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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P04180: Variant p.Arg164His

Phosphatidylcholine-sterol acyltransferase
Gene: LCAT
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Variant information Variant position: help 164 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 Arginine (R) to Histidine (H) at position 164 (R164H, p.Arg164His). 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 large size and basic (R) to medium size and polar (H) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 0 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 LCATD; also found in a patient with intermediate phenotype between LCATD and FED; loss of activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 164 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 440 The length of the canonical sequence.
Location on the sequence: help YLHTLVQNLVNNGYVRDETV R AAPYDWRLEPGQQEEYYRKL 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                         YLHTLVQNLVNNGYVRDETVRAAPYDWRLEPGQQEEYYRKL

Mouse                         YLHTLVQNLVNNGYVRDETVRAAPYDWRLAPHQQDEYYKKL

Rat                           YLHTLVQNLVNNGYVRDETVRAAPYDWRLAPRQQDEYYQKL

Rabbit                        YMHTLVQNLVNNGYVRDETVRAAPYDWRLEPSQQEEYYGKL
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 25 – 440 Phosphatidylcholine-sterol acyltransferase
Site 173 – 173 Determinant for substrate specificity
Mutagenesis 173 – 173 E -> A. Increased activity towards PAPC. Increased PAPC/POPC activity ratio.
Mutagenesis 173 – 173 E -> D. Little change in enzyme specific activity nor in PAPC/POPC activity ratio.
Mutagenesis 173 – 173 E -> K. Decreased enzyme specific activity. Increased PAPC/POPC activity ratio.
Mutagenesis 173 – 173 E -> L. Increased activity towards PAPC. Increased PAPC/POPC activity ratio.
Mutagenesis 173 – 173 E -> Q. Decreased enzyme specific activity. Increased PAPC/POPC activity ratio.
Beta strand 163 – 165



Literature citations
A single G to A nucleotide transition in exon IV of the lecithin: cholesterol acyltransferase (LCAT) gene results in an Arg140 to His substitution and causes LCAT-deficiency.
Steyrer E.; Haubenwallner S.; Hoerl G.; Giessauf W.; Kostner G.M.; Zechner R.;
Hum. Genet. 96:105-109(1995)
Cited for: VARIANT LCATD HIS-164; CHARACTERIZATION OF VARIANT LCATD HIS-164; Compound heterozygosity (G71R/R140H) in the lecithin:cholesterol acyltransferase (LCAT) gene results in an intermediate phenotype between LCAT-deficiency and fish-eye disease.
Hoerl G.; Kroisel P.M.; Wagner E.; Tiran B.; Petek E.; Steyrer E.;
Atherosclerosis 187:101-109(2006)
Cited for: VARIANT ARG-95; VARIANT LCATD HIS-164; CHARACTERIZATION OF VARIANT ARG-95;
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.