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:
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 GAIAVYFYWMNFLLYLQRFE NCGIFIVMLEVILKTLLRSTV
Mouse GAIAIFFYWMNFLLYLQRFE NCGIFIVMLEVIFKTLLRSTG
Rat GAIAIFFYWMNFLLYLQRFE NCGIFIVMLEVIFKTLLRSTG
Caenorhabditis elegans AALCIFFGWINLLFMIRKMP RFGIFVVMFVDIVKTFFRFFP
Drosophila ASIAVFLSWFRLLLFLQRFD QVGIYVVMFLEILQTLIKVLM
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.
Type Positions Description
1 – 1119 Transient receptor potential cation channel subfamily A member 1
851 – 873 Cytoplasmic
856 – 856 Cysteine sulfenic acid (-SOH); transient; in hyperoxia
633 – 856 Alternate; transient; in hyperoxia; unknown whether inter- or intrachain
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.
851 – 856
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.;
Cited for: VARIANT FEPS1 SER-855; CHARACTERIZATION OF VARIANT FEPS1 SER-855; FUNCTION; SUBCELLULAR LOCATION; ACTIVITY REGULATION;
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.