ETFA

Electron-transfer-flavoprotein, alpha polypeptide
PDB rendering based on 1efv.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1EFV​, 1T9G​, 2A1T​, 2A1U​
Identifiers
Symbols	ETFA ; EMA; GA2; MADD
External IDs	OMIM: 608053 MGI: 106092 HomoloGene: 100 GeneCards: ETFA Gene
Gene ontology Molecular function • fatty-acyl-CoA binding • acyl-CoA dehydrogenase activity • electron carrier activity • oxidoreductase activity • flavin adenine dinucleotide binding • oxidoreductase activity, acting on the CH-CH group of donors, with a flavin as acceptor Cellular component • mitochondrion • mitochondrial matrix • extracellular exosome Biological process • respiratory electron transport chain • fatty acid beta-oxidation using acyl-CoA dehydrogenase • cellular metabolic process • small molecule metabolic process • lipid homeostasis Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	2108	110842
Ensembl	ENSG00000140374	ENSMUSG00000032314
UniProt	P13804	Q99LC5
RefSeq (mRNA)	NM_000126	NM_145615
RefSeq (protein)	NP_000117	NP_663590
Location (UCSC)	Chr 15: 76.22 – 76.31 Mb	Chr 9: 55.45 – 55.51 Mb
PubMed search

Electron-transfer-flavoprotein, alpha polypeptide (glutaric aciduria II), also known as ETFA, is a protein which in humans is encoded by the ETFA gene.^[1]

ETFA participates in catalyzing the initial step of the mitochondrial fatty acid beta oxidation. It shuttles electrons between primary flavoprotein dehydrogenases and the membrane-bound electron transfer flavoprotein ubiquinone oxidoreductase. Defects in electron-transfer-flavoprotein have been implicated in type II glutaricaciduria in which multiple acyl CoA dehydrogenase deficiencies result in large excretion of glutaric, lactic, ethylmalonic, butyric, isobutyric, 2-methyl-butyric, and isovaleric acids.^[1]

References

1. "Entrez Gene: ETFA electron-transfer-flavoprotein, alpha polypeptide (glutaric aciduria II)".

Further reading

• Frerman FE (1988). "Acyl-CoA dehydrogenases, electron transfer flavoprotein and electron transfer flavoprotein dehydrogenase.". Biochem. Soc. Trans. 16 (3): 416–8. PMID 3053288.
• Freneaux E, Sheffield VC, Molin L; et al. (1992). "Glutaric acidemia type II. Heterogeneity in beta-oxidation flux, polypeptide synthesis, and complementary DNA mutations in the alpha subunit of electron transfer flavoprotein in eight patients.". J. Clin. Invest. 90 (5): 1679–86. doi:10.1172/JCI116040. PMC 443224. PMID 1430199.
• Indo Y, Glassberg R, Yokota I, Tanaka K (1991). "Molecular characterization of variant alpha-subunit of electron transfer flavoprotein in three patients with glutaric acidemia type II--and identification of glycine substitution for valine-157 in the sequence of the precursor, producing an unstable mature protein in a patient.". Am. J. Hum. Genet. 49 (3): 575–80. PMC 1683153. PMID 1882842.
• Finocchiaro G, Ito M, Ikeda Y, Tanaka K (1988). "Molecular cloning and nucleotide sequence of cDNAs encoding the alpha-subunit of human electron transfer flavoprotein.". J. Biol. Chem. 263 (30): 15773–80. PMID 3170610.
• White RA, Dowler LL, Angeloni SV, Koeller DM (1996). "Assignment of Etfdh, Etfb, and Etfa to chromosomes 3, 7, and 13: the mouse homologs of genes responsible for glutaric acidemia type II in human.". Genomics 33 (1): 131–4. doi:10.1006/geno.1996.0170. PMID 8617498.
• Roberts DL, Frerman FE, Kim JJ (1997). "Three-dimensional structure of human electron transfer flavoprotein to 2.1-A resolution.". Proc. Natl. Acad. Sci. U.S.A. 93 (25): 14355–60. doi:10.1073/pnas.93.25.14355. PMC 26136. PMID 8962055.
• Bross P, Pedersen P, Winter V; et al. (1999). "A polymorphic variant in the human electron transfer flavoprotein alpha-chain (alpha-T171) displays decreased thermal stability and is overrepresented in very-long-chain acyl-CoA dehydrogenase-deficient patients with mild childhood presentation.". Mol. Genet. Metab. 67 (2): 138–47. doi:10.1006/mgme.1999.2856. PMID 10356313.
• Jones M, Talfournier F, Bobrov A; et al. (2002). "Electron transfer and conformational change in complexes of trimethylamine dehydrogenase and electron transferring flavoprotein.". J. Biol. Chem. 277 (10): 8457–65. doi:10.1074/jbc.M111105200. PMID 11756429.
• Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Olsen RK, Andresen BS, Christensen E; et al. (2003). "Clear relationship between ETF/ETFDH genotype and phenotype in patients with multiple acyl-CoA dehydrogenation deficiency.". Hum. Mutat. 22 (1): 12–23. doi:10.1002/humu.10226. PMID 12815589.
• Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Kimura K, Wakamatsu A, Suzuki Y; et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
• Schiff M, Froissart R, Olsen RK; et al. (2006). "Electron transfer flavoprotein deficiency: functional and molecular aspects.". Mol. Genet. Metab. 88 (2): 153–8. doi:10.1016/j.ymgme.2006.01.009. PMID 16510302.
• Olsen JV, Blagoev B, Gnad F; et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.". Cell 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
• Chiong MA, Sim KG, Carpenter K; et al. (2007). "Transient multiple acyl-CoA dehydrogenation deficiency in a newborn female caused by maternal riboflavin deficiency.". Mol. Genet. Metab. 92 (1–2): 109–14. doi:10.1016/j.ymgme.2007.06.017. PMID 17689999.