Sequence information
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:
NCIIFLGPVKGSVFFRNCRD
C KCTLACQQFRVRDCRKLEVF
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 NCIIFLGPVKGSVFFRNCRDC KCTLACQQFRVRDCRKLEVF
Mouse NCVIFLGPVKGSVFFRNCRDC KCTLACQQFRVRDCRKLEVF
Chicken NCQIFLGPIKGSVFFRNCKDC KCIVACQQFRTRDCRRLEVF
Xenopus laevis NCRIFLGPVKGSVFFRDCKDC KCVVACQQFRTRDCRRMDVF
Zebrafish NCRIVLGPVKGSVFFRDCKDI KCVVACQQFRTRDCKKMDVF
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
2 – 350
Protein XRP2
Domain
24 – 179
C-CAP/cofactor C-like
Mutagenesis
101 – 101
F -> A. Reduces affinity for mouse ARL3.
Mutagenesis
115 – 115
Q -> A. Reduces affinity for mouse ARL3.
Mutagenesis
116 – 116
Q -> A. Reduces affinity and GTP-hydrolysis rate for mouse ARL3.
Mutagenesis
118 – 118
R -> A. Reduces affinity and GTP-hydrolysis rate for mouse ARL3.
Mutagenesis
120 – 120
R -> H. Reduces affinity for mouse ARL3; when associated with S-121.
Mutagenesis
121 – 121
D -> S. Reduces affinity for mouse ARL3; when associated with H-120.
Beta strand
106 – 121
Literature citations
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;
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.