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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q86SU0: Variant p.Arg97Gln

Immunoglobulin-like domain-containing receptor 1
Gene: ILDR1
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Variant information Variant position: help 97 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 Arginine (R) to Glutamine (Q) at position 97 (R97Q, p.Arg97Gln). 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 large size and basic (R) to medium size and polar (Q) 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 DFNB42; no effect on interaction with MARVELD2; loss of tight junction location. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 97 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 546 The length of the canonical sequence.
Location on the sequence: help SYQAALSLGQDPSNDCNDNQ R EVRIVAQRRGQNEPVLGVDY 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                         SYQAALSLGQDPSNDCNDNQREVRIVAQRRGQNEPVLGVDY

Mouse                         SYQAALSLGQDPSNDCSDNQREVRIVAQRRGQSEPVLGVDY

Xenopus laevis                AYQASLSLNQDPANDCNDNQREVRIVIQKRGQNEPVLGVDY
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 24 – 546 Immunoglobulin-like domain-containing receptor 1
Topological domain 24 – 167 Extracellular
Domain 24 – 162 Ig-like V-type
Disulfide bond 45 – 145
Alternative sequence 92 – 209 Missing. In isoform 4.



Literature citations
Loss-of-function mutations of ILDR1 cause autosomal-recessive hearing impairment DFNB42.
Borck G.; Ur Rehman A.; Lee K.; Pogoda H.M.; Kakar N.; von Ameln S.; Grillet N.; Hildebrand M.S.; Ahmed Z.M.; Nurnberg G.; Ansar M.; Basit S.; Javed Q.; Morell R.J.; Nasreen N.; Shearer A.E.; Ahmad A.; Kahrizi K.; Shaikh R.S.; Ali R.A.; Khan S.N.; Goebel I.; Meyer N.C.; Kimberling W.J.; Webster J.A.; Stephan D.A.; Schiller M.R.; Bahlo M.; Najmabadi H.; Gillespie P.G.; Nurnberg P.; Wollnik B.; Riazuddin S.; Smith R.J.; Ahmad W.; Muller U.; Hammerschmidt M.; Friedman T.B.; Riazuddin S.; Leal S.M.; Ahmad J.; Kubisch C.;
Am. J. Hum. Genet. 88:127-137(2011)
Cited for: VARIANTS DFNB42 GLN-97; 195-GLN--ILE-546 DEL; 379-GLU--ILE-546 DEL AND GLN-453; VARIANT CYS-463; Analysis of the 'angulin' proteins LSR, ILDR1 and ILDR2--tricellulin recruitment, epithelial barrier function and implication in deafness pathogenesis.
Higashi T.; Tokuda S.; Kitajiri S.; Masuda S.; Nakamura H.; Oda Y.; Furuse M.;
J. Cell Sci. 126:966-977(2013)
Cited for: CHARACTERIZATION OF VARIANTS DFNB42 GLN-97; 195-GLN--ILE-546 DEL; 379-GLU--ILE-546 DEL AND GLN-453; FUNCTION; SUBCELLULAR LOCATION; INTERACTION WITH MARVELD2 AND OCLN;
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.