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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P78363: Variant p.Leu1971Arg

Retinal-specific phospholipid-transporting ATPase ABCA4
Gene: ABCA4
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Variant information Variant position: help 1971 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 Leucine (L) to Arginine (R) at position 1971 (L1971R, p.Leu1971Arg). 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 medium size and hydrophobic (L) to large size and basic (R) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -2 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 FFM; highly reduced ATP-binding capacity; abolishes basal and retinal-stimulated ATP hydrolysis. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 1971 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 2273 The length of the canonical sequence.
Location on the sequence: help SSPAVDRLCVGVRPGECFGL L GVNGAGKTTTFKMLTGDTTV 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                         SSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTV

Mouse                         SSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTV

Bovine                        SSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTAV

Slime mold                    SKIAVYNSTLAIPTGQTFGLLGLNGCGKSTTLGMISGEISP
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 1 – 2273 Retinal-specific phospholipid-transporting ATPase ABCA4
Topological domain 1895 – 2273 Cytoplasmic
Domain 1938 – 2170 ABC transporter 2
Mutagenesis 1975 – 1975 G -> D. Inhibition of retinal-stimulated ATP hydrolysis.
Mutagenesis 1978 – 1978 K -> M. Inhibits ATPase activity; when associated with M-969. Decreases translocase activity; when associated with M-969. Does not affect protein subcellular localization in endoplasmic reticulum; when associated with M-969. Loss of ATP-dependent all-trans-retinal transport; when associated with M-1978. Loss in N-retinylidene-PE transfer activity. Inhibits ATPase activity with increasing retinal concentration. Does not affect ATP-independent N-retinylidene-PE binding. Does not affect ATP-dependent of N-retinylidene-PE release. Significantly reduces PE flippase activity. Inhibition of retinal-stimulated ATP hydrolysis.



Literature citations
Spectrum of ABCR gene mutations in autosomal recessive macular dystrophies.
Rozet J.-M.; Gerber S.; Souied E.; Perrault I.; Chatelin S.; Ghazi I.; Leowski C.; Dufier J.-L.; Munnich A.; Kaplan J.;
Eur. J. Hum. Genet. 6:291-295(1998)
Cited for: VARIANTS STGD1 TRP-18; CYS-212; HIS-636; MET-1019; VAL-1038; CYS-1108; TRP-1640; SER-1977 AND HIS-2107; VARIANTS FFM PRO-11; PRO-541; VAL-1038; GLU-1091; CYS-1508; PHE-1970 AND ARG-1971;
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.