Q9M4B5 · PFD4_ARATH
- ProteinPrefoldin subunit 4
- GenePFD4
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids129 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it (PubMed:19825635).
Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins (PubMed:19825635).
Together with other chaperonins, contribute to the regulation of gene expression by modulating the spliceosome function on pre-mRNA splicing post-transcriptionally by acting as a co-chaperone of Hsp90 to control levels of LSM8, especially in cold conditions (PubMed:32396196).
Required for microtubules (MTs) (MTs) organization and dynamicity (PubMed:19004800, PubMed:28412546).
Involved in the process leading to microtubules dissociation in response to gibberellic acid (GA) probably due to the DELLA proteins-mediated translocation of the prefoldin co-chaperone complex from the cytoplasm to the nucleus (PubMed:28412546).
Prevents cold acclimation (e.g. 7 days at 4 degrees Celsius) in a DELLA proteins-dependent manner by promoting nuclear proteasome-mediated HY5 degradation, thus modulating the expression of several genes and reducing anthocyanin biosynthesis, but seems not involved in constitutive freezing tolerance (PubMed:28412546).
Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins (PubMed:19825635).
Together with other chaperonins, contribute to the regulation of gene expression by modulating the spliceosome function on pre-mRNA splicing post-transcriptionally by acting as a co-chaperone of Hsp90 to control levels of LSM8, especially in cold conditions (PubMed:32396196).
Required for microtubules (MTs) (MTs) organization and dynamicity (PubMed:19004800, PubMed:28412546).
Involved in the process leading to microtubules dissociation in response to gibberellic acid (GA) probably due to the DELLA proteins-mediated translocation of the prefoldin co-chaperone complex from the cytoplasm to the nucleus (PubMed:28412546).
Prevents cold acclimation (e.g. 7 days at 4 degrees Celsius) in a DELLA proteins-dependent manner by promoting nuclear proteasome-mediated HY5 degradation, thus modulating the expression of several genes and reducing anthocyanin biosynthesis, but seems not involved in constitutive freezing tolerance (PubMed:28412546).
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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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Cellular Component | prefoldin complex | |
Molecular Function | Hsp90 protein binding | |
Molecular Function | unfolded protein binding | |
Biological Process | cellular response to gibberellin stimulus | |
Biological Process | cold acclimation | |
Biological Process | cortical microtubule organization | |
Biological Process | mRNA processing | |
Biological Process | protein folding | |
Biological Process | response to cold | |
Biological Process | response to salt stress |
Keywords
- Molecular function
Names & Taxonomy
Protein names
- Recommended namePrefoldin subunit 4
- 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 accessionQ9M4B5
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: In the presence of gibberellic acid (GA) and at room temperature, the prefoldin complex stays in the cytoplasm and is functional (PubMed:28412546).
But in the absence of GA or in response to cold, the prefoldin complex is localized to the nucleus in the presence of DELLA proteins, which severely compromises alpha/beta-tubulin heterodimer availability, thus affecting microtubules (MTs) organization (PubMed:28412546).
This changing subcellular localization follows a daily rhythm coordinated oscillation (By similarity).
But in the absence of GA or in response to cold, the prefoldin complex is localized to the nucleus in the presence of DELLA proteins, which severely compromises alpha/beta-tubulin heterodimer availability, thus affecting microtubules (MTs) organization (PubMed:28412546).
This changing subcellular localization follows a daily rhythm coordinated oscillation (By similarity).
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Hypersensitivity to oryzalin (a microtubule inhibitor) (PubMed:19004800).
Increased sensitivity to high salt treatment (PubMed:32396196).
Smaller plants due to reduced cells size and associated with lower levels of both alpha and beta tubulin subunits, as well as highly disorganized cortical microtubules (MTs) (PubMed:28412546, PubMed:32396196).
Increased capacity to tolerate freezing temperatures upon acclimation (e.g. 7 days at 4 degrees Celsius) associated with a continuous accumulation of HY5 in cold conditions, characterized by a lower ubiquitination status (PubMed:28412546).
Reduced levels of LSM8 and of LSM2-8 complex via a post-transcriptional process, especially in cold conditions (at protein level) (PubMed:32396196).
Slightly reduced production of U6 snRNA at room temperature, but to higher extent in cold situation (PubMed:32396196).
Lower pre-mRNA splicing events and reduced production of U6 snRNA in plants lacking PFD2, PFD4 and PFD6, probably due to a reduced activity of the LSM2-8 complex (PubMed:32396196).
Increased sensitivity to high salt treatment (PubMed:32396196).
Smaller plants due to reduced cells size and associated with lower levels of both alpha and beta tubulin subunits, as well as highly disorganized cortical microtubules (MTs) (PubMed:28412546, PubMed:32396196).
Increased capacity to tolerate freezing temperatures upon acclimation (e.g. 7 days at 4 degrees Celsius) associated with a continuous accumulation of HY5 in cold conditions, characterized by a lower ubiquitination status (PubMed:28412546).
Reduced levels of LSM8 and of LSM2-8 complex via a post-transcriptional process, especially in cold conditions (at protein level) (PubMed:32396196).
Slightly reduced production of U6 snRNA at room temperature, but to higher extent in cold situation (PubMed:32396196).
Lower pre-mRNA splicing events and reduced production of U6 snRNA in plants lacking PFD2, PFD4 and PFD6, probably due to a reduced activity of the LSM2-8 complex (PubMed:32396196).
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 8 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_0000124845 | 1-129 | Prefoldin subunit 4 | ||
Proteomic databases
PTM databases
Interaction
Subunit
Heterohexamer of two PFD-alpha type and four PFD-beta type subunits forming prefoldin co-chaperone complex (By similarity).
Interacts with ABI3 (via C-terminus) (PubMed:10743655).
Interacts with PFD6 (PubMed:19004800).
Binds to HY5 in the nucleus and at low temperature (e.g. at 4 degrees Celsius) (PubMed:28412546).
Interacts with LSM8, a specific subunit of the LSM2-8 complex, which is a core component of the spliceosome (PubMed:32396196).
Binds to HSP90 to facilitate the formation of a larger complex made at least of HSP90, PFD4 and LSM8 (PubMed:32396196).
Interacts with ABI3 (via C-terminus) (PubMed:10743655).
Interacts with PFD6 (PubMed:19004800).
Binds to HY5 in the nucleus and at low temperature (e.g. at 4 degrees Celsius) (PubMed:28412546).
Interacts with LSM8, a specific subunit of the LSM2-8 complex, which is a core component of the spliceosome (PubMed:32396196).
Binds to HSP90 to facilitate the formation of a larger complex made at least of HSP90, PFD4 and LSM8 (PubMed:32396196).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | IntAct | |
---|---|---|---|---|---|
BINARY | Q9M4B5 | ABI3 Q01593 | 2 | EBI-2130809, EBI-1578892 | |
BINARY | Q9M4B5 | MPK11 Q9LMM5 | 3 | EBI-2130809, EBI-2358699 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for coiled coil.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Coiled coil | 25-59 | ||||
Coiled coil | 95-115 | ||||
Sequence similarities
Belongs to the prefoldin subunit beta family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length129
- Mass (Da)14,881
- Last updated2011-05-31 v3
- Checksum1562DF409E43884A
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC003981 EMBL· GenBank· DDBJ | AAF99774.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CP002684 EMBL· GenBank· DDBJ | AEE28346.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT004788 EMBL· GenBank· DDBJ | AAO44054.1 EMBL· GenBank· DDBJ | mRNA | ||
AK227759 EMBL· GenBank· DDBJ | BAE99742.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ251088 EMBL· GenBank· DDBJ | CAB75510.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. |