UniProtKB/Swiss-Prot P02647: Variant p.Pro189Arg

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

189 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 Proline (P) to Arginine (R) at position 189 (P189R, p.Pro189Arg). 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 (P) to large size and basic (R) 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 rs121912722 [ dbSNP | Ensembl ]

Sequence information Variant position:

189 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:

GEEMRDRARAHVDALRTHLA P YSDELRQRLAARLEALKENG 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                         GEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENG

Gorilla                       GEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENG

                              AEELRDRARTHVDALRAQLAPYSDDLRERLAARLEALKEGG

Rhesus macaque                GEEVRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENG

Chimpanzee                    GEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENG

Mouse                         AEEFRDRMRTHVDSLRTQLAPHSEQMRESLAQRLAELKSN-

Rat                           AEEFRDRMRVNADALRAKFGLYSDQMRENLAQRLTEIKNH-

Pig                           AEELRDRLRAHVEALRQHVAPYSDDLRQRMAARFEALKEGG

Bovine                        AQELRDRARAHVETLRQQLAPYSDDLRQRLTARLEALKEGG

Rabbit                        AEELRDSARTHVDTLRTKLAPYSNELQQRLAARLESIKEGG

Chicken                       AEEARDRLRGHVEELRKNLAPYSDELRQKLSQKLEEIREKG

Zebrafish                     MDDIRKAFESNIEETKSKVVPMVEAVRTKLTERLEDLRTMA

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	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
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.
Helix	166 – 203

Literature citations
Apolipoprotein A-I variants. Naturally occurring substitutions of proline residues affect plasma concentration of apolipoprotein A-I.
von Eckardstein A.; Funke H.; Henke A.; Altland K.; Benninghoven A.; Assmann G.; Welp S.; Roetrige A.; Kock R.;
J. Clin. Invest. 84:1722-1730(1989)
Cited for: VARIANTS ARG-27; ARG-28 AND ARG-189;

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.