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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P35523: Variant p.Pro480Leu

Chloride channel protein 1
Gene: CLCN1
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Variant information Variant position: help 480 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 Proline (P) to Leucine (L) at position 480 (P480L, p.Pro480Leu). 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 -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: help In MCAD; loss of chloride transport; changed chloride channel activity; changed gating of the channel; dominant effect. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 480 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 988 The length of the canonical sequence.
Location on the sequence: help IFLFFVMKFWMSIVATTMPI P CGGFMPVFVLGAAFGRLVGE 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                         IFLFFVMKFWMSIVATTMPIPCGGFMPVFVLGAAFGRLVGE

                              IFLFFIMKFWMSIVATTMPIPCGGFMPVFVLGAAFGRLVGE

Mouse                         ILLFFVMKFWMSIVATTMPIPCGGFMPVFVLGAAFGRLVGE

Rat                           ILLFFVMKFWMSIVATTMPIPCGGFMPVFVLGAAFGRLVGE

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 – 988 Chloride channel protein 1
Transmembrane 479 – 498 Helical
Binding site 484 – 484
Mutagenesis 496 – 496 R -> K. Changed gating of the channel.
Mutagenesis 499 – 499 G -> KE. Changed gating of the channel.
Mutagenesis 499 – 499 G -> Q. No effect on gating of the channel.
Mutagenesis 500 – 500 E -> Q. No effect on channel function.
Beta strand 477 – 480



Literature citations
Multimeric structure of ClC-1 chloride channel revealed by mutations in dominant myotonia congenita (Thomsen).
Steinmeyer K.; Lorenz C.; Pusch M.; Koch M.C.; Jentsch T.J.;
EMBO J. 13:737-743(1994)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]; VARIANT MCAD LEU-480; VARIANT GLN-300; CHARACTERIZATION OF VARIANTS MCAD GLU-230 AND LEU-480; CHARACTERIZATION OF VARIANT GLN-300; FUNCTION; SUBCELLULAR LOCATION; SUBUNIT; Mutations in dominant human myotonia congenita drastically alter the voltage dependence of the CIC-1 chloride channel.
Pusch M.; Steinmeyer K.; Koch M.C.; Jentsch T.J.;
Neuron 15:1455-1463(1995)
Cited for: VARIANT MCAD MET-290; VARIANT MCAR LYS-291; CHARACTERIZATION OF VARIANTS MCAD MET-290; GLN-317 AND LEU-480; CHARACTERIZATION OF VARIANT MCAR LYS-291; CHARACTERIZATION OF VARIANT MYOTONIA LEVIOR ARG-552; MUTAGENESIS OF ILE-290 AND GLU-291; Decrement of compound muscle action potential is related to mutation type in myotonia congenita.
Colding-Joergensen E.; DunOe M.; Schwartz M.; Vissing J.;
Muscle Nerve 27:449-455(2003)
Cited for: VARIANTS MCAD VAL-128; LYS-193; SER-307 AND LEU-480; VARIANT MCAR GLU-285; VARIANTS THR-437 AND ASN-614;
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.