Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Automatic assignment of GO terms using logical inference, based on on inter-ontology links
Combined Automated Annotation using Multiple IEA Methods
PtdIns4P synthesis by PI4KIIIα at the plasma membrane and its impact on plasma membrane identity.
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Human EFR3A is palmitoylated on its N-terminal Cys6-Cys9 cluster, which is required for plasma-membrane localization; EFR3 is part of an evolutionarily conserved PI4KIIIalpha complex that targets the kinase to the plasma membrane.
"we show that PI4KIIIα was targeted to the plasma membrane as part of an evolutionarily conserved complex containing Efr3/rolling blackout, which we found was a palmitoylated peripheral membrane protein."
EFR3s are palmitoylated plasma membrane proteins that control responsiveness to G-protein-coupled receptors.
Plasticity of PI4KIIIα interactions at the plasma membrane.
The leukodystrophy protein FAM126A (hyccin) regulates PtdIns(4)P synthesis at the plasma membrane.
Molecular basis for plasma membrane recruitment of PI4KA by EFR3.
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The EFR3A C terminus (residues 724-787) folds on binding TTC7B-FAM126A, directly contacting both; disrupting this interface lowers PI4KA plasma-membrane recruitment. No direct EFR3A-PI4KA contact was seen.
"The EFR3A C terminus undergoes a disorder-order transition upon binding to the PI4KA complex, with an unexpected direct interaction with both TTC7B and FAM126A."
Structural insights into assembly and regulation of the plasma membrane phosphatidylinositol 4-kinase complex.
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Structure of yeast Efr3-Ypp1; a conserved Efr3 basic patch binds acidic phospholipids. The equivalent basic-patch mutant of mouse EFR3A (K50E/R53A/R61E/R68E/R70E) loses plasma-membrane localization.
"Whereas wild-type EFR3A-GFP localized to the plasma membrane"
Amyloid β oligomers suppress excitatory transmitter release via presynaptic depletion of phosphatidylinositol-4,5-bisphosphate.
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Halving or presynaptically deleting mouse Efr3a prevents amyloid-beta-induced PIP2 depletion and loss of release probability; Efr3a was used to reduce Gq-coupled GPCR responsiveness.
"Taken together, these results indicate that reducing Efr3a is an effective method to inhibit Aβ-induced PIP2 depletion."
EFR3A: a new raft domain organizing protein?
Rare deleterious mutations of the gene EFR3A in autism spectrum disorders.
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Rare nonsynonymous EFR3A variants were enriched in ASD cases versus controls, and EFR3A is expressed in fetal cortical neurons.
"Rare nonsynonymous mutations in EFR3A were more common among cases (16 / 2,196 = 0.73%) than matched controls (12 / 3,389 = 0.35%)"
UniProt record for human EFR3A