKLRDALNDALREEVQRLKIAAGQVPNMNRNPFNGGLPQQRQQQQQQQQQMASYFSQPQQMQYFGSNQVQHHRPNQPQNSSNGGGRCLNDSMDFM*