Variant position: 108 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 350 The length of the canonical sequence.
Location on the sequence:
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 NCIIFLGPVKGSVFFRNCRD CKCTLACQQFRVRDCRKLEVF
Mouse NCVIFLGPVKGSVFFRNCRD CKCTLACQQFRVRDCRKLEVF
Chicken NCQIFLGPIKGSVFFRNCKD CKCIVACQQFRTRDCRRLEVF
Xenopus laevis NCRIFLGPVKGSVFFRDCKD CKCVVACQQFRTRDCRRMDVF
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
2 – 350 Protein XRP2
24 – 179 C-CAP/cofactor C-like
101 – 101 F -> A. Reduces affinity for mouse ARL3.
115 – 115 Q -> A. Reduces affinity for mouse ARL3.
116 – 116 Q -> A. Reduces affinity and GTP-hydrolysis rate for mouse ARL3.
118 – 118 R -> A. Reduces affinity and GTP-hydrolysis rate for mouse ARL3.
120 – 120 R -> H. Reduces affinity for mouse ARL3; when associated with S-121.
121 – 121 D -> S. Reduces affinity for mouse ARL3; when associated with H-120.
106 – 121
Next-generation genetic testing for retinitis pigmentosa.
Neveling K.; Collin R.W.; Gilissen C.; van Huet R.A.; Visser L.; Kwint M.P.; Gijsen S.J.; Zonneveld M.N.; Wieskamp N.; de Ligt J.; Siemiatkowska A.M.; Hoefsloot L.H.; Buckley M.F.; Kellner U.; Branham K.E.; den Hollander A.I.; Hoischen A.; Hoyng C.; Klevering B.J.; van den Born L.I.; Veltman J.A.; Cremers F.P.; Scheffer H.;
Hum. Mutat. 33:963-972(2012)
Cited for: VARIANT RP2 TYR-108;
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.