ELO2 fatty acid elongase ELO2 [Saccharomyces cerevisiae S288C] - Gene

Summary

Official Symbol: ELO2
Official Full Name: fatty acid elongase ELO2
Primary source: SGD:S000000630
Locus tag: YCR034W
See related: AllianceGenome:SGD:S000000630; FungiDB:YCR034W; VEuPathDB:YCR034W
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Also known as: FEN1; GNS1; VBM2
Summary: Enables fatty acid elongase activity. Involved in fatty acid biosynthetic process; late endosome to vacuole transport via multivesicular body sorting pathway; and sphingolipid biosynthetic process. Located in endoplasmic reticulum. Human ortholog(s) of this gene implicated in spinocerebellar ataxia type 38. Orthologous to several human genes including ELOVL2 (ELOVL fatty acid elongase 2). [provided by Alliance of Genome Resources, Dec 2024]
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Chromosome III - NC_001135.5 Genomic Context describing neighboring genes

Go to nucleotide: Graphics FASTA GenBank

Inefficient flap processing by Fen1 could play a role in the continued expansions seen in humans with trinucleotide repeat expansion diseases.
Title: Haploinsufficiency of yeast FEN1 causes instability of expanded CAG/CTG tracts in a length-dependent manner.
Results describe a series of pair-wise interactions among FEN-1, Pol4 and Dnl4, the factors that complete the repair of DNA double-strand breaks by non-homologous end-joining.
Title: Processing and joining of DNA ends coordinated by interactions among Dnl4/Lif1, Pol4, and FEN-1.
A new model is proposed for the role of FEN-1 in inhibiting trinucleotide repeat expansion in the genome.
Title: Concerted action of exonuclease and Gap-dependent endonuclease activities of FEN-1 contributes to the resolution of triplet repeat sequences (CTG)n- and (GAA)n-derived secondary structures formed during maturation of Okazaki fragments.

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

Function	Evidence Code	Pubs
enables fatty acid elongase activity	IBA Inferred from Biological aspect of Ancestor more info
enables fatty acid elongase activity	IEA Inferred from Electronic Annotation more info
enables fatty acid elongase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables transferase activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in fatty acid biosynthetic process	IEA Inferred from Electronic Annotation more info
involved_in fatty acid elongation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in fatty acid elongation, monounsaturated fatty acid	IBA Inferred from Biological aspect of Ancestor more info
involved_in fatty acid elongation, polyunsaturated fatty acid	IBA Inferred from Biological aspect of Ancestor more info
involved_in fatty acid elongation, saturated fatty acid	IBA Inferred from Biological aspect of Ancestor more info
involved_in late endosome to vacuole transport via multivesicular body sorting pathway	IGI Inferred from Genetic Interaction more info	PubMed
involved_in lipid biosynthetic process	IEA Inferred from Electronic Annotation more info
involved_in sphingolipid biosynthetic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in sphingolipid biosynthetic process	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in very long-chain fatty acid biosynthetic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in very long-chain fatty acid biosynthetic process	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in vesicle-mediated transport	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in endoplasmic reticulum	IDA Inferred from Direct Assay more info	PubMed
located_in endoplasmic reticulum	IEA Inferred from Electronic Annotation more info
is_active_in endoplasmic reticulum membrane	IBA Inferred from Biological aspect of Ancestor more info
located_in endoplasmic reticulum membrane	IEA Inferred from Electronic Annotation more info
located_in membrane	IEA Inferred from Electronic Annotation more info

NP_009963.1

Fatty acid elongase, involved in sphingolipid biosynthesis; acts on fatty acids of up to 24 carbons in length; mutations have regulatory effects on 1,3-beta-glucan synthase, vacuolar ATPase, and the secretory pathway; ELO2 has a paralog, ELO1, that arose from the whole genome duplication; lethality of the elo2 elo3 double null mutation is functionally complemented by human ELOVL1 and weakly complemented by human ELOVL3 or ELOV7