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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P31641: Variant p.Ala78Glu

Sodium- and chloride-dependent taurine transporter
Gene: SLC6A6
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Variant information Variant position: help 78 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 Glutamate (E) at position 78 (A78E, p.Ala78Glu). 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 acidic (E) 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 HTRDC; severely decreased taurine transport activity in patient cells; does not affect cell membrane localization; reduces taurine transport in vitro. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 78 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 620 The length of the canonical sequence.
Location on the sequence: help FVGLGNVWRFPYLCYKNGGG A FLIPYFIFLFGSGLPVFFLE 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                         FVGLGNVWRFPYLCYKNGGGAFLIPYFIFLFGSGLPVFFLE

                              FVGLGNVWRFPYLCYKNGGGAFLIPYFIFLFGGGLPVFFLE

Mouse                         FVGLGNVWRFPYLCYKNGGGAFLIPYFIFLFGSGLPVFFLE

Rat                           FVGLGNVWRFPYLCYKNGGGAFLIPYFIFLFGSGLPVFFLE

Bovine                        FVGLGNVWRFPYLCYKNGGGAFLIPYFIFLFGGGLPVFFLE
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 1 – 620 Sodium- and chloride-dependent taurine transporter
Topological domain 71 – 78 Extracellular
Binding site 59 – 59
Binding site 60 – 60
Binding site 62 – 62
Binding site 62 – 62
Binding site 67 – 67
Binding site 83 – 83
Mutagenesis 58 – 58 F -> A. Reduces taurine transport.
Mutagenesis 62 – 62 G -> A. Reduces taurine transport.
Mutagenesis 63 – 63 N -> A. Reduces taurine transport.



Literature citations
Biallelic mutation of human SLC6A6 encoding the taurine transporter TAUT is linked to early retinal degeneration.
Preising M.N.; Goerg B.; Friedburg C.; Qvartskhava N.; Budde B.S.; Bonus M.; Toliat M.R.; Pfleger C.; Altmueller J.; Herebian D.; Beyer M.; Zoellner H.J.; Wittsack H.J.; Schaper J.; Klee D.; Zechner U.; Nuernberg P.; Schipper J.; Schnitzler A.; Gohlke H.; Lorenz B.; Haeussinger D.; Bolz H.J.;
FASEB J. 33:11507-11527(2019)
Cited for: INVOLVEMENT IN HTRDC; FUNCTION; VARIANT HTRDC GLU-78; CHARACTERIZATION OF VARIANT HTRDC GLU-78; TRANSPORTER ACTIVITY; SUBCELLULAR LOCATION;
Structural characterization reveals substrate recognition by the taurine transporter TauT.
Xu H.; Bai Q.; Wang H.; Zhao J.; Guo A.; Li R.; Chen Q.; Wei Y.; Li N.; Huang Z.; Zhao Y.;
Cell Discov. 11:28-28(2025)
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (2.77 ANGSTROMS) IN COMPLEXES WITH TAURINE; SODIUM; CHLORIDE AND LIPIDS; FUNCTION; TRANSPORTER ACTIVITY; ACTIVITY REGULATION; SUBCELLULAR LOCATION; TOPOLOGY; DISULFIDE BONDS; CHARACTERIZATION OF VARIANTS GLU-78 AND VAL-399; MUTAGENESIS OF GLY-62; ASN-63; TYR-138; SER-301; ASN-333; SER-337 AND SER-402;
Transport and inhibition mechanism for human TauT-mediated taurine uptake.
Chao Y.; Zhou Z.; Xia H.; Yang C.; Li T.; Tang Y.Q.; Shu Y.; Ba Q.; Hong J.; Li D.; Qu Q.;
Cell Res. 35:381-384(2025)
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (2.58 ANGSTROMS) OF 1-582 IN COMPLEXES WITH TAURINE; BETA-ALANINE; SODIUM; CHLORIDE AND LIPIDS; FUNCTION; TRANSPORTER ACTIVITY; ACTIVITY REGULATION; SUBCELLULAR LOCATION; TOPOLOGY; DISULFIDE BONDS; CHARACTERIZATION OF VARIANTS GLU-78 AND VAL-399; MUTAGENESIS OF GLY-57; PHE-58; TYR-138; PHE-300; ALA-308; VAL-405 AND GLU-406;
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.