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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P41180: Variant p.Thr100Ile

Extracellular calcium-sensing receptor
Gene: CASR
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Variant information Variant position: help 100 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 Threonine (T) to Isoleucine (I) at position 100 (T100I, p.Thr100Ile). 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 polar (T) to medium size and hydrophobic (I) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -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: help In NSHPT; Abolished G-protein coupled receptor activity. Any additional useful information about the variant.


Sequence information Variant position: help 100 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 1078 The length of the canonical sequence.
Location on the sequence: help EINSSPALLPNLTLGYRIFD T CNTVSKALEATLSFVAQNKI 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                         EINSSPALLPNLTLGYRIFDTCNTVSKALEATLSFVAQNKI

Mouse                         EINSSPALLPNMTLGYRIFDTCNTVSKALEATLSFVAQNKI

Rat                           EINSSPSLLPNMTLGYRIFDTCNTVSKALEATLSFVAQNKI

Pig                           EINSSPALLPNMTLGYRIFDTCNTVSKALEATLSFVAQNKI

Bovine                        EINSSPALLPNMTLGYRIFDTCNTVSKALEATLSFVAQNKI
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 20 – 1078 Extracellular calcium-sensing receptor
Topological domain 20 – 612 Extracellular
Region 22 – 188 Ligand-binding 1 (LB1)
Binding site 81 – 81
Binding site 84 – 84
Binding site 87 – 87
Binding site 88 – 88
Binding site 100 – 100
Glycosylation 90 – 90 N-linked (GlcNAc...) asparagine
Disulfide bond 60 – 101
Mutagenesis 102 – 102 N -> I. Abolishes G-protein coupled receptor activity.



Literature citations
Structural mechanism of ligand activation in human calcium-sensing receptor.
Geng Y.; Mosyak L.; Kurinov I.; Zuo H.; Sturchler E.; Cheng T.C.; Subramanyam P.; Brown A.P.; Brennan S.C.; Mun H.C.; Bush M.; Chen Y.; Nguyen T.X.; Cao B.; Chang D.D.; Quick M.; Conigrave A.D.; Colecraft H.M.; McDonald P.; Fan Q.R.;
Elife 5:0-0(2016)
Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 20-607 IN COMPLEX WITH CALCIUM; PHOSPHATE AND SULFATE ANIONS AND TRYPTOPHAN; FUNCTION; ACTIVITY REGULATION; DOMAIN; DISULFIDE BONDS; GLYCOSYLATION AT ASN-261; ASN-287; ASN-446; ASN-468; ASN-488; ASN-541 AND ASN-594; MUTAGENESIS OF ARG-69; ASN-102; THR-145; SER-147; SER-170; TYR-218; SER-417 AND TRP-458; CHARACTERIZATION OF VARIANTS NSHPT ILE-100; LEU-227 AND LYS-551; CHARACTERIZATION OF VARIANTS HHC1 HIS-66; MET-81; PRO-159; GLY-172; GLY-215; LYS-297 AND GLU-557; Genetic testing in familial isolated hyperparathyroidism: unexpected results and their implications.
Warner J.; Epstein M.; Sweet A.; Singh D.; Burgess J.; Stranks S.; Hill P.; Perry-Keene D.; Learoyd D.; Robinson B.; Birdsey P.; Mackenzie E.; Teh B.T.; Prins J.B.; Cardinal J.;
J. Med. Genet. 41:155-160(2004)
Cited for: VARIANTS NSHPT ILE-100; LYS-336 DEL; PRO-650 AND MET-689; VARIANTS SER-986; GLY-990 AND GLN-1011;
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.