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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P13866: Variant p.Ala304Val

Sodium/glucose cotransporter 1
Gene: SLC5A1
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Variant information Variant position: help 304 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 Valine (V) at position 304 (A304V, p.Ala304Val). 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 hydrophobic (V) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 0 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 GGM; impairs trafficking to the plasma membrane. Any additional useful information about the variant.


Sequence information Variant position: help 304 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 664 The length of the canonical sequence.
Location on the sequence: help SILTLWYWCTDQVIVQRCLS A KNMSHVKGGCILCGYLKLMP 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                         SILTLWYWCTDQVIVQRCLSAKNMSHVKGGCILCGYLKLMP

Mouse                         AILALWYWCTDQVIVQRCLSAKNMSHVKADCTLCGYLKLLP

Rat                           SILALWYWCTDQVIVQRCLSAKNMSHVKAGCTLCGYLKLLP

Rabbit                        SILTLWYWCTDQVIVQRCLSAKNLSHVKAGCILCGYLKVMP

Sheep                         TIISLWYWCTDQVIVQRCLSAKNMSHVKAGCIMCGYMKLLP
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 – 664 Sodium/glucose cotransporter 1
Topological domain 299 – 313 Cytoplasmic
Site 300 – 300 Implicated in sodium coupling
Disulfide bond 255 – 511
Mutagenesis 287 – 287 T -> A. Acquires D-mannose, D-fructose and L-sorbose transporter activity; when associated with L-83 and C-290.
Mutagenesis 287 – 287 T -> N. Loss of D-glucose transporter activity. Has strict selectivity for D-galactose.
Mutagenesis 287 – 287 T -> SA. Has normal D-glucose and D-galactose transporter activity.
Mutagenesis 290 – 290 Y -> C. Loss of D-galactose transporter activity. Has strict selectivity for D-glucose. Acquires D-mannose, D-fructose and L-sorbose transporter activity; when associated with A-287 and L-83.
Mutagenesis 291 – 291 W -> A. Loss of D-glucose transporter activity.
Mutagenesis 292 – 292 C -> A. Has no effect on water permeability.
Mutagenesis 321 – 321 K -> Q. Acquires D-mannose and D-allose transporter activity comparable to glucose and galactose.
Beta strand 304 – 307



Literature citations
Defects in Na+/glucose cotransporter (SGLT1) trafficking and function cause glucose-galactose malabsorption.
Martin M.G.; Turk E.; Lostao M.P.; Kerner C.; Wright E.M.;
Nat. Genet. 12:216-220(1996)
Cited for: VARIANTS GGM ASN-28; GLY-28; SER-51; TRP-135; PRO-159; THR-166; 191-TYR--ALA-664 DEL; 254-LYS--ALA-664 DEL; LEU-276; TYR-292; ARG-295; SER-300; VAL-304; SER-369; 379-ARG--ALA-664 DEL; GLN-379; VAL-388; SER-405; THR-411; ARG-426; ASN-470; HIS-499 AND GLN-615; FUNCTION; TRANSPORTER ACTIVITY;
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.