UniProtKB/SwissProt variant VAR

Variant information

Variant position:

502

The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:

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:

From Leucine (L) to Proline (P) at position 502 (L502P, p.Leu502Pro).

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:

Similar physico-chemical property. Both residues are medium size and hydrophobic.

The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:

-3

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:

In ACADVLD; decreased association with mitochondrial inner membrane; no effect on acyl-CoA dehydrogenase activity.

Any additional useful information about the variant.

Sequence information

Variant position:

502

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:

KELSGLGSALKNPFGNAGLL L GEAGKQLRRRAGLGSGLSLS

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                         KELSGLGSALKNPFGNAGLLLGEAGKQLRRRAGLGSGLSLS

Mouse                         KELTGLGNALKNPFGNVGLLMGEAGKQLRRRTGIGSGLSLS

Rat                           KELTGLGNALKNPLGNVGLLIGEASKQLRRRTGIGSGLSLS

Bovine                        KELSGLGNALKNPFGNAGLLLGEAGKQLRRRAGLGSGLSLS

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
Modified residue	517 – 517	Phosphoserine
Modified residue	522 – 522	Phosphoserine
Mutagenesis	490 – 490	A -> GVSDH. Changed substrate specificity with decreased affinity for tetradecanoyl-CoA and hexadecanoyl-CoA.

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;

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P49748: Variant p.Leu502Pro