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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q96P68: Variant p.Leu124Arg

2-oxoglutarate receptor 1
Gene: OXGR1
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Variant information Variant position: help 124 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 Leucine (L) to Arginine (R) at position 124 (L124R, p.Leu124Arg). 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 Change from medium size and hydrophobic (L) to large size and basic (R) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -2 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 CAON2; likely pathogenic; loss of alpha-ketoglutarate-dependent G protein-coupled receptor activity at pH 5 but not at PH 7 when expressed in a heterologous system. Any additional useful information about the variant.


Sequence information Variant position: help 124 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 337 The length of the canonical sequence.
Location on the sequence: help FMCKFIRFSFHFNLYSSILF L TCFSIFRYCVIIHPMSCFSI 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                         FMCKFIRFSFHFNLYSSILFLTCFSIFRYCVIIHPMSCFSI

Mouse                         FMCKFIRFGFHFNLYSSILFLTCFSLFRYVVIIHPMSCFSI

Rat                           FMCKFIRFGFHFNLYSSILFLTCFSLFRYIVIIHPMSCFSI
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 – 337 2-oxoglutarate receptor 1
Transmembrane 117 – 137 Helical; Name=3
Disulfide bond 106 – 183
Mutagenesis 106 – 106 C -> A. Loss of itaconate-induced intracellular calcium response.
Mutagenesis 107 – 107 K -> A. Slightly decreases itaconate- or alpha-ketoglutarate-induced intracellular calcium response.
Mutagenesis 110 – 110 R -> A. Loss of itaconate-induced receptor endocytosis and intracellular calcium response.
Mutagenesis 114 – 114 H -> A. Markedly impairs itaconate- or alpha-ketoglutarate-induced intracellular calcium response.
Mutagenesis 118 – 118 Y -> F. Markedly impairs itaconate- or alpha-ketoglutarate-induced intracellular calcium response.
Mutagenesis 121 – 121 I -> A. Markedly impairs itaconate- or alpha-ketoglutarate-induced intracellular calcium response.



Literature citations
OXGR1 is a candidate disease gene for human calcium oxalate nephrolithiasis.
Majmundar A.J.; Widmeier E.; Heneghan J.F.; Daga A.; Wu C.W.; Buerger F.; Hugo H.; Ullah I.; Amar A.; Ottlewski I.; Braun D.A.; Jobst-Schwan T.; Lawson J.A.; Zahoor M.Y.; Rodig N.M.; Tasic V.; Nelson C.P.; Khaliq S.; Schoenauer R.; Halbritter J.; Sayer J.A.; Fathy H.M.; Baum M.A.; Shril S.; Mane S.; Alper S.L.; Hildebrandt F.;
Genet. Med. 25:100351-100351(2023)
Cited for: INVOLVEMENT IN CAON2; VARIANTS CAON2 HIS-93; ARG-124; ARG-217; ARG-233 AND PHE-287; CHARACTERIZATION OF VARIANTS CAON2 HIS-93; ARG-124; ARG-217 AND ARG-233; FUNCTION;
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.