PlantTFDB
PlantRegMap/PlantTFDB v5.0
Plant Transcription Factor Database
Transcription Factor Information
Basic Information | Signature Domain | Sequence | 
Basic Information? help Back to Top
TF ID Gh_D05G2577
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium
Family bZIP
Protein Properties Length: 323aa    MW: 35485.4 Da    PI: 8.1611
Description bZIP family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Gh_D05G2577genomeNAU-NBIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1bZIP_126.91e-08167225563
                  CHHHCHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHH CS
       bZIP_1   5 krerrkqkNReAArrsRqRKkaeieeLeekvkeLeaeNkaLkkeleelkkevaklksev 63 
                  kr++r   NR +A rs +RK  ++ eLe+kv++L++e + L  ++  l+     l++e+
  Gh_D05G2577 167 KRAKRILANRQSAARSKERKIRYTSELERKVQTLQTEATNLSAQVTVLQRDTTGLTTEN 225
                  9****************************************999988887776666665 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
SMARTSM003381.1E-15163227IPR004827Basic-leucine zipper domain
PROSITE profilePS5021710.921165228IPR004827Basic-leucine zipper domain
Gene3DG3DSA:1.20.5.1702.9E-10167221No hitNo description
PfamPF001708.5E-8167224IPR004827Basic-leucine zipper domain
SuperFamilySSF579599.85E-11167219No hitNo description
CDDcd147033.11E-23168217No hitNo description
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0006355Biological Processregulation of transcription, DNA-templated
GO:0003700Molecular Functiontranscription factor activity, sequence-specific DNA binding
GO:0043565Molecular Functionsequence-specific DNA binding
Sequence ? help Back to Top
Protein Sequence    Length: 323 aa     Download sequence    Send to blast
MDKIPPRGVH HRRAHSDTTF RFDDLLLFDP SDLDLSSLDL PASSSNPTPP PVVPVPIYSS  60
DDSSSNGHHP RSSHSNPRQI SSHLRSLSVD SDFFDGLGLT GPAISGGAGD EKFGGKGAAG  120
EKRVHHRNSN SMDGTASFEV ESLMAVGGVK KAIAPDRLAE LALIDPKRAK RILANRQSAA  180
RSKERKIRYT SELERKVQTL QTEATNLSAQ VTVLQRDTTG LTTENKELKL RLQAMEQQAQ  240
LRDALNEALR EEVQRLKIQA GQMSAMNGNH FNSGLPQFFS HQPSPHHFGG QQTPQQQQHQ  300
QMPESSTNNG HPQPQFMDFN QGA
Expression -- UniGene ? help Back to Top
UniGene ID E-value Expressed in
Ghi.212580.0boll
Expression -- Description ? help Back to Top
Source Description
UniprotTISSUE SPECIFICITY: Mostly expressed in dividing cells, present in leaves, roots and seedlings. {ECO:0000269|PubMed:15108305, ECO:0000269|PubMed:15824315}.
Functional Description ? help Back to Top
Source Description
UniProtTranscription 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. {ECO:0000269|PubMed:11432846, ECO:0000269|PubMed:12124400, ECO:0000269|PubMed:15108305, ECO:0000269|PubMed:15824315, ECO:0000269|PubMed:17947581, ECO:0000269|PubMed:19820165, ECO:0000269|PubMed:20547563}.
Regulation -- Description ? help Back to Top
Source Description
UniProtINDUCTION: 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. {ECO:0000269|PubMed:15108305}.
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_016687329.10.0PREDICTED: transcription factor VIP1-like
SwissprotQ9MA751e-89VIP1_ARATH; Transcription factor VIP1
TrEMBLA0A1U8JGC10.0A0A1U8JGC1_GOSHI; transcription factor VIP1-like
STRINGGorai.009G285000.10.0(Gossypium raimondii)
Orthologous Group ? help Back to Top
LineageOrthologous Group IDTaxa NumberGene Number
MalvidsOGEM79932639
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT1G43700.12e-74VIRE2-interacting protein 1
Publications ? help Back to Top
  1. Wang Y, et al.
    The putative Agrobacterium transcriptional activator-like virulence protein VirD5 may target T-complex to prevent the degradation of coat proteins in the plant cell nucleus.
    New Phytol., 2014. 203(4): p. 1266-81
    [PMID:24865527]
  2. Xu DB, et al.
    A G-protein β subunit, AGB1, negatively regulates the ABA response and drought tolerance by down-regulating AtMPK6-related pathway in Arabidopsis.
    PLoS ONE, 2015. 10(1): p. e0116385
    [PMID:25635681]
  3. Chen J, et al.
    ZmbZIP91 regulates expression of starch synthesis-related genes by binding to ACTCAT elements in their promoters.
    J. Exp. Bot., 2016. 67(5): p. 1327-38
    [PMID:26689855]
  4. Tsugama D,Liu S,Takano T
    VIP1 is very important/interesting protein 1 regulating touch responses of Arabidopsis.
    Plant Signal Behav, 2016. 11(6): p. e1187358
    [PMID:27171129]
  5. Tsugama D,Liu S,Takano T
    The bZIP Protein VIP1 Is Involved in Touch Responses in Arabidopsis Roots.
    Plant Physiol., 2016. 171(2): p. 1355-65
    [PMID:27208231]
  6. Takeo K,Ito T
    Subcellular localization of VIP1 is regulated by phosphorylation and 14-3-3 proteins.
    FEBS Lett., 2017. 591(13): p. 1972-1981
    [PMID:28542772]
  7. Wang L,Lacroix B,Guo J,Citovsky V
    The Agrobacterium VirE2 effector interacts with multiple members of the Arabidopsis VIP1 protein family.
    Mol. Plant Pathol., 2018. 19(5): p. 1172-1183
    [PMID:28802023]