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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P98196: Variant p.Gln84Glu

Phospholipid-transporting ATPase IH
Gene: ATP11A
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Variant information Variant position: help 84 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 Glutamine (Q) to Glutamate (E) at position 84 (Q84E, p.Gln84Glu). 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 polar (Q) to medium size and acidic (E) 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 HLD24; results in altered lipid distribution at the cell membrane characterized by decreased phosphatidylcholine and increased sphingomyelin concentrations in the outer leaflet; affects substrate specificity resulting in novel flippase activity toward phosphatidylcholine; does not affect flippase activity toward phosphatidylserine and phosphatidylethanolamine; does not affect location to the cell membrane. Any additional useful information about the variant.


Sequence information Variant position: help 84 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 1134 The length of the canonical sequence.
Location on the sequence: help NLFEQFRRVANFYFLIIFLV Q LIIDTPTSPVTSGLPLFFVI 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                         NLFEQFRRVANFYFLIIFLVQLIIDTPTSPVTSGLPLFFVI

Mouse                         NLFEQFRRIANFYFLIIFLVQLIIDTPTSPVTSGLPLFFVI
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 – 1134 Phospholipid-transporting ATPase IH
Topological domain 83 – 88 Extracellular
Mutagenesis 84 – 84 Q -> A. Does not affect flippase activity toward phosphatidylserine. Like the wild type, it is unable to translocate phosphatidylcholine.
Mutagenesis 84 – 84 Q -> D. Does not affect flippase activity toward phosphatidylserine. Like the wild type, it is unable to translocate phosphatidylcholine.
Mutagenesis 84 – 84 Q -> N. Does not affect flippase activity toward phosphatidylserine. Like the wild type, it is unable to translocate phosphatidylcholine.



Literature citations
A sublethal ATP11A mutation associated with neurological deterioration causes aberrant phosphatidylcholine flipping in plasma membranes.
Segawa K.; Kikuchi A.; Noji T.; Sugiura Y.; Hiraga K.; Suzuki C.; Haginoya K.; Kobayashi Y.; Matsunaga M.; Ochiai Y.; Yamada K.; Nishimura T.; Iwasawa S.; Shoji W.; Sugihara F.; Nishino K.; Kosako H.; Ikawa M.; Uchiyama Y.; Suematsu M.; Ishikita H.; Kure S.; Nagata S.;
J. Clin. Invest. 131:0-0(2021)
Cited for: VARIANT HLD24 GLU-84; CHARACTERIZATION OF VARIANT HLD24 GLU-84; INVOLVEMENT IN HLD24; FUNCTION; SUBCELLULAR LOCATION; MUTAGENESIS OF GLN-84;
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.