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UniProtKB/Swiss-Prot P37088: Variant p.Gly327Cys

Amiloride-sensitive sodium channel subunit alpha
Gene: SCNN1A
Variant information

Variant position:  327
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  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:  From Glycine (G) to Cysteine (C) at position 327 (G327C, p.Gly327Cys).
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 glycine (G) to medium size and polar (C)
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:  In PHA1B; results in a significant reduction of channel function as compared to wild-type; significantly lowers both Li+ and Na+ ion currents.
Any additional useful information about the variant.

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



Sequence information

Variant position:  327
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  669
The length of the canonical sequence.

Location on the sequence:   TFNDKNNSNLWMSSMPGINN  G LSLMLRAEQNDFIPLLSTVT
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                         TFNDK--NNSNLWMSSMPGINNGLSLMLRAEQNDFIPLLSTVT

Chimpanzee                    TFNDK--NNSNLWMSSMPGINNGLSLMLRAEQNDFIPLLST

Mouse                         TFNNK--NNSNLWMSSMPGVNNGLSLTLRTEQNDFIPLLST

Rat                           TFNDK--NNSNLWMSSMPGVNNGLSLTLRTEQNDFIPLLST

Bovine                        TFNDK--NSSNLWMSSMPGVNNGLSLTLRTEQNDFIPLLST

Rabbit                        TFNDK--NNSSLWMSSMPGINNGLSLTLRTEQNDFIPLLST

Chicken                       TFND---NSSSLWTSSLPGINNGLSLVVRTEQNDFIPLLST

Xenopus laevis                TFNQNQSDQSNLWSSSMPGIKNGLTLVLRTEQHDYIPLLSS

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.

TypePositionsDescription
Chain 1 – 669 Amiloride-sensitive sodium channel subunit alpha
Topological domain 107 – 562 Extracellular
Alternative sequence 246 – 669 Missing. In isoform 3.
Alternative sequence 327 – 345 Missing. In isoform 4.
Beta strand 327 – 332


Literature citations

Renin-aldosterone response, urinary Na/K ratio and growth in pseudohypoaldosteronism patients with mutations in epithelial sodium channel (ENaC) subunit genes.
Hanukoglu A.; Edelheit O.; Shriki Y.; Gizewska M.; Dascal N.; Hanukoglu I.;
J. Steroid Biochem. Mol. Biol. 111:268-274(2008)
Cited for: GENOTYPE-PHENOTYPE RELATIONSHIPS IN PHA1B; LONG-TERM EFFECTS OF MUTATIONS ON PHA1B; VARIANT PHA1B CYS-327; CHARACTERIZATION OF VARIANT PHA1B CYS-327;

Novel mutations in epithelial sodium channel (ENaC) subunit genes and phenotypic expression of multisystem pseudohypoaldosteronism.
Edelheit O.; Hanukoglu I.; Gizewska M.; Kandemir N.; Tenenbaum-Rakover Y.; Yurdakoek M.; Zajaczek S.; Hanukoglu A.;
Clin. Endocrinol. (Oxf.) 62:547-553(2005)
Cited for: VARIANT PHA1B CYS-327;

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.