O80536 · PIF3_ARATH

Function

function

Transcription factor acting in the phytochrome signaling pathway (PubMed:10466729, PubMed:14508006).
Activates transcription by binding to the G box (5'-CACGTG-3'), particularly in the dark but barely in far-red light (PubMed:10797009, PubMed:31732705).
Acts as a negative regulator of phytochrome B signaling (PubMed:14508006).
Represses chlorophyll biosynthesis and photosynthesis in the dark (PubMed:23548744).
Recruits the histone deacetylase HDA15 to the promoters of chlorophyll biosynthetic and photosynthetic genes (PubMed:23548744).
HDA15 represses their transcription by histone deacetylation (PubMed:23548744).
Promotes the expression of MDP60 to modulate hypocotyl cell elongation in response to light and ethylene signaling (PubMed:29167353).
Required for submergence-induced and ethylene-dependent underwater hypocotyl elongation (PubMed:31638649).

Activity regulation

Sequestered by PhyA from its target genes promoters in far-red light.

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 Functionidentical protein binding
Molecular Functionprotein dimerization activity
Molecular Functionsequence-specific DNA binding
Molecular Functiontranscription cis-regulatory region binding
Biological Processde-etiolation
Biological Processgibberellic acid mediated signaling pathway
Biological Processpositive regulation of anthocyanin metabolic process
Biological Processred or far-red light signaling pathway
Biological Processred, far-red light phototransduction
Biological Processregulation of DNA-templated transcription
Biological Processregulation of photosynthesis, light reaction
Biological Processregulation of plant organ morphogenesis
Biological Processresponse to abscisic acid
Biological Processresponse to auxin
Biological Processresponse to cold
Biological Processresponse to ethylene
Biological Processresponse to heat
Biological Processresponse to red or far red light
Biological Processresponse to salt
Biological Processresponse to water-immersion restraint stress
Biological Processunidimensional cell growth

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Transcription factor PIF3
  • Alternative names
    • Basic helix-loop-helix protein 8
      (AtbHLH8
      ; bHLH 8
      )
    • Phytochrome-associated protein 3
    • Phytochrome-interacting factor 3
    • Transcription factor EN 100
    • bHLH transcription factor bHLH008

Gene names

    • Name
      PIF3
    • Synonyms
      BHLH8
      , EN100
      , PAP3
    • ORF names
      F14J9.19
    • Ordered locus names
      At1g09530

Organism names

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

Accessions

  • Primary accession
    O80536
  • Secondary accessions
    • A5Y7A2
    • A5Y7A3
    • A5Y7A4
    • A5Y7A5
    • A5Y7A6

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

Inhibited submergence-induced and ethylene-dependent underwater hypocotyl elongation.

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variant124in strain: cv. An-2 and cv. Su-0
Natural variant141in strain: cv. An-2 and cv. Su-0
Natural variant176in strain: cv. An-2 and cv. Su-0
Natural variant186in strain: cv. An-2 and cv. Su-0
Natural variant209in strain: cv. An-2 and cv. Su-0
Natural variant220in strain: cv. An-2 and cv. Su-0
Natural variant236in strain: cv. An-2 and cv. Su-0

Variants

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

The viewer provides 39 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_00001274281-524Transcription factor PIF3

Post-translational modification

Phosphorylated by PHYA; this phosphorylation is repressed by PIA2.
Dephosphorylated by TOPP4 during photomorphogenesis, leading to subsequent degradation of PIF3 by the proteasomal pathway.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

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

Induction

By UV treatment (PubMed:12679534).
Repressed by red (R) and far red (FR) light treatments in a phyB- and phyA-dependent manner, and via a PTAC12/HMR/PAP5 regulated process (PubMed:25944101).
Up-regulated by abscisic acid (ABA), ethylene (ACC), auxin (IAA), salt (NaCl), cold and heat (PubMed:23708772).
Follows a tenous circadian rhythm with slightly higher levels at the end of the light phase (PubMed:23708772).

Developmental stage

Accumulates progressively in maturating seeds to reach a peak in dry seeds (PubMed:23708772).
Expressed upon seed imbibition (PubMed:23708772).

Gene expression databases

Interaction

Subunit

Homodimer (PubMed:25944101).
Can form a heterodimer with REP1 and PIF4. Phytochrome B binds specifically to DNA-bound PIF3, but only upon red light induced conversion to the Pfr form (PfrB). Reconversion to Pr form causes rapid dissociation. Interacts with APRR1/TOC1. Binds to PIA2; this interaction may trigger the repression of PHYA-mediated phosphorylation (PubMed:27143545).
Interacts with TOPP4 (Probable) (PubMed:11828023, PubMed:12826627, PubMed:12897250, PubMed:26704640, PubMed:27143545).
Interacts with FYPP1 and FYPP3 (PubMed:31527236).
Interacts with HDA15 in the dark (PubMed:23548744).
Associates to PTAC12/HMR/PAP5 which acts as a transcriptional coactivator (PubMed:25944101).
Binds to PhyA (PubMed:31732705).

Binary interactions

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for compositional bias, region, domain.

TypeIDPosition(s)Description
Compositional bias38-66Polar residues
Region38-70Disordered
Region141-194Disordered
Compositional bias145-194Polar residues
Region239-259Disordered
Compositional bias281-305Polar residues
Region281-358Disordered
Compositional bias306-329Basic and acidic residues
Domain343-392bHLH
Region483-524Disordered

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    524
  • Mass (Da)
    56,990
  • Last updated
    1998-11-01 v1
  • Checksum
    1044AC01D598DE7C
MPLFELFRLTKAKLESAQDRNPSPPVDEVVELVWENGQISTQSQSSRSRNIPPPQANSSRAREIGNGSKTTMVDEIPMSVPSLMTGLSQDDDFVPWLNHHPSLDGYCSDFLRDVSSPVTVNEQESDMAVNQTAFPLFQRRKDGNESAPAASSSQYNGFQSHSLYGSDRARDLPSQQTNPDRFTQTQEPLITSNKPSLVNFSHFLRPATFAKTTNNNLHDTKEKSPQSPPNVFQTRVLGAKDSEDKVLNESVASATPKDNQKACLISEDSCRKDQESEKAVVCSSVGSGNSLDGPSESPSLSLKRKHSNIQDIDCHSEDVEEESGDGRKEAGPSRTGLGSKRSRSAEVHNLSERRRRDRINEKMRALQELIPNCNKVDKASMLDEAIEYLKSLQLQVQIMSMASGYYLPPAVMFPPGMGHYPAAAAAMAMGMGMPYAMGLPDLSRGGSSVNHGPQFQVSGMQQQPVAMGIPRVSGGGIFAGSSTIGNGSTRDLSGSKDQTTTNNNSNLKPIKRKQGSSDQFCGSS

Features

Showing features for sequence conflict, compositional bias.

TypeIDPosition(s)Description
Sequence conflict15in Ref. 3; AAC99771
Compositional bias38-66Polar residues
Compositional bias145-194Polar residues
Compositional bias281-305Polar residues
Compositional bias306-329Basic and acidic residues
Sequence conflict344in Ref. 3; AAC99771

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF100166
EMBL· GenBank· DDBJ
AAC95156.1
EMBL· GenBank· DDBJ
mRNA
AF251693
EMBL· GenBank· DDBJ
AAL55715.1
EMBL· GenBank· DDBJ
mRNA
AF088280
EMBL· GenBank· DDBJ
AAC99771.1
EMBL· GenBank· DDBJ
mRNA
AC003970
EMBL· GenBank· DDBJ
AAC33213.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002684
EMBL· GenBank· DDBJ
AEE28457.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002684
EMBL· GenBank· DDBJ
AEE28458.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002684
EMBL· GenBank· DDBJ
ANM60410.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002684
EMBL· GenBank· DDBJ
ANM60411.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002684
EMBL· GenBank· DDBJ
ANM60412.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002684
EMBL· GenBank· DDBJ
ANM60413.1
EMBL· GenBank· DDBJ
Genomic DNA
AK117255
EMBL· GenBank· DDBJ
BAC41930.1
EMBL· GenBank· DDBJ
mRNA
EF193482
EMBL· GenBank· DDBJ
ABP96435.1
EMBL· GenBank· DDBJ
Genomic DNA
EF193483
EMBL· GenBank· DDBJ
ABP96436.1
EMBL· GenBank· DDBJ
Genomic DNA
EF193484
EMBL· GenBank· DDBJ
ABP96437.1
EMBL· GenBank· DDBJ
Genomic DNA
EF193485
EMBL· GenBank· DDBJ
ABP96438.1
EMBL· GenBank· DDBJ
Genomic DNA
EF193486
EMBL· GenBank· DDBJ
ABP96439.1
EMBL· GenBank· DDBJ
Genomic DNA
EF193487
EMBL· GenBank· DDBJ
ABP96440.1
EMBL· GenBank· DDBJ
Genomic DNA
EF193488
EMBL· GenBank· DDBJ
ABP96441.1
EMBL· GenBank· DDBJ
Genomic DNA
EF193489
EMBL· GenBank· DDBJ
ABP96442.1
EMBL· GenBank· DDBJ
Genomic DNA
EF193490
EMBL· GenBank· DDBJ
ABP96443.1
EMBL· GenBank· DDBJ
Genomic DNA
EF193491
EMBL· GenBank· DDBJ
ABP96444.1
EMBL· GenBank· DDBJ
Genomic DNA
EF193492
EMBL· GenBank· DDBJ
ABP96445.1
EMBL· GenBank· DDBJ
Genomic DNA
EF193493
EMBL· GenBank· DDBJ
ABP96446.1
EMBL· GenBank· DDBJ
Genomic DNA
EF193494
EMBL· GenBank· DDBJ
ABP96447.1
EMBL· GenBank· DDBJ
Genomic DNA
EF193495
EMBL· GenBank· DDBJ
ABP96448.1
EMBL· GenBank· DDBJ
Genomic DNA
EF193496
EMBL· GenBank· DDBJ
ABP96449.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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