UniProtKB/SwissProt variant VAR

Variant information

Variant position:

267

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 Glycine (G) to Arginine (R) at position 267 (G267R, p.Gly267Arg).

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:

Change from glycine (G) to large size and basic (R)

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

BLOSUM score:

-2

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 ACADMD.

Any additional useful information about the variant.

Other resources:

Links to websites of interest for the variant.

Variant rs121434274 [ dbSNP | Ensembl ]

Sequence information

Variant position:

267

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

Protein sequence length:

421

The length of the canonical sequence.

Location on the sequence:

TRGIVFEDVKVPKENVLIGD G AGFKVAMGAFDKTRPVVAAG

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                         TRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRPVVAAG

Chimpanzee                    TRGIVFEDVKVPRENVLIGDGAGFKVAMGAFDKTRPVVAAG

Mouse                         TRGIAFEDVRVPKENVLIGEGAGFKIAMGAFDRTRPTVAAG

Rat                           TRGITFEDVRVPKENVLIGEGAGFKIAMGAFDRTRPTVAAG

Pig                           TRGIVFEDVRVPKENVLTGEGAGFKIAMGTFDKTRPPVAAG

Bovine                        TRGIVFEDVRVPKENVLIGEGAGFKIAMGAFDKTRPPVAAA

Caenorhabditis elegans        TRVITFEDVRVPAENVLGAPGAGFKVAMEAFDMTRPGVAAG

Drosophila                    TRGITFEDVRVPKENVLIGEGAGFKIAMGTFDKTRPPVAAG

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	26 – 421	Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
Modified residue	259 – 259	N6-acetyllysine; alternate
Modified residue	259 – 259	N6-succinyllysine; alternate
Modified residue	271 – 271	N6-acetyllysine; alternate
Modified residue	271 – 271	N6-succinyllysine; alternate
Modified residue	279 – 279	N6-acetyllysine
Mutagenesis	280 – 280	T -> E. Narrower substrate specificity. Changed substrate specificity towards longer acyl chains; when associated with G-401. Loss of acyl-CoA dehydrogenase activity; when associated with T-410.
Turn	266 – 268

Literature citations

Molecular survey of a prevalent mutation, 985A-to-G transition, and identification of five infrequent mutations in the medium-chain Acyl-CoA dehydrogenase (MCAD) gene in 55 patients with MCAD deficiency.
Yokota I.; Coates P.M.; Hale D.E.; Rinaldo P.; Tanaka K.;
Am. J. Hum. Genet. 49:1280-1291(1991)
Cited for: VARIANTS ACADMD ILE-149; ARG-244; ARG-267 AND THR-375;

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P11310: Variant p.Gly267Arg