UniProtKB/Swiss-Prot P06727: Variant p.Ala161Ser

Apolipoprotein A-IV
Gene: APOA4
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Variant information Variant position:

161 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 Alanine (A) to Serine (S) at position 161 (A161S, p.Ala161Ser). 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 small size and hydrophobic (A) 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
Polymorphism:

Eight alleles have been characterized (APOA-IV*0 to APOA-IV*7). APOA-IV*1 is the major allele (90%), APOA-IV*2 is also common (8%), the others are rare alleles. Additional information on the polymorphism described.
Variant description:

In Seattle-3. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs12721043 [ dbSNP | Ensembl ]

Sequence information Variant position:

161 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

396 The length of the canonical sequence.
Location on the sequence:

QLRTQVSTQAEQLRRQLTPY A QRMERVLRENADSLQASLRP 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                         QLRTQVSTQAEQLRRQLTPYAQRMERVLRENADSLQASLRP

                              ELRTQVNTHAEQLRNQLTSHAQRMQSALRQNVDDLHSSLTP

Mouse                         DLQDQINTQTQEMKLQLTPYIQRMQTTIKENVDNLHTSMMP

Rat                           DLQAQINAQTQDMKRQLTPYIQRMQTTIQDNVENLQSSMVP

Pig                           GLRTQVNTQVQQLQRQLKPYAERMESVLRQNIRNLEASVAP

Bovine                        ELRTQVDTQAQQLRRQLTPYVERMEKVMRQNLDQLQASLAP

Cat                           ELRTQVNTHAEHLRRHLTSHAQRMEAVLRENVDNLQSSLTP

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	21 – 396	Apolipoprotein A-IV
Repeat	159 – 180	6
Region	33 – 330	13 X 22 AA approximate tandem repeats
Helix	117 – 223

Literature citations
The effects of scale: variation in the APOA1/C3/A4/A5 gene cluster.
Fullerton S.M.; Buchanan A.V.; Sonpar V.A.; Taylor S.L.; Smith J.D.; Carlson C.S.; Salomaa V.; Stengaard J.H.; Boerwinkle E.; Clark A.G.; Nickerson D.A.; Weiss K.M.;
Hum. Genet. 115:36-56(2004)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; VARIANTS MET-13; HIS-77; ASN-147; SER-161; SER-367 AND HIS-380; Two novel apolipoprotein A-IV variants in individuals with familial combined hyperlipidemia and diminished levels of lipoprotein lipase activity.
Deeb S.S.; Nevin D.N.; Iwasaki L.; Brunzell J.D.;
Hum. Mutat. 8:319-325(1996)
Cited for: VARIANT SEATTLE-3 SER-161; VARIANT SEATTLE-1 LEU-178; VARIANT SEATTLE-2 GLN-264;

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.