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:
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 ERVLRDLRIFRIFEGTNDIL RLFVALQGCMDKGKELSGLGS
Mouse ERVLRDIRIFRIFEGANDIL RLFVALQGCMDKGKELTGLGN
Rat ERVLRDIRIFRIFEGTNDIL RLFVALQGCMDKGKELTGLGN
Bovine ERVLRDLRIFRIFEGTNDIL RLFVALQGCMDKGKELSGLGN
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
41 – 655 Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
41 – 482 Catalytic
462 – 462 Proton acceptor
482 – 482 N6-acetyllysine; alternate
482 – 482 N6-succinyllysine; alternate
458 – 458 F -> T. Decreased acyl-CoA dehydrogenase activity. Decreased affinity for acyl-CoA. No effect on FAD cofactor-binding.
458 – 458 F -> V. Loss of acyl-CoA dehydrogenase activity. Loss of FAD cofactor-binding.
458 – 458 F -> Y. Decreased acyl-CoA dehydrogenase activity. No effect on affinity for acyl-CoA. Decreased FAD cofactor-binding.
462 – 462 E -> D. Decreased acyl-CoA dehydrogenase activity. No effect on affinity for acyl-CoA. No effect on FAD cofactor-binding.
462 – 462 E -> Q. Loss of acyl-CoA dehydrogenase activity. No effect on FAD cofactor-binding.
465 – 485
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;
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.