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UniProtKB/Swiss-Prot P02647: Variant p.Arg173Ser

Apolipoprotein A-I
Gene: APOA1
Variant information

Variant position:  173
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  US
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:  From Arginine (R) to Serine (S) at position 173 (R173S, p.Arg173Ser).
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:  Change from large size and basic (R) to small size and polar (S)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -1
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:  In Boston; no evidence of association with premature coronary heart disease; associated with decreased levels of HDL cholesterol; associated with decreased serum cellular cholesterol efflux; associated with decreased lecithin-cholesterol acyltransferase (LCAT) activity.
Any additional useful information about the variant.



Sequence information

Variant position:  173
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  267
The length of the canonical sequence.

Location on the sequence:   GARQKLHELQEKLSPLGEEM  R DRARAHVDALRTHLAPYSDE
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                         GARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDE

Gorilla                       GARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDE

                              GARQKLQELQEKLSPLAEELRDRARTHVDALRAQLAPYSDD

Rhesus macaque                GTRQKLHELHEKLSPLGEEVRDRARAHVDALRTHLAPYSDE

Chimpanzee                    GARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDE

Mouse                         SARQKLQELQGRLSPVAEEFRDRMRTHVDSLRTQLAPHSEQ

Rat                           ---KNAKEMQRHLKVVAEEFRDRMRVNADALRAKFGLYSDQ

Pig                           GARQKVQELQEKLSPLAEELRDRLRAHVEALRQHVAPYSDD

Bovine                        GARQKVQELQDKLSPLAQELRDRARAHVETLRQQLAPYSDD

Rabbit                        SARQKLTELQEKLSPLAEELRDSARTHVDTLRTKLAPYSNE

Chicken                       LTKQKVELMQAKLTPVAEEARDRLRGHVEELRKNLAPYSDE

Zebrafish                     LNRQNAEQLRAKLEPLMDDIRKAFESNIEETKSKVVPMVEA

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.

TypePositionsDescription
Chain 19 – 267 Proapolipoprotein A-I
Chain 25 – 267 Apolipoprotein A-I
Chain 25 – 266 Truncated apolipoprotein A-I
Repeat 167 – 188 6
Region 68 – 267 10 X approximate tandem repeats
Helix 166 – 203


Literature citations

Case report: A novel apolipoprotein A-I missense mutation apoA-I (Arg149Ser)Boston associated with decreased lecithin-cholesterol acyltransferase activation and cellular cholesterol efflux.
Anthanont P.; Asztalos B.F.; Polisecki E.; Zachariah B.; Schaefer E.J.;
J. Clin. Lipidol. 9:390-395(2015)
Cited for: VARIANT BOSTON SER-173;

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.