Q8W2F3 · PIF4_ARATH

Function

function

Transcription factor acting negatively in the phytochrome B signaling pathway. May regulate the expression of a subset of genes involved in cell expansion by binding to the G-box motif (By similarity).
Activated by CRY1 and CRY2 in response to low blue light (LBL) by direct binding at chromatin on E-box variant 5'-CA[CT]GTG-3' to stimulate specific gene expression to adapt global physiology (e.g. hypocotyl elongation in low blue light) (PubMed:26724867).
Element of a PIF4/HMR/MED14-dependent thermoresponsive process; collaboratively with its transcriptional coactivator PTAC12/HMR/PAP5, involved in the regulation of thermoresponsive growth-relevant genes (e.g. mainly involved in biosynthesis and signaling of the phytohormone auxin) leading to daytime warm temperature elicitation of MED14-dependent thermomorphogenesis (e.g. hypocotyl elongation) (PubMed:30635559, PubMed:33824329, PubMed:36063057).

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 Componentnucleus
Molecular FunctionDNA binding
Molecular FunctionDNA-binding transcription factor activity
Molecular Functionpromoter-specific chromatin binding
Molecular Functionprotein dimerization activity
Biological Processde-etiolation
Biological Processphototropism
Biological Processpositive regulation of thermomorphogenesis
Biological Processred light signaling pathway
Biological Processred or far-red light signaling pathway
Biological Processred, far-red light phototransduction
Biological Processregulation of auxin biosynthetic process
Biological Processregulation of auxin mediated signaling pathway
Biological Processregulation of plant organ morphogenesis
Biological Processregulation of transcription by RNA polymerase II
Biological Processresponse to auxin
Biological Processresponse to cold
Biological Processresponse to ethylene
Biological Processresponse to heat
Biological Processresponse to low fluence blue light stimulus by blue low-fluence system
Biological Processresponse to salt
Biological Processresponse to temperature stimulus

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Transcription factor PIF4
  • Alternative names
    • Basic helix-loop-helix protein 9
      (AtbHLH9
      ; bHLH 9
      )
    • Phytochrome-interacting factor 4
    • Short under red-light 2
    • Transcription factor EN 102
    • bHLH transcription factor bHLH009

Gene names

    • Name
      PIF4
    • Synonyms
      BHLH9
      , EN102
      , SRL2
    • ORF names
      MFL8.13
    • Ordered locus names
      At2g43010

Organism names

  • Taxonomic identifier
  • Strains
    • cv. Wassilewskija
    • cv. Columbia
    • cv. An-2
    • cv. Bla-6
    • cv. Br-0
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    Q8W2F3
  • Secondary accessions
    • A5Y7D4
    • A5Y7D5
    • A5Y7D6
    • A5Y7D7
    • A5Y7D8

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

Reduced responses to warm temperature (e.g. 27 degrees Celsius), including thermoresponsive growth-relevant genes expression and hypocotyl growth; this phenotype is stronger in the doule mutant lacking both PIF4 and PTAC12/HMR/PAP5.

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variant231in strain: cv. Bla-6, cv. Et-0, cv. Li-5:3, cv. Mt-0, cv. Pa-2 and cv. Tsu-1

Variants

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

The viewer provides 32 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001274291-430Transcription factor PIF4

Proteomic databases

PTM databases

Expression

Tissue specificity

Mainly expressed in leaves, stems and seedlings, and, to a lower extent, in fruits, flowers and roots.

Induction

By UV treatment. Down-regulated by ethylene (ACC) and auxin (IAA), but up-regulated by salt (NaCl), cold and heat (PubMed:23708772).
Follows a free-running robust circadian rhythm, with higher levels during the light phase (PubMed:23708772).
Rapidly induced by light in etiolated plants. Sixfold induction by both red and far-red light. Accumulates in response to warm temperatures (e.g. 27 degrees Celsius) via PTAC12/HMR/PAP5-mediated stabilization in the light (PubMed:30635559, PubMed:33824329).

Developmental stage

Expressed in maturating seeds, dry seeds and upon seed imbibition.

Gene expression databases

Interaction

Subunit

Interacts preferentially with the Pfr form of phytochrome B (phyB). Binds DNA as a homodimer, but once bound to DNA, loses its capacity to interact with phyB. Interacts with APRR1/TOC1 and PIF3. Binds to RGL2 and RGA. Forms non-functional heterodimer with HFR1. Interacts with PHYB, CRY1 and CRY2 in the nucleus in response to low blue light (LBL) (PubMed:12826627, PubMed:12897250, PubMed:20093430, PubMed:23224238, PubMed:26724867).
Interacts with FYPP1 and FYPP3 (PubMed:31527236).
Associates to PTAC12/HMR/PAP5, which acts as a transcriptional coactivator to trigger the thermoresponsive growth-relevant genes and promote warm-temperature-dependent PIF4 accumulation (PubMed:25944101, PubMed:30635559).
Interacts with MED14 (PubMed:36063057).

Binary interactions

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region42-71Disordered
Compositional bias48-64Basic and acidic residues
Compositional bias97-112Polar residues
Region97-136Disordered
Compositional bias116-136Pro residues
Compositional bias160-177Polar residues
Region160-183Disordered
Region223-266Disordered
Compositional bias235-254Polar residues
Domain257-306bHLH
Compositional bias405-423Polar residues
Region405-430Disordered

Sequence similarities

Belongs to the bHLH protein family.

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q8W2F3-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Name
    Long
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    430
  • Mass (Da)
    48,363
  • Last updated
    2002-03-01 v1
  • Checksum
    B4C081D0BF907C26
MEHQGWSFEENYSLSTNRRSIRPQDELVELLWRDGQVVLQSQTHREQTQTQKQDHHEEALRSSTFLEDQETVSWIQYPPDEDPFEPDDFSSHFFSTMDPLQRPTSETVKPKSSPEPPQVMVKPKACPDPPPQVMPPPKFRLTNSSSGIRETEMEQYSVTTVGPSHCGSNPSQNDLDVSMSHDRSKNIEEKLNPNASSSSGGSSGCSFGKDIKEMASGRCITTDRKRKRINHTDESVSLSDAIGNKSNQRSGSNRRSRAAEVHNLSERRRRDRINERMKALQELIPHCSKTDKASILDEAIDYLKSLQLQLQVMWMGSGMAAAAASAPMMFPGVQPQQFIRQIQSPVQLPRFPVMDQSAIQNNPGLVCQNPVQNQIISDRFARYIGGFPHMQAATQMQPMEMLRFSSPAGQQSQQPSSVPTKTTDGSRLDH

Q8W2F3-2

  • Name
    Short
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
F4IQ51F4IQ51_ARATHPIF4428
A0A1P8AX01A0A1P8AX01_ARATHPIF4437
A0A1P8AX08A0A1P8AX08_ARATHPIF4472
A0A178VYH3A0A178VYH3_ARATHPIF4404

Features

Showing features for compositional bias, sequence conflict, alternative sequence.

TypeIDPosition(s)Description
Compositional bias48-64Basic and acidic residues
Compositional bias97-112Polar residues
Compositional bias116-136Pro residues
Compositional bias160-177Polar residues
Sequence conflict204in Ref. 5; AAK25931
Compositional bias235-254Polar residues
Alternative sequenceVSP_002146268-279in isoform Short
Alternative sequenceVSP_002147280-430in isoform Short
Compositional bias405-423Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJ440755
EMBL· GenBank· DDBJ
CAD29449.1
EMBL· GenBank· DDBJ
mRNA
AF251694
EMBL· GenBank· DDBJ
AAL55716.1
EMBL· GenBank· DDBJ
mRNA
AC006224
EMBL· GenBank· DDBJ
AAD22130.2
EMBL· GenBank· DDBJ
Genomic DNA
CP002685
EMBL· GenBank· DDBJ
AEC10197.1
EMBL· GenBank· DDBJ
Genomic DNA
AY142625
EMBL· GenBank· DDBJ
AAN13083.1
EMBL· GenBank· DDBJ
mRNA
AF360221
EMBL· GenBank· DDBJ
AAK25931.1
EMBL· GenBank· DDBJ
mRNA
EF193514
EMBL· GenBank· DDBJ
ABP96467.1
EMBL· GenBank· DDBJ
Genomic DNA
EF193515
EMBL· GenBank· DDBJ
ABP96468.1
EMBL· GenBank· DDBJ
Genomic DNA
EF193516
EMBL· GenBank· DDBJ
ABP96469.1
EMBL· GenBank· DDBJ
Genomic DNA
EF193517
EMBL· GenBank· DDBJ
ABP96470.1
EMBL· GenBank· DDBJ
Genomic DNA
EF193518
EMBL· GenBank· DDBJ
ABP96471.1
EMBL· GenBank· DDBJ
Genomic DNA
EF193519
EMBL· GenBank· DDBJ
ABP96472.1
EMBL· GenBank· DDBJ
Genomic DNA
EF193520
EMBL· GenBank· DDBJ
ABP96473.1
EMBL· GenBank· DDBJ
Genomic DNA
EF193521
EMBL· GenBank· DDBJ
ABP96474.1
EMBL· GenBank· DDBJ
Genomic DNA
EF193522
EMBL· GenBank· DDBJ
ABP96475.1
EMBL· GenBank· DDBJ
Genomic DNA
EF193523
EMBL· GenBank· DDBJ
ABP96476.1
EMBL· GenBank· DDBJ
Genomic DNA
EF193524
EMBL· GenBank· DDBJ
ABP96477.1
EMBL· GenBank· DDBJ
Genomic DNA
EF193525
EMBL· GenBank· DDBJ
ABP96478.1
EMBL· GenBank· DDBJ
Genomic DNA
EF193526
EMBL· GenBank· DDBJ
ABP96479.1
EMBL· GenBank· DDBJ
Genomic DNA
EF193527
EMBL· GenBank· DDBJ
ABP96480.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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