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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q00604: Variant p.Arg121Gln

Norrin
Gene: NDP
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Variant information Variant position: help 121 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 121 (R121Q, p.Arg121Gln). 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 EVR2 and ND; reduced amount of protein in the extracellular matrix. Any additional useful information about the variant.


Sequence information Variant position: help 121 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 133 The length of the canonical sequence.
Location on the sequence: help SKLKALRLRCSGGMRLTATY R YILSCHCEECNS 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                         SKLKALRLRCSGGMRLTATYRYILSCHCEECNS

Mouse                         SKLKALRLRCSGGMRLTATYRYILSCHCEECSS

Bovine                        SKLKALRLRCSGGMRLTATYRYILSCHCEECSS
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 25 – 133 Norrin
Domain 39 – 132 CTCK
Disulfide bond 65 – 126
Disulfide bond 69 – 128
Disulfide bond 131 – 131 Interchain
Beta strand 115 – 133



Literature citations
Norrie disease protein (norrin) forms disulfide-linked oligomers associated with the extracellular matrix.
Perez-Vilar J.; Hill R.L.;
J. Biol. Chem. 272:33410-33415(1997)
Cited for: SUBCELLULAR LOCATION; OLIGOMERIZATION; MUTAGENESIS OF CYS-95; CHARACTERIZATION OF VARIANTS ND GLU-60 AND GLN-121; Identification of two new missense mutations (K58N and R121Q) in the Norrie disease (ND) gene in two Spanish families.
Fuentes J.J.; Volpini V.; Fernandez-Toral F.; Coto E.; Estivill X.;
Hum. Mol. Genet. 2:1953-1955(1993)
Cited for: VARIANTS ND ASN-58 AND GLN-121; Missense mutations in the NDP gene in patients with a less severe course of Norrie disease.
Meindl A.; Lorenz B.; Achatz H.; Hellebrand H.; Schmitz-Valckenberg P.; Meitinger T.;
Hum. Mol. Genet. 4:489-490(1995)
Cited for: VARIANTS ND GLN-104; TRP-121 AND GLN-121; Genotype-phenotype variations in five Spanish families with Norrie disease or X-linked FEVR.
Riveiro-Alvarez R.; Trujillo-Tiebas M.J.; Gimenez-Pardo A.; Garcia-Hoyos M.; Cantalapiedra D.; Lorda-Sanchez I.; Rodriguez de Alba M.; Ramos C.; Ayuso C.;
Mol. Vis. 11:705-712(2005)
Cited for: VARIANTS EVR2 CYS-38 AND GLN-121;
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.