Variant position: 490 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 LFVALQGCMDKGKELSGLGS ALKNPFGNAGLLLGEAGKQLR
Mouse LFVALQGCMDKGKELTGLGN ALKNPFGNVGLLMGEAGKQLR
Rat LFVALQGCMDKGKELTGLGN ALKNPLGNVGLLIGEASKQLR
Bovine LFVALQGCMDKGKELSGLGN ALKNPFGNAGLLLGEAGKQLR
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
483 – 516 Membrane-anchoring
482 – 482 N6-acetyllysine; alternate
482 – 482 N6-succinyllysine; alternate
490 – 490 A -> GVSDH. Changed substrate specificity with decreased affinity for tetradecanoyl-CoA and hexadecanoyl-CoA.
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;
Relationship between structure and substrate-chain-length specificity of mitochondrial very-long-chain acyl-coenzyme A dehydrogenase.
Souri M.; Aoyama T.; Yamaguchi S.; Hashimoto T.;
Eur. J. Biochem. 257:592-598(1998)
Cited for: VARIANT ACADVLD PRO-490; CHARACTERIZATION OF VARIANT ACADVLD PRO-490; FUNCTION; CATALYTIC ACTIVITY; PATHWAY; SUBSTRATE SPECIFICITY; MUTAGENESIS OF ALA-490;
Molecular heterogeneity in very-long-chain acyl-CoA dehydrogenase deficiency causing pediatric cardiomyopathy and sudden death.
Mathur A.; Sims H.F.; Gopalakrishnan D.; Gibson B.; Rinaldo P.; Vockley J.; Hug G.; Strauss A.W.;
Cited for: VARIANTS ACADVLD GLU-130 DEL; PRO-213; GLU-247; MET-260; LYS-278 DEL; ALA-283; ASP-441; LEU-458; PRO-490; LYS-534; TRP-613 AND GLN-615;
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