UniProtKB/Swiss-Prot Q86SU0: Variant p.Arg453Gln

Immunoglobulin-like domain-containing receptor 1
Gene: ILDR1
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Variant information Variant position:

453 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

US 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:

From Arginine (R) to Glutamine (Q) at position 453 (R453Q, p.Arg453Gln). 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:

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:

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:

In DFNB42; uncertain significance; no effect on interaction with MARVELD2; no effect on tight junction location. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs372564314 [ dbSNP | Ensembl ]

Sequence information Variant position:

453 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

546 The length of the canonical sequence.
Location on the sequence:

RPSHPPFRSRCQERPRRPSP R ESTQRHGRRRRHRSYSPPLP 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                         RPSHPPFRSRCQERPRRPS-----PRESTQRHGRRRRH-RSYSPPLP

Mouse                         -------------PPRRPE-----PREGAQRR-ERRRH-RS

Xenopus laevis                RSNPHSDRARPTERRRSPERGDQGRRGSPDRYSRSQRHRRS

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
Chain	24 – 546	Immunoglobulin-like domain-containing receptor 1
Topological domain	189 – 546	Cytoplasmic
Region	399 – 546	Disordered
Compositional bias	435 – 454	Basic and acidic residues
Alternative sequence	266 – 546	Missing. In isoform 3.
Alternative sequence	330 – 546	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.