Sequence information
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:
LFVALQGCMDKGKELSGLGS
A LKNPFGNAGLLLGEAGKQLR
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 LFVALQGCMDKGKELSGLGSA LKNPFGNAGLLLGEAGKQLR
Mouse LFVALQGCMDKGKELTGLGNA LKNPFGNVGLLMGEAGKQLR
Rat LFVALQGCMDKGKELTGLGNA LKNPLGNVGLLIGEASKQLR
Bovine LFVALQGCMDKGKELSGLGNA LKNPFGNAGLLLGEAGKQLR
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
483 – 516
Membrane-anchoring
Modified residue
482 – 482
N6-acetyllysine; alternate
Modified residue
482 – 482
N6-succinyllysine; alternate
Mutagenesis
490 – 490
A -> GVSDH. Changed substrate specificity with decreased affinity for tetradecanoyl-CoA and hexadecanoyl-CoA.
Literature citations
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.;
Circulation 99:1337-1343(1999)
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;
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.