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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P02647: Variant p.Leu198Ser

Apolipoprotein A-I
Gene: APOA1
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Variant information Variant position: help 198 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 Leucine (L) to Serine (S) at position 198 (L198S, p.Leu198Ser). 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 hydrophobic (L) to small size and polar (S) 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 AMYLD3; plasma level of HDL and apoA-I protein were significantly lower in the patient. Any additional useful information about the variant.


Sequence information Variant position: help 198 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 267 The length of the canonical sequence.
Location on the sequence: help AHVDALRTHLAPYSDELRQR L AARLEALKENGGARLAEYHA 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                         AHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHA

Gorilla                       AHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHA

                              THVDALRAQLAPYSDDLRERLAARLEALKEGGGASLAEYHA

Rhesus macaque                AHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHA

Chimpanzee                    AHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHA

Mouse                         THVDSLRTQLAPHSEQMRESLAQRLAELKSN--PTLNEYHT

Rat                           VNADALRAKFGLYSDQMRENLAQRLTEIKNH--PTLIEYHT

Pig                           AHVEALRQHVAPYSDDLRQRMAARFEALKEGGGS-LAEYQA

Bovine                        AHVETLRQQLAPYSDDLRQRLTARLEALKEGGGS-LAEYHA

Rabbit                        THVDTLRTKLAPYSNELQQRLAARLESIKEGGGASLAEYQA

Chicken                       GHVEELRKNLAPYSDELRQKLSQKLEEIREKGIPQASEYQA

Zebrafish                     SNIEETKSKVVPMVEAVRTKLTERLEDLRTMAAPYAEEYKE
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 19 – 267 Proapolipoprotein A-I
Chain 25 – 267 Apolipoprotein A-I
Chain 25 – 266 Truncated apolipoprotein A-I
Repeat 189 – 210 7
Region 68 – 267 10 X approximate tandem repeats
Modified residue 190 – 190 3'-chlorotyrosine; alternate
Modified residue 190 – 190 3'-nitrotyrosine; alternate
Modified residue 216 – 216 3'-chlorotyrosine; alternate
Modified residue 216 – 216 3'-nitrotyrosine; alternate
Mutagenesis 190 – 190 Y -> F. Abolished chlorination and nitration without preventing inhibition in presence of myeloproxidase; when associated with F-42, F-53, F-124, F-139, F-216 and F-260.
Mutagenesis 216 – 216 Y -> F. Abolished chlorination and nitration without preventing inhibition in presence of myeloproxidase; when associated with F-42, F-53, F-124, F-139, F-190 and F-260.
Helix 166 – 203



Literature citations
The new apolipoprotein A-I variant leu(174) --> Ser causes hereditary cardiac amyloidosis, and the amyloid fibrils are constituted by the 93-residue N-terminal polypeptide.
Obici L.; Bellotti V.; Mangione P.; Stoppini M.; Arbustini E.; Verga L.; Zorzoli I.; Anesi E.; Zanotti G.; Campana C.; Vigano M.; Merlini G.;
Am. J. Pathol. 155:695-702(1999)
Cited for: VARIANT AMYLD3 SER-198; CHARACTERIZATION OF VARIANT AMYLD3 SER-198; INVOLVEMENT IN AMYLD3;
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.