Q8W2F3 · PIF4_ARATH
- ProteinTranscription factor PIF4
- GenePIF4
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids430 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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 annotations | all molecular function | nucleotide binding | molecular_function | nucleic acid binding | dna binding | chromatin binding | dna-binding transcription factor activity | rna binding | cytoskeletal motor activity | catalytic activity | nuclease activity | signaling receptor binding | structural molecule activity | transporter activity | binding | protein binding | translation factor activity, rna binding | lipid binding | kinase activity | transferase activity | hydrolase activity | oxygen binding | enzyme regulator activity | carbohydrate binding | signaling receptor activity | translation regulator activity | transcription regulator activity | other molecular function | all biological process | carbohydrate metabolic process | generation of precursor metabolites and energy | nucleobase-containing compound metabolic process | dna metabolic process | translation | lipid metabolic process | transport | response to stress | cell cycle | cell communication | signal transduction | cell-cell signaling | multicellular organism development | circadian rhythm | biological_process | metabolic process | catabolic process | biosynthetic process | response to light stimulus | response to external stimulus | tropism | response to biotic stimulus | response to abiotic stimulus | response to endogenous stimulus | embryo development | post-embryonic development | fruit ripening | abscission | pollination | flower development | cellular process | programmed cell death | photosynthesis | cellular component organization | cell growth | protein metabolic process | cellular homeostasis | secondary metabolic process | reproductive process | cell differentiation | protein modification process | growth | epigenetic regulation of gene expression | response to chemical | anatomical structure development | regulation of molecular function | other biological process | all cellular component | cellular_component | extracellular region | cell wall | intracellular anatomical structure | nucleus | nuclear envelope | nucleoplasm | nucleolus | cytoplasm | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | cytosol | ribosome | cytoskeleton | plasma membrane | chloroplast | plastid | thylakoid | membrane | external encapsulating structure | other cellular component | |||
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Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameTranscription factor PIF4
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ8W2F3
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 231 | in strain: cv. Bla-6, cv. Et-0, cv. Li-5:3, cv. Mt-0, cv. Pa-2 and cv. Tsu-1 | ||||
Sequence: H → D |
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.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000127429 | 1-430 | Transcription factor PIF4 | |||
Sequence: MEHQGWSFEENYSLSTNRRSIRPQDELVELLWRDGQVVLQSQTHREQTQTQKQDHHEEALRSSTFLEDQETVSWIQYPPDEDPFEPDDFSSHFFSTMDPLQRPTSETVKPKSSPEPPQVMVKPKACPDPPPQVMPPPKFRLTNSSSGIRETEMEQYSVTTVGPSHCGSNPSQNDLDVSMSHDRSKNIEEKLNPNASSSSGGSSGCSFGKDIKEMASGRCITTDRKRKRINHTDESVSLSDAIGNKSNQRSGSNRRSRAAEVHNLSERRRRDRINERMKALQELIPHCSKTDKASILDEAIDYLKSLQLQLQVMWMGSGMAAAAASAPMMFPGVQPQQFIRQIQSPVQLPRFPVMDQSAIQNNPGLVCQNPVQNQIISDRFARYIGGFPHMQAATQMQPMEMLRFSSPAGQQSQQPSSVPTKTTDGSRLDH |
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).
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).
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
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8W2F3 | BZR1 Q8S307 | 4 | EBI-625716, EBI-1803261 | |
BINARY | Q8W2F3 | HFR1 Q9FE22 | 2 | EBI-625716, EBI-626001 | |
BINARY | Q8W2F3 | RGA Q9SLH3 | 4 | EBI-625716, EBI-963624 | |
BINARY | Q8W2F3-2 | PHYA P14712 | 2 | EBI-625732, EBI-624446 | |
BINARY | Q8W2F3-2 | PHYB P14713 | 3 | EBI-625732, EBI-300727 | |
BINARY | Q8W2F3-2 | PIF3 O80536 | 3 | EBI-625732, EBI-625701 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 42-71 | Disordered | ||||
Sequence: QTHREQTQTQKQDHHEEALRSSTFLEDQET | ||||||
Compositional bias | 48-64 | Basic and acidic residues | ||||
Sequence: TQTQKQDHHEEALRSST | ||||||
Compositional bias | 97-112 | Polar residues | ||||
Sequence: MDPLQRPTSETVKPKS | ||||||
Region | 97-136 | Disordered | ||||
Sequence: MDPLQRPTSETVKPKSSPEPPQVMVKPKACPDPPPQVMPP | ||||||
Compositional bias | 116-136 | Pro residues | ||||
Sequence: PPQVMVKPKACPDPPPQVMPP | ||||||
Compositional bias | 160-177 | Polar residues | ||||
Sequence: TVGPSHCGSNPSQNDLDV | ||||||
Region | 160-183 | Disordered | ||||
Sequence: TVGPSHCGSNPSQNDLDVSMSHDR | ||||||
Region | 223-266 | Disordered | ||||
Sequence: DRKRKRINHTDESVSLSDAIGNKSNQRSGSNRRSRAAEVHNLSE | ||||||
Compositional bias | 235-254 | Polar residues | ||||
Sequence: SVSLSDAIGNKSNQRSGSNR | ||||||
Domain | 257-306 | bHLH | ||||
Sequence: RAAEVHNLSERRRRDRINERMKALQELIPHCSKTDKASILDEAIDYLKSL | ||||||
Compositional bias | 405-423 | Polar residues | ||||
Sequence: SSPAGQQSQQPSSVPTKTT | ||||||
Region | 405-430 | Disordered | ||||
Sequence: SSPAGQQSQQPSSVPTKTTDGSRLDH |
Sequence similarities
Belongs to the bHLH protein family.
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
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.
- NameLong
- Length430
- Mass (Da)48,363
- Last updated2002-03-01 v1
- ChecksumB4C081D0BF907C26
Q8W2F3-2
- NameShort
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F4IQ51 | F4IQ51_ARATH | PIF4 | 428 | ||
A0A1P8AX01 | A0A1P8AX01_ARATH | PIF4 | 437 | ||
A0A1P8AX08 | A0A1P8AX08_ARATH | PIF4 | 472 | ||
A0A178VYH3 | A0A178VYH3_ARATH | PIF4 | 404 |
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 48-64 | Basic and acidic residues | ||||
Sequence: TQTQKQDHHEEALRSST | ||||||
Compositional bias | 97-112 | Polar residues | ||||
Sequence: MDPLQRPTSETVKPKS | ||||||
Compositional bias | 116-136 | Pro residues | ||||
Sequence: PPQVMVKPKACPDPPPQVMPP | ||||||
Compositional bias | 160-177 | Polar residues | ||||
Sequence: TVGPSHCGSNPSQNDLDV | ||||||
Sequence conflict | 204 | in Ref. 5; AAK25931 | ||||
Sequence: G → S | ||||||
Compositional bias | 235-254 | Polar residues | ||||
Sequence: SVSLSDAIGNKSNQRSGSNR | ||||||
Alternative sequence | VSP_002146 | 268-279 | in isoform Short | |||
Sequence: RRRDRINERMKA → VLHRFVYIIYNI | ||||||
Alternative sequence | VSP_002147 | 280-430 | in isoform Short | |||
Sequence: Missing | ||||||
Compositional bias | 405-423 | Polar residues | ||||
Sequence: SSPAGQQSQQPSSVPTKTT |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |