UniProtKB/Swiss-Prot Q9NQ40: Variant p.Arg132Trp

Solute carrier family 52, riboflavin transporter, member 3
Gene: SLC52A3
Chromosomal location: 20p13
Variant information

Variant position:  132
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Disease [Disclaimer]
The variants are classified into three categories: Disease, Polymorphism and Unclassified.
  • Disease: Variants implicated in disease according to literature reports.
  • Polymorphism: Variants not reported to be implicated in disease.
  • Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:  From Arginine (R) to Tryptophan (W) at position 132 (R132W, p.Arg132Trp).
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

Involvement in disease:  Brown-Vialetto-Van Laere syndrome 1 (BVVLS1) [MIM:211530]: A rare neurologic disorder characterized by sensorineural hearing loss and a variety of cranial nerve palsies, which develop over a relatively short period of time in a previously healthy individual. Sensorineural hearing loss may precede the neurological signs. The course is invariably progressive, but the rate of decline is variable within and between families. With disease evolution, long tract signs, lower motor neuron signs, cerebellar ataxia and lower cranial nerve (III-VI) palsies develop, giving rise to a complex picture resembling amyotrophic lateral sclerosis. Diaphragmatic weakness and respiratory compromise are some of the most distressing features, leading to recurrent chest infections and respiratory failure, which are often the cause of patients' demise. {ECO:0000269|PubMed:20206331, ECO:0000269|PubMed:20920669, ECO:0000269|PubMed:21110228, ECO:0000269|PubMed:22273710, ECO:0000269|PubMed:22633641, ECO:0000269|PubMed:22718020, ECO:0000269|PubMed:22824638, ECO:0000269|PubMed:27702554}. Note=The disease is caused by mutations affecting the gene represented in this entry.
The name and a short description of the disease associated with the variant. For more information about the disease, the user can refer to OMIM, following the link provided after the disease acronym.

Variant description:  In BVVLS1; loss of localization to cell membrane; loss of riboflavin transport; does not affect protein abundance.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.

Sequence information

Variant position:  132
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  469
The length of the canonical sequence.

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.





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.

Chain 1 – 469 Solute carrier family 52, riboflavin transporter, member 3
Topological domain 119 – 137 Cytoplasmic

Literature citations

Brown-Vialetto-Van Laere syndrome, a ponto-bulbar palsy with deafness, is caused by mutations in c20orf54.
Green P.; Wiseman M.; Crow Y.J.; Houlden H.; Riphagen S.; Lin J.P.; Raymond F.L.; Childs A.M.; Sheridan E.; Edwards S.; Josifova D.J.;
Am. J. Hum. Genet. 86:485-489(2010)
Cited for: VARIANTS BVVLS1 LYS-36; TRP-132; LEU-224; ALA-413 AND LEU-457; VARIANT MET-350;

Effect of clinical mutations on functionality of the human riboflavin transporter-2 (hRFT-2).
Nabokina S.M.; Subramanian V.S.; Said H.M.;
Mol. Genet. Metab. 105:652-657(2012)

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.