Variant position: 112 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 931 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 STSLSIEEERFLDAAEYGNI PVVRKMLEECHSLNVNCVDYM
Mouse STSLSIEEERFLDAAEYGNI PVVRKMLEECHSLNVNCVDYM
Bovine STSLSIEEERFLDAAEYGNI PVVRKMLEECLSLNVNCVDYM
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 – 931 Short transient receptor potential channel 6
1 – 438 Cytoplasmic
97 – 126 ANK 1
110 – 110 N -> H. Increases calcium ion transport.
125 – 125 N -> A. No effect on RNF24-binding; when associated with A-127; A-128 and A-130.
127 – 127 N -> A. No effect on RNF24-binding; when associated with A-125; A-128 and A-130.
128 – 128 C -> A. No effect on RNF24-binding; when associated with A-125; A-127 and A-130.
130 – 130 D -> A. No effect on RNF24-binding; when associated with A-125; A-127 and A-128.
132 – 132 M -> T. Increases cation channel activity. Increases significantly inward and outward currents and does not show channel inactivation. Increases calcium ion transport.
111 – 119
A mutation in the TRPC6 cation channel causes familial focal segmental glomerulosclerosis.
Winn M.P.; Conlon P.J.; Lynn K.L.; Farrington M.K.; Creazzo T.; Hawkins A.F.; Daskalakis N.; Kwan S.Y.; Ebersviller S.; Burchette J.L.; Pericak-Vance M.A.; Howell D.N.; Vance J.M.; Rosenberg P.B.;
Cited for: VARIANT FSGS2 GLN-112;
TRPC6 G757D Loss-of-Function Mutation Associates with FSGS.
Riehle M.; Buescher A.K.; Gohlke B.O.; Kassmann M.; Kolatsi-Joannou M.; Braesen J.H.; Nagel M.; Becker J.U.; Winyard P.; Hoyer P.F.; Preissner R.; Krautwurst D.; Gollasch M.; Weber S.; Harteneck C.;
J. Am. Soc. Nephrol. 27:2771-2783(2016)
Cited for: MUTAGENESIS OF ASN-110; MET-132; 755-GLU--GLY-757; 755-GLU-GLU-756; 826-LYS-LYS-827 AND GLN-889; VARIANTS FSGS2 SER-109; GLN-112; SER-125; SER-143; GLN-175; LEU-218; ALA-395; ASP-757; PRO-780; CYS-895; LEU-895 AND LYS-897; CHARACTERIZATION OF VARIANTS FSGS2 SER-109; GLN-112; SER-125; SER-143; GLN-175; LEU-218; ALA-395; ASP-757; PRO-780; CYS-895; LEU-895 AND LYS-897; VARIANT VAL-404; CHARACTERIZATION OF VARIANT VAL-404; FUNCTION; SUBCELLULAR LOCATION; SUBUNIT;
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.