UniProtKB/Swiss-Prot P16219: Variant p.Arg171Trp

Short-chain specific acyl-CoA dehydrogenase, mitochondrial
Gene: ACADS
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Variant information Variant position:

171 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

LB/B 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 Arginine (R) to Tryptophan (W) at position 171 (R171W, p.Arg171Trp). 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 large size and basic (R) to large size and aromatic (W) 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:

69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs1800556 [ dbSNP | Ensembl ]

Sequence information Variant position:

171 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

412 The length of the canonical sequence.
Location on the sequence:

CFALSEPGNGSDAGAASTTA R AEGDSWVLNGTKAWITNAWE 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                         CFALSEPGNGSDAGAASTTARAEGDSWVLNGTKAWITNAWE

Mouse                         CFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWITNSWE

Rat                           CFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWITNSWE

Pig                           CFALSEPGNGSDAGAAATTAQADHDSWVLSGTKAWITNAWE

Bovine                        CFALSEPGNGSDAGAAATTARADGDSWVLSGTKAWITNAWE

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	25 – 412	Short-chain specific acyl-CoA dehydrogenase, mitochondrial
Binding site	161 – 161
Beta strand	169 – 173

Literature citations
Identification of four new mutations in the short-chain acyl-CoA dehydrogenase (SCAD) gene in two patients: one of the variant alleles, 511C-->T, is present at an unexpectedly high frequency in the general population, as was the case for 625G-->A, together conferring susceptibility to ethylmalonic aciduria.
Gregersen N.; Winter V.S.; Corydon M.J.; Corydon T.J.; Rinaldo P.; Ribes A.; Martinez G.; Bennett M.J.; Vianey-Saban C.; Bhala A.; Hale D.E.; Lehnert W.; Kmoch S.; Roig M.; Riudor E.; Eiberg H.; Andresen B.S.; Bross P.; Bolund L.A.; Koelvraa S.;
Hum. Mol. Genet. 7:619-627(1998)
Cited for: VARIANTS ACADSD CYS-92; ARG-177 AND CYS-383; VARIANTS TRP-171 AND SER-209; Role of common gene variations in the molecular pathogenesis of short-chain acyl-CoA dehydrogenase deficiency.
Corydon M.J.; Vockley J.; Rinaldo P.; Rhead W.J.; Kjeldsen M.; Winter V.S.; Riggs C.; Babovic-Vuksanovic D.; Smeitink J.; De Jong J.; Levy H.; Sewell A.C.; Roe C.; Matern D.; Dasouki M.; Gregersen N.;
Pediatr. Res. 49:18-23(2001)
Cited for: VARIANTS ACADSD SER-90; GLU-104 DEL; VAL-192; TRP-325; LEU-353 AND TRP-380; VARIANTS TRP-171 AND SER-209; CHARACTERIZATION OF VARIANTS ACADSD SER-90; GLU-104 DEL; VAL-192; TRP-325; LEU-353 AND TRP-380; CHARACTERIZATION OF VARIANTS TRP-171 AND SER-209; FUNCTION; CATALYTIC ACTIVITY; PATHWAY;

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.