Q9MA75 · VIP1_ARATH

Function

function

Transcription activator that binds specifically to the VIP1 response elements (VREs) DNA sequence 5'-ACNGCT-3' found in some stress genes (e.g. TRX8 and MYB44), when phosphorylated/activated by MPK3. Required for Agrobacterium VirE2 nuclear import and tumorigenicity. Promotes transient expression of T-DNA in early stages by interacting with VirE2 in complex with the T-DNA and facilitating its translocation to the nucleus, and mediates stable genetic transformation by Agrobacterium by binding H2A histone. Prevents cell differentiation and shoot formation. Limits sulfate utilization efficiency (SUE) and sulfate uptake, especially in low-sulfur conditions (PubMed:11432846, PubMed:12124400, PubMed:15108305, PubMed:15824315, PubMed:17947581, PubMed:19820165, PubMed:20547563).
Plays a role in osmosensory response by binding to the 5'-AGCTGT/G-3' DNA sequence found in the promoters of the hypoosmolarity-responsive genes CYP707A1 and CYP707A3 (PubMed:22452852, PubMed:25093810).
Involved in the negative regulation of touch-induced root bending and salt-dependent root bending (PubMed:27208231, PubMed:30010769, PubMed:31504762).

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytosol
Cellular Componentnucleus
Molecular Functionchromatin binding
Molecular FunctionDNA-binding transcription factor activity
Molecular Functionmitogen-activated protein kinase binding
Molecular Functionnucleic acid binding
Molecular Functionsequence-specific DNA binding
Molecular Functiontranscription cis-regulatory region binding
Biological Processcellular response to sulfate starvation
Biological Processdefense response
Biological ProcessDNA-mediated transformation
Biological Processimport into nucleus
Biological Processnegative regulation of cell differentiation
Biological Processosmosensory signaling pathway
Biological Processresponse to osmotic stress
Biological Processsulfate transport
Biological Processthigmotropism

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Transcription factor VIP1
  • Alternative names
    • Protein SULPHATE UTILIZATION EFFICIENCY 3
    • VirE2-interacting protein 1
      (AtVIP1
      )
    • bZIP transcription factor 51
      (AtbZIP51
      ; bZIP protein 51
      )

Gene names

    • Name
      VIP1
    • Synonyms
      BZIP51
      , SUE3
    • ORF names
      F2J6.6
    • Ordered locus names
      At1g43700

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    Q9MA75
  • Secondary accessions
    • Q8LDQ9
    • Q9M5N9

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Cytoplasm
Nucleus
Note: Confined to nucleus when phosphorylated (PubMed:17947581).
Transiently accumulates in the nucleus when cells are exposed to hypoosmotic conditions (PubMed:25093810, PubMed:31504762).

Keywords

Phenotypes & Variants

Disruption phenotype

Enhanced low sulfur tolerance with higher rate of sulfate uptake at low sulfate levels. Improved tolerance to heavy metal (e.g. CdCl2) and oxidative stress (e.g. paraquat).

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis79Cytoplasmic and nuclear.
Mutagenesis79Only nuclear.
Mutagenesis163-341Transient T-DNA transformation end expression, but impaired stable genetic transformation by Agrobacterium, loss of multimerization, and abolished interaction with histone H2A.
Mutagenesis212Impaired VIP1 response elements (VREs) DNA-binding and altered subsequent transcription activation.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 33 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00004055931-341Transcription factor VIP1
Modified residue79Phosphoserine

Post-translational modification

Phosphorylated by MPK3. This phosphorylation promotes nuclear localization.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Mostly expressed in dividing cells, present in leaves, roots and seedlings.

Induction

Transcriptionally activated during the acquisition of pluripotentiality (in protoplasts) by pericentromeric chromatin decondensation and DNA demethylation. Targeted to degradation by the proteasome by VBF and Agrobacterium virF in SCF(VBF) and SCF(virF) E3 ubiquitin ligase complexes after mediating T-DNA translocation to the nucleus.

Gene expression databases

Interaction

Subunit

Forms homomultimers. Interacts with Agrobacterium tumefaciens VirE2 and mediates its translocation to the host nucleus. Binds to VIP2. Forms a complex made of Agrobacterium VirE2, VIP1, VIP2 and single-stranded DNA (ssDNA). The interaction with KAP1 mediates its nuclear import. Binds to the H2A histone RAT5. Interacts with MPK3 and Agrobacterium virF. Forms a complex made of VIP1, VBF and Agrobacterium virE2. Interacts with SCF(VBF) E3 ubiquitin ligase complex. Binds directly to VBF. Forms heterodimers with BZIP34 and BZIP61.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
XENO Q9MA75virF P155973EBI-606057, EBI-605118

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias, domain, motif.

TypeIDPosition(s)Description
Region1-33Disordered
Region1-162Necessary and sufficient for transient T-DNA transformation end expression
Compositional bias19-33Basic and acidic residues
Region59-106Disordered
Compositional bias75-95Polar residues
Region135-156Disordered
Region163-341Involved in homomultimerization and histone H2A binding
Domain194-257bZIP
Region196-217Basic motif
Motif198-205Nuclear localization signal
Region222-257Leucine-zipper
Compositional bias307-333Polar residues
Region307-341Disordered

Sequence similarities

Belongs to the bZIP family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    341
  • Mass (Da)
    37,791
  • Last updated
    2000-10-01 v1
  • Checksum
    10BE8D8230C53531
MEGGGRGPNQTILSEIEHMPEAPRQRISHHRRARSETFFSGESIDDLLLFDPSDIDFSSLDFLNAPPPPQQSQQQPQASPMSVDSEETSSNGVVPPNSLPPKPEARFGRHVRSFSVDSDFFDDLGVTEEKFIATSSGEKKKGNHHHSRSNSMDGEMSSASFNIESILASVSGKDSGKKNMGMGGDRLAELALLDPKRAKRILANRQSAARSKERKIRYTGELERKVQTLQNEATTLSAQVTMLQRGTSELNTENKHLKMRLQALEQQAELRDALNEALRDELNRLKVVAGEIPQGNGNSYNRAQFSSQQSAMNQFGNKTNQQMSTNGQPSLPSYMDFTKRG

Features

Showing features for compositional bias, sequence conflict.

TypeIDPosition(s)Description
Compositional bias19-33Basic and acidic residues
Compositional bias75-95Polar residues
Sequence conflict132in Ref. 4; AAM63070
Compositional bias307-333Polar residues
Sequence conflict319in Ref. 4; AAM63070

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AC009526
EMBL· GenBank· DDBJ
AAF63120.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002684
EMBL· GenBank· DDBJ
AEE31988.1
EMBL· GenBank· DDBJ
Genomic DNA
AY065453
EMBL· GenBank· DDBJ
AAL38894.1
EMBL· GenBank· DDBJ
mRNA
AY117284
EMBL· GenBank· DDBJ
AAM51359.1
EMBL· GenBank· DDBJ
mRNA
AY085857
EMBL· GenBank· DDBJ
AAM63070.1
EMBL· GenBank· DDBJ
mRNA
AF225983
EMBL· GenBank· DDBJ
AAF37279.4
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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