UniProtKB/SwissProt variant VAR

Variant information

Variant position:

111

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

Type of variant:

US

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 Serine (S) to Proline (P) at position 111 (S111P, p.Ser111Pro).

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 polar (S) to medium size and hydrophobic (P)

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

Variant description:

In GURDP; unknown pathological significance.

Any additional useful information about the variant.

Other resources:

Links to websites of interest for the variant.

Variant rs121434634 [ dbSNP | Ensembl ]

Sequence information

Variant position:

111

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

Protein sequence length:

749

The length of the canonical sequence.

Location on the sequence:

LMDANYVMDETLGTATFTVS S MKVGEKKEVPFIFNQVTEMV

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                         LMDANYVMDETLGTATFTVSSMKVGEKKEVPFIFNQVTEMV

Mouse                         LMDANYVMDETLGTATFPVSSMKVGEKKEVPFIFNQVTEMI

Rat                           LMDANYVMDETLGTATFPVSSMKVGEKKEVPFIFNQVTEMI

Bovine                        LMDANYVMDETLGTTTFPISSMKVGEKKQVPFIFNQVTEMI

Rabbit                        LMDANYVMDETLGTATFPVSSMKVGEKKEVPFIFNQVTEMI

Horse                         LMDANYVMDETLGTATFTLSSMKVGEKKEVPFIFNQVTEMI

Chicken                       LMDANYVMDETLGMATFPISSLKLGEKKEVQLTFNNVTEMT

Xenopus laevis                LMDANYVMDESLGTTTFPILSVKPGEKKQVPFTFNKVTEMI

Xenopus tropicalis            LMDANYVMDESLGTTTFPISSVKPGEKKQVPFTFNKVTEMI

Zebrafish                     LMDANYVMDETLGTAKYSLSKLKVAQMEHVTLSIGKTTKVF

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	1 – 749	Cytosolic phospholipase A2
Domain	6 – 122	C2
Region	1 – 178	Phospholipid binding
Metal binding	93 – 93	Calcium 2
Metal binding	94 – 94	Calcium 2; via carbonyl oxygen
Metal binding	95 – 95	Calcium 2
Helix	109 – 111

Literature citations

Inherited human cPLA(2alpha) deficiency is associated with impaired eicosanoid biosynthesis, small intestinal ulceration, and platelet dysfunction.
Adler D.H.; Cogan J.D.; Phillips J.A.; Schnetz-Boutaud N.; Milne G.L.; Iverson T.; Stein J.A.; Brenner D.A.; Morrow J.D.; Boutaud O.; Oates J.A.;
J. Clin. Invest. 118:2121-2131(2008)
Cited for: INVOLVEMENT IN GURDP; VARIANTS GURDP PRO-111 AND HIS-485; VARIANT LYS-651; FUNCTION; CATALYTIC ACTIVITY; PATHWAY;

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P47712: Variant p.Ser111Pro