UniProtKB/Swiss-Prot P0DJI8: Variant p.Val75Ala

Serum amyloid A-1 protein
Gene: SAA1
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Variant information Variant position:

75 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 Valine (V) to Alanine (A) at position 75 (V75A, p.Val75Ala). 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 hydrophobic (V) to small size and hydrophobic (A) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

0 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:

At least 5 different SAA1 alleles have been described: SAA1.1 (SAA1alpha), SAA1.2 (SAA1beta), SAA1.3 (SAA1gamma), SAA1.4 (SAA1delta), SAA1.5 (also named SAA1beta but which differs from SAA1.2). We use here the revised nomenclature described in PubMed:10211414. The sequence shown is that of SAA1.2. Additional information on the polymorphism described.
Variant description:

In allele SAA1.1 and allele SAA1.3. Any additional useful information about the variant.

Sequence information Variant position:

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

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

HARGNYDAAKRGPGGAWAAE V ITDARENIQRFFGHGAEDSL 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                         HARGNYDAAKRGPGGAWAAEVITDARENIQRFFGHGAEDSL

Mouse                         HARGNYDAAQRGPGGVWAAEKISDGREAFQEFFGRGHEDTI

Rabbit                        HARGNYDAAQRGPGGVWAAKVISDAREDLQRLMGHGAEDSM

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 – 122	Serum amyloid A-1 protein
Chain	19 – 94	Amyloid protein A
Chain	20 – 122	Serum amyloid protein A(2-104)
Chain	20 – 121	Serum amyloid protein A(2-103)
Chain	20 – 120	Serum amyloid protein A(2-102)
Chain	21 – 122	Serum amyloid protein A(3-104)
Chain	22 – 119	Serum amyloid protein A(4-101)
Mutagenesis	65 – 65	R -> A. Reduces affinity for heparin; when associated with A-33 and A-37.
Mutagenesis	80 – 80	R -> A. Reduces affinity for heparin and nearly abolishes association with HDL; when associated with A-18 and A-89.
Mutagenesis	89 – 89	H -> A. Reduces affinity for heparin and nearly abolishes association with HDL; when associated with A-18 and A-80.
Helix	67 – 86

Literature citations
Human serum amyloid A (SAA): biosynthesis and postsynthetic processing of preSAA and structural variants defined by complementary DNA.
Sipe J.D.; Colten H.R.; Goldberger G.; Edge M.D.; Tack B.F.; Cohen A.S.; Whitehead A.S.;
Biochemistry 24:2931-2936(1985)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE SAA1.1); VARIANTS VAL-70; ALA-75 AND SER-77; Human serum amyloid A. Three hepatic mRNAs and the corresponding proteins in one person.
Kluve-Beckerman B.; Dwulet F.E.; Benson M.D.;
J. Clin. Invest. 82:1670-1675(1988)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE SAA1.1); VARIANTS VAL-70; ALA-75 AND SER-77; The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
The MGC Project Team;
Genome Res. 14:2121-2127(2004)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE SAA1.1); VARIANTS VAL-70; ALA-75 AND SER-77; Heterogeneity of human serum amyloid A protein. Five different variants from one individual demonstrated by cDNA sequence analysis.
Steinkasserer A.; Weiss E.H.; Schwaeble W.; Linke R.P.;
Biochem. J. 268:187-193(1990)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 73-122; VARIANTS ALA-75; SER-77 AND ASN-78; Identification of two novel amyloid A protein subsets coexisting in an individual patient of AA-amyloidosis.
Baba S.; Takahashi T.; Kasama T.; Shirasawa H.;
Biochim. Biophys. Acta 1180:195-200(1992)
Cited for: PROTEIN SEQUENCE OF 19-94; MASS SPECTROMETRY; DISEASE; VARIANTS ALA-75 AND ASN-78; ALLELE SAA1.3;

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.