UniProtKB/SwissProt variant VAR

Variant information

Variant position:

182

The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:

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:

From Arginine (R) to Leucine (L) at position 182 (R182L, p.Arg182Leu).

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 large size and basic (R) to medium size and hydrophobic (L)

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

Variant description:

In AH1; partial loss of activity.

Any additional useful information about the variant.

Other resources:

Links to websites of interest for the variant.

Variant rs104894086 [ dbSNP | Ensembl ]

Sequence information

Variant position:

182

The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:

285

The length of the canonical sequence.

Location on the sequence:

KDTFITHELAAEAAGNLVGP R DFVSVRCAKRRGSTCVLAGM

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                         KD-----------TFITHELAAEAAGNLVG---------------------------------PRDFVSVRCAKRRGSTCVLAGM

Mouse                         KD-----------TVITHELAAAAAGNLVG-----------

Rat                           KD-----------TVITHELAAAAAGNLVG-----------

Pig                           KD-----------TVITHELAAEAAGNLVG-----------

Bovine                        KD-----------TVITHELAAEVAGNLVG-----------

Sheep                         KD-----------TIITHELAAEAAGNLVG-----------

Horse                         KD-----------TVITHELAAESAGNLVG-----------

Chicken                       KD-----------TLITHETAAAPPGNIVG-----------

Xenopus laevis                KD-----------TVITHEKAAETPGNIVG-----------

Zebrafish                     QE-----------TMITHEISAETPGNVVG-----------

Drosophila                    STFGSGNSSGSGADQLAHYVADLVGGKMNGAVIQSLSGPLA

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	64 – 285	Steroidogenic acute regulatory protein, mitochondrial
Domain	67 – 280	START
Modified residue	195 – 195	Phosphoserine; by PKA
Beta strand	182 – 192

Literature citations

The pathophysiology and genetics of congenital lipoid adrenal hyperplasia.
Bose H.S.; Sugawara T.; Strauss J.F. III; Miller W.L.;
N. Engl. J. Med. 335:1870-1878(1996)
Cited for: VARIANTS AH1 GLY-169; LYS-169; LEU-182; VAL-218; ARG-272 DEL AND PRO-275; CHARACTERIZATION OF VARIANTS AH1 GLY-169; LYS-169; LEU-182; VAL-218; ARG-272 DEL AND PRO-275; CATALYTIC ACTIVITY;

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P49675: Variant p.Arg182Leu