Sequence information
Variant position: 965 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 2273 The length of the canonical sequence.
Location on the sequence:
AVDRLNITFYENQITAFLGH
N GAGKTTTLSILTGLLPPTSG
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 AVDRLNITFYENQITAFLGHN GAGKTTTLSILTGLLPPTSG
Mouse AVDRLNITFYENQITAFLGHN GAGKTTTLSILTGLLPPTSG
Slime mold AVNDLSIDMYKNRIHSFLGPN GSGKSTTLSMLTGMIEPTSG
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
1 – 2273
Retinal-specific phospholipid-transporting ATPase ABCA4
Topological domain
857 – 1376
Cytoplasmic
Domain
929 – 1160
ABC transporter 1
Nucleotide binding
963 – 970
ATP 1
Mutagenesis
966 – 966
G -> D. Abolishes basal and retinal-stimulated ATP hydrolysis.
Mutagenesis
969 – 969
K -> M. Abolishes basal and retinal-stimulated ATP hydrolysis.
Mutagenesis
969 – 969
K -> M. Inhibits ATPase activity; when associated with M-1978. Decreases translocase activity; when associated with M-1978. Does not affect protein subcellular localization in endoplasmic reticulum; when associated with M-1978.
Literature citations
Differential phospholipid substrates and directional transport by ATP-binding cassette proteins ABCA1, ABCA7, and ABCA4 and disease-causing mutants.
Quazi F.; Molday R.S.;
J. Biol. Chem. 288:34414-34426(2013)
Cited for: CATALYTIC ACTIVITY; ACTIVITY REGULATION; FUNCTION; SUBCELLULAR LOCATION; VARIANTS STGD1 PRO-100; ILE-608; ILE-959; SER-965 AND MET-1537; CHARACTERIZATION OF VARIANTS STGD1 PRO-100; ILE-608; ILE-959; SER-965 AND MET-1537; MUTAGENESIS OF CYS-1502; ARG-2107 AND PRO-2180;
Complex inheritance of ABCR mutations in Stargardt disease: linkage disequilibrium, complex alleles, and pseudodominance.
Shroyer N.F.; Lewis R.A.; Lupski J.R.;
Hum. Genet. 106:244-248(2000)
Cited for: VARIANTS STGD1 ASP-340; GLN-572; ALA-863; SER-965; VAL-1038; ALA-1780 AND HIS-1898; VARIANT GLN-943;
Frequency of ABCA4 mutations in 278 Spanish controls: an insight into the prevalence of autosomal recessive Stargardt disease.
Riveiro-Alvarez R.; Aguirre-Lamban J.; Lopez-Martinez M.A.; Trujillo-Tiebas M.J.; Cantalapiedra D.; Vallespin E.; Avila-Fernandez A.; Ramos C.; Ayuso C.;
Br. J. Ophthalmol. 93:1359-1364(2009)
Cited for: VARIANTS STGD1 VAL-156; CYS-212; LYS-380; ARG-550; PRO-572; TRP-602; ARG-607; CYS-653; ASP-767; ILE-897; ALA-901; MET-931; SER-965; MET-1019; HIS-1108; LEU-1129; LEU-1380; ILE-1433; LEU-1486; TYR-1490; GLN-1640; TRP-1640; ARG-1748; ASP-1799; PRO-1940; GLU-1961; SER-1977; PHE-2027; ARG-2060; HIS-2107; TYR-2150 AND VAL-2241;
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.