Variant position: 299 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 457 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 ARVGLGITTVLTMTTQSSGS RASLPKVSYVKAIDIWMAVCL
Mouse ARVGLGITTVLTMTTQSSGS RASLPKVSYVKAIDIWMAVCL
Rat ARVGLGITTVLTMTTQSSGS RASLPKVSYVKAIDIWMAVCL
Bovine ARVGLGITTVLTMTTQSSGS RASLPKVSYVKAIDIWMAVCL
Zebrafish ARVGLGITTVLTMTTQSSGS RASLPKVSYVKAIDIWMAVCL
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
29 – 457 Glycine receptor subunit alpha-1
299 – 309 Extracellular
289 – 289 Important for obstruction of the ion pore in the closed conformation
282 – 282 G -> A. Increased single-channel conductance. No effect on glycine sensitivity, but decreased rate of activation.
304 – 304 K -> C. Decreases channel conductance; the mutant channel requires much higher glycine concentrations for activation.
299 – 301
Mutations in the alpha 1 subunit of the inhibitory glycine receptor cause the dominant neurologic disorder, hyperekplexia.
Shiang R.; Ryan S.G.; Zhu Y.-Z.; Hahn A.F.; O'Connell P.; Wasmuth J.J.;
Nat. Genet. 5:351-357(1993)
Cited for: VARIANTS HKPX1 LEU-299 AND GLN-299;
Decreased agonist affinity and chloride conductance of mutant glycine receptors associated with human hereditary hyperekplexia.
Langosch D.; Laube B.; Runstroem N.; Schmieden V.; Bormann J.; Betz H.;
EMBO J. 13:4223-4228(1994)
Cited for: CHARACTERIZATION OF VARIANTS HKPX1 LEU-299 AND GLN-299; FUNCTION; SUBCELLULAR LOCATION;
An additional family with Startle disease and a G1192A mutation at the alpha 1 subunit of the inhibitory glycine receptor gene.
Schorderet D.F.; Pescia G.; Bernasconi A.; Regli F.;
Hum. Mol. Genet. 3:1201-1201(1994)
Cited for: VARIANT HKPX1 LEU-299;
Identification of intracellular and extracellular domains mediating signal transduction in the inhibitory glycine receptor chloride channel.
Lynch J.W.; Rajendra S.; Pierce K.D.; Handford C.A.; Barry P.H.; Schofield P.R.;
EMBO J. 16:110-120(1997)
Cited for: CHARACTERIZATION OF VARIANTS HKPX1 ASN-272; LEU-299; GLN-299; GLU-304 AND CYS-307; FUNCTION; SUBCELLULAR LOCATION; BIOPHYSICOCHEMICAL PROPERTIES;
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.