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UniProtKB/Swiss-Prot O75762: Variant p.Asn855Ser

Transient receptor potential cation channel subfamily A member 1
Gene: TRPA1
Variant information

Variant position:  855
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 Asparagine (N) to Serine (S) at position 855 (N855S, p.Asn855Ser).
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 medium size and polar (N) to small size and polar (S)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  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:  In FEPS1; 5-fold increase in inward current when stimulated by the agonist cinnamaldehyde compared to wild-type at normal neuronal resting potential; consistent with a gain of function mutation.
Any additional useful information about the variant.

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



Sequence information

Variant position:  855
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  1119
The length of the canonical sequence.

Location on the sequence:   GAIAVYFYWMNFLLYLQRFE  N CGIFIVMLEVILKTLLRSTV
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                         GAIAVYFYWMNFLLYLQRFENCGIFIVMLEVILKTLLRSTV

Mouse                         GAIAIFFYWMNFLLYLQRFENCGIFIVMLEVIFKTLLRSTG

Rat                           GAIAIFFYWMNFLLYLQRFENCGIFIVMLEVIFKTLLRSTG

Caenorhabditis elegans        AALCIFFGWINLLFMIRKMPRFGIFVVMFVDIVKTFFRFFP

Drosophila                    ASIAVFLSWFRLLLFLQRFDQVGIYVVMFLEILQTLIKVLM

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 – 1119 Transient receptor potential cation channel subfamily A member 1
Topological domain 851 – 873 Cytoplasmic
Modified residue 856 – 856 Cysteine sulfenic acid (-SOH); transient; in hyperoxia
Disulfide bond 633 – 856 Alternate; transient; in hyperoxia; unknown whether inter- or intrachain
Mutagenesis 856 – 856 C -> S. Decrease in activation by hyperoxia and diallyl disulfide. Important decrease in activation by hyperoxia and diallyl disulfide; when associated with S-633.
Beta strand 851 – 856


Literature citations

A gain-of-function mutation in TRPA1 causes familial episodic pain syndrome.
Kremeyer B.; Lopera F.; Cox J.J.; Momin A.; Rugiero F.; Marsh S.; Woods C.G.; Jones N.G.; Paterson K.J.; Fricker F.R.; Villegas A.; Acosta N.; Pineda-Trujillo N.G.; Ramirez J.D.; Zea J.; Burley M.W.; Bedoya G.; Bennett D.L.; Wood J.N.; Ruiz-Linares A.;
Neuron 66:671-680(2010)
Cited for: VARIANT FEPS1 SER-855; CHARACTERIZATION OF VARIANT FEPS1 SER-855; FUNCTION; SUBCELLULAR LOCATION; ACTIVITY REGULATION;

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.