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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P55017: Variant p.Val153Met

Solute carrier family 12 member 3
Gene: SLC12A3
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Variant information Variant position: help 153 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 Valine (V) to Methionine (M) at position 153 (V153M, p.Val153Met). 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 Similar physico-chemical property. Both residues are medium size and hydrophobic. 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 GTLMNS. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 153 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 1021 The length of the canonical sequence.
Location on the sequence: help PVRFGWVKGVMIRCMLNIWG V ILYLRLPWITAQAGIVLTWI 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                         PVRFGWVKGVMIRCMLNIWGVILYLRLPWITAQAGIVLTWI

Mouse                         PVRFGWVKGVMIRCMLNIWGVILYLRLPWITAQAGIVLTWL

Rat                           PVRFGWVKGVMIRCMLNIWGVILYLRLPWITAQAGIVLTWL
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 – 1021 Solute carrier family 12 member 3
Transmembrane 138 – 166 Discontinuously helical
Topological domain 167 – 167 Extracellular
Binding site 148 – 148
Binding site 149 – 149
Binding site 151 – 151
Mutagenesis 149 – 149 N -> A. Reduced sensitivity to thiazide diuretics. Reduced sodium and chloride ion cotransporter activity.
Mutagenesis 158 – 158 R -> A. Strongly reduced sodium and chloride ion cotransporter activity.



Literature citations
Novel mutations in the SLC12A3 gene causing Gitelman's syndrome in Swedes.
Fava C.; Montagnana M.; Rosberg L.; Burri P.; Joensson A.; Wanby P.; Wahrenberg H.; Hulthen U.L.; Aurell M.; Guidi G.C.; Melander O.;
DNA Seq. 18:395-399(2007)
Cited for: VARIANTS GTLMNS LYS-68; ASN-69; HIS-145; MET-153; ASP-230; ALA-342; LEU-677 AND SER-867; Novel NCC mutants and functional analysis in a new cohort of patients with Gitelman syndrome.
Glaudemans B.; Yntema H.G.; San-Cristobal P.; Schoots J.; Pfundt R.; Kamsteeg E.J.; Bindels R.J.; Knoers N.V.; Hoenderop J.G.; Hoefsloot L.H.;
Eur. J. Hum. Genet. 20:263-270(2012)
Cited for: VARIANTS GTLMNS MET-60; HIS-62; GLN-83; TRP-83; ASP-121; CYS-135; CYS-145; MET-150; MET-153; PRO-157; LEU-158; MET-163; VAL-166; ARG-172; LEU-178; THR-192; ILE-194; GLN-209; ARG-235; ASN-259; PRO-272; MET-304; PRO-304; VAL-313; TRP-321; TRP-334; GLU-374; MET-382; ILE-392; CYS-399; 433-GLN--CYS-436 DELINS LEU; SER-439; SER-442; ARG-463; THR-464; CYS-475; HIS-489; CYS-507; THR-523; SER-534; LEU-536; GLY-546; LEU-555; ARG-560; ASN-566 DEL; LEU-615; CYS-642; CYS-642; GLY-642; HIS-642; LEU-643; MET-647; HIS-655; LYS-ALA-PHE-TYR-SER-ASP-VAL-ILE-713 INS; VAL-729; ARG-735; ARG-741; LEU-751; THR-824; ASN-839; PHE-849; PRO-850; CYS-852; CYS-862; THR-872; GLN-887; TRP-934; TRP-935; GLN-955; GLY-958; ARG-980; TYR-985; GLN-1009 AND ARG-1021; CHARACTERIZATION OF VARIANT GTLMNS ASP-121; ILE-392; SER-442; CYS-475; HIS-489; LEU-751 AND ARG-1021; FUNCTION; SUBCELLULAR LOCATION;
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.