Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P49748: Variant p.Ala490Pro

Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
Gene: ACADVL
Feedback?
Variant information Variant position: help 490 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance
Residue change: help From Alanine (A) to Proline (P) at position 490 (A490P, p.Ala490Pro). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties: help Change from small size and hydrophobic (A) to medium size and hydrophobic (P) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -1 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page
Variant description: help In ACADVLD; decreased association with mitochondrial inner membrane; may affect substrate specificity, possibly reducing the affinity for long-chain acyl-CoA substrates. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 490 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 655 The length of the canonical sequence.
Location on the sequence: help 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         LFVALQGCMDKGKELSGLGSALKNPFGNAGLLLGEAGKQLR

Mouse                         LFVALQGCMDKGKELTGLGNALKNPFGNVGLLMGEAGKQLR

Rat                           LFVALQGCMDKGKELTGLGNALKNPLGNVGLLIGEASKQLR

Bovine                        LFVALQGCMDKGKELSGLGNALKNPFGNAGLLLGEAGKQLR
Sequence annotation in neighborhood: help 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.
TypePositionsDescription
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 VARIANTS ACADVLD PRO-490 AND PRO-502; HOMODIMERIZATION; 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.