UniProtKB/Swiss-Prot P02647: Variant p.Glu163Gly

Apolipoprotein A-I
Gene: APOA1
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Variant information Variant position:

163 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 Glycine (G) at position 163 (E163G, p.Glu163Gly). 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 glycine (G) 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.

Variant rs758509542 [ dbSNP | Ensembl ]

Sequence information Variant position:

163 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:

VEPLRAELQEGARQKLHELQ E KLSPLGEEMRDRARAHVDAL 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                         VEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDAL

Gorilla                       VEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDAL

                              VAPLGSELREGARQKLQELQEKLSPLAEELRDRARTHVDAL

Rhesus macaque                VEPLRAELHEGTRQKLHELHEKLSPLGEEVRDRARAHVDAL

Chimpanzee                    VEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDAL

Mouse                         VAPLGAELQESARQKLQELQGRLSPVAEEFRDRMRTHVDSL

Rat                           LEPLGTELHKNAK----EMQRHLKVVAEEFRDRMRVNADAL

Pig                           MAPLGAEFREGARQKVQELQEKLSPLAEELRDRLRAHVEAL

Bovine                        VAPLGEEFREGARQKVQELQDKLSPLAQELRDRARAHVETL

Rabbit                        VEPLGAELRESARQKLTELQEKLSPLAEELRDSARTHVDTL

Chicken                       LTPVAQELKELTKQKVELMQAKLTPVAEEARDRLRGHVEEL

Zebrafish                     LEPVFQEYSALNRQNAEQLRAKLEPLMDDIRKAFESNIEET

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.

Type	Positions	Description
Chain	19 – 267	Proapolipoprotein A-I
Chain	25 – 267	Apolipoprotein A-I
Chain	25 – 266	Truncated apolipoprotein A-I
Repeat	145 – 166	5
Region	68 – 267	10 X approximate tandem repeats
Turn	159 – 164

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.