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UniProtKB/Swiss-Prot P02647: Variant p.Glu171Val

Apolipoprotein A-I
Gene: APOA1
Variant information

Variant position:  171
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  LB/B
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 Glutamate (E) to Valine (V) at position 171 (E171V, p.Glu171Val).
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 medium size and acidic (E) to medium size and hydrophobic (V)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -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

Polymorphism:  Genetic variations in APOA1 can result in APOA1 deficiency and are associated with low levels of HDL cholesterol [MIM:107680].
Additional information on the polymorphism described.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  171
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:   QEGARQKLHELQEKLSPLGE  E MRDRARAHVDALRTHLAPYS
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                         QEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYS

Gorilla                       QEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYS

                              REGARQKLQELQEKLSPLAEELRDRARTHVDALRAQLAPYS

Rhesus macaque                HEGTRQKLHELHEKLSPLGEEVRDRARAHVDALRTHLAPYS

Chimpanzee                    QEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYS

Mouse                         QESARQKLQELQGRLSPVAEEFRDRMRTHVDSLRTQLAPHS

Rat                           H----KNAKEMQRHLKVVAEEFRDRMRVNADALRAKFGLYS

Pig                           REGARQKVQELQEKLSPLAEELRDRLRAHVEALRQHVAPYS

Bovine                        REGARQKVQELQDKLSPLAQELRDRARAHVETLRQQLAPYS

Rabbit                        RESARQKLTELQEKLSPLAEELRDSARTHVDTLRTKLAPYS

Chicken                       KELTKQKVELMQAKLTPVAEEARDRLRGHVEELRKNLAPYS

Zebrafish                     SALNRQNAEQLRAKLEPLMDDIRKAFESNIEETKSKVVPMV

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

Structural analysis of human apolipoprotein A-I variants. Amino acid substitutions are nonrandomly distributed throughout the apolipoprotein A-I primary structure.
von Eckardstein A.; Funke H.; Walter M.; Altland K.; Benninghoven A.; Assmann G.;
J. Biol. Chem. 265:8610-8617(1990)
Cited for: VARIANTS GLU-113; MET-131; GLY-163; VAL-171 AND LYS-222;

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.