Sequence information
Variant position: 469 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 655 The length of the canonical sequence.
Location on the sequence:
ERVLRDLRIFRIFEGTNDIL
R LFVALQGCMDKGKELSGLGS
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human ERVLRDLRIFRIFEGTNDILR LFVALQGCMDKGKELSGLGS
Mouse ERVLRDIRIFRIFEGANDILR LFVALQGCMDKGKELTGLGN
Rat ERVLRDIRIFRIFEGTNDILR LFVALQGCMDKGKELTGLGN
Bovine ERVLRDLRIFRIFEGTNDILR LFVALQGCMDKGKELSGLGN
Sequence annotation in neighborhood: The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:Type: the type of sequence feature. Positions: endpoints of the sequence feature. Description: contains additional information about the feature.
Type Positions Description
Chain
41 – 655
Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
Region
41 – 482
Catalytic
Active site
462 – 462
Proton acceptor
Modified residue
482 – 482
N6-acetyllysine; alternate
Modified residue
482 – 482
N6-succinyllysine; alternate
Mutagenesis
458 – 458
F -> T. Decreased acyl-CoA dehydrogenase activity. Decreased affinity for acyl-CoA. No effect on FAD cofactor-binding.
Mutagenesis
458 – 458
F -> V. Loss of acyl-CoA dehydrogenase activity. Loss of FAD cofactor-binding.
Mutagenesis
458 – 458
F -> Y. Decreased acyl-CoA dehydrogenase activity. No effect on affinity for acyl-CoA. Decreased FAD cofactor-binding.
Mutagenesis
462 – 462
E -> D. Decreased acyl-CoA dehydrogenase activity. No effect on affinity for acyl-CoA. No effect on FAD cofactor-binding.
Mutagenesis
462 – 462
E -> Q. Loss of acyl-CoA dehydrogenase activity. No effect on FAD cofactor-binding.
Helix
465 – 485
Literature citations
Clear correlation of genotype with disease phenotype in very-long-chain acyl-CoA dehydrogenase deficiency.
Andresen B.S.; Olpin S.; Poorthuis B.J.H.M.; Scholte H.R.; Vianey-Saban C.; Wanders R.; Ijlst L.; Morris A.; Pourfarzam M.; Bartlett K.; Baumgartner E.R.; de Klerk J.B.C.; Schroeder L.D.; Corydon T.J.; Lund H.; Winter V.; Bross P.; Bolund L.; Gregersen N.;
Am. J. Hum. Genet. 64:479-494(1999)
Cited for: VARIANTS ACADVLD MET-260; ALA-283; TRP-469; PRO-502 AND TRP-613;
Expression and characterization of mutations in human very long-chain acyl-CoA dehydrogenase using a prokaryotic system.
Goetzman E.S.; Wang Y.; He M.; Mohsen A.W.; Ninness B.K.; Vockley J.;
Mol. Genet. Metab. 91:138-147(2007)
Cited for: CATALYTIC ACTIVITY (ISOFORM 2); SUBCELLULAR LOCATION (ISOFORM 2); TOPOLOGY (ISOFORM 2); CHARACTERIZATION OF VARIANT ACADVLD MET-260; ALA-283; TRP-469; PRO-490; PRO-502 AND TRP-613;
Disclaimer:
Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.