Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniPathway vocabulary mapping
Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features
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
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
A 5-bp deletion in ELOVL4 is associated with two related forms of autosomal dominant macular dystrophy.
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Identified ELOVL4 as a retinal photoreceptor-specific gene whose 5-bp deletion causes autosomal dominant Stargardt-like macular dystrophy, and recognized its homology to yeast very-long-chain fatty acid biosynthesis proteins, first implicating fatty-acid biosynthesis in inherited macular degeneration.
"Bioinformatic analysis of ELOVL4 revealed that it has homology to a group of yeast proteins that function in the biosynthesis of very long chain fatty acids."
Dominant negative mechanism underlies autosomal dominant Stargardt-like macular dystrophy linked to mutations in ELOVL4.
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Wild-type ELOVL4 localizes to the endoplasmic reticulum via its C-terminal ER-retention sequence, and forms a complex with C-terminally truncated mutant ELOVL4, supporting oligomerization and a dominant-negative disease mechanism.
"Wild type ELOVL4 containing an endoplasmic reticulum retention sequence was localized to the endoplasmic reticulum as expected."
ELOVL1 production of C24 acyl-CoAs is linked to C24 sphingolipid synthesis.
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Determined in vitro substrate specificities of all seven mammalian elongases (ELOVL1-7), including ELOVL4; elongases catalyze the first of four steps of the ER-bound VLCFA elongation cycle.
"Elongases catalyze the first of four steps in the VLCFA elongation cycle; mammals have seven elongases (ELOVL1-7). In the present study, we determined the precise substrate specificities of all the ELOVLs by in vitro analyses."
A reference map of the human binary protein interactome.
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Large-scale systematic yeast two-hybrid map (HuRI) of human binary protein-protein interactions; the source of many ELOVL4 GO:0005515 IPI annotations.
"Here we present a human 'all-by-all' reference interactome map of human binary protein interactions, or 'HuRI'."
The 3-hydroxyacyl-CoA dehydratase 1/2 form complex with trans-2-enoyl-CoA reductase involved in substrates transfer in very long chain fatty acid elongation.
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Describes the ER-membrane VLCFA elongation machinery as a four-component system (ELOVL, KAR, HACD, TECR) and the physical HACD-TECR complex, providing context for the experimentally observed ELOVL4-TECR interaction.
"the VLCFAs elongation machinery is located in ER membrane and consists of four components, FA elongase (ELOVL), 3-ketoacyl-CoA reductase (KAR), 3-hydroxyacyl-CoA dehydratase (HACD), and trans-2-enoyl-CoA reductase (TECR)"
UniProt entry Q9GZR5 (ELOV4_HUMAN)
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ELOVL4 catalyzes the first and rate-limiting reaction of the four-reaction long/very-long-chain fatty acid elongation cycle in the ER, adding two carbons per cycle and producing very-long-chain saturated and polyunsaturated fatty acids.
"Catalyzes the first and rate-limiting reaction of the four"
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ELOVL4 is an endoplasmic reticulum membrane multi-pass membrane protein.
"Endoplasmic reticulum membrane"