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UniProtKB/Swiss-Prot Q13093: Variant p.Val379Ala

Platelet-activating factor acetylhydrolase
Gene: PLA2G7
Variant information

Variant position:  379
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 379 (V379A, p.Val379Ala).
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

Variant description:  Retains the ability to associate with HDL particles.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  379
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  441
The length of the canonical sequence.

Location on the sequence:   FATGKIIGHMLKLKGDIDSN  V AIDLSNKASLAFLQKHLGLH
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                         FATGKIIGHMLKLKGDIDSNVAIDLSNKASLAFLQKHLGLH

                              FTTGKIVGYIFTLKGDIDSNVAIDLCNKASLAFLQKHLGLR

Mouse                         FVTGKIIGNKLTLKGEIDSRVAIDLTNKASMAFLQKHLGLQ

Bovine                        FATSKIIGYLFTLKGDIDSNVAISLSNKASLAFLQKHLGLQ

Chicken                       FVSGEIIGKFFKLKGEIDPNEAIDICNHASLAFLQKHLSLK

Caenorhabditis elegans        FIFPSWLAKKFGVQGRTEPSLCMQAAIELSLAFLEN-----

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.

TypePositionsDescription
Chain 22 – 441 Platelet-activating factor acetylhydrolase
Mutagenesis 367 – 367 H -> N. Reduces the association with HDL particles.
Mutagenesis 368 – 368 M -> K. Impairs the association with HDL particles.
Mutagenesis 369 – 369 L -> A. Impairs the association with HDL particles.
Mutagenesis 370 – 370 K -> T. Reduces the association with HDL particles.
Helix 377 – 396


Literature citations

Submission
SeattleSNPs variation discovery resource;
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; VARIANTS PRO-45; HIS-92; ASN-191; THR-198 AND ALA-379;

Submission
Mural R.J.; Istrail S.; Sutton G.G.; Florea L.; Halpern A.L.; Mobarry C.M.; Lippert R.; Walenz B.; Shatkay H.; Dew I.; Miller J.R.; Flanigan M.J.; Edwards N.J.; Bolanos R.; Fasulo D.; Halldorsson B.V.; Hannenhalli S.; Turner R.; Yooseph S.; Lu F.; Nusskern D.R.; Shue B.C.; Zheng X.H.; Zhong F.; Delcher A.L.; Huson D.H.; Kravitz S.A.; Mouchard L.; Reinert K.; Remington K.A.; Clark A.G.; Waterman M.S.; Eichler E.E.; Adams M.D.; Hunkapiller M.W.; Myers E.W.; Venter J.C.;
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]; VARIANT ALA-379;

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]; VARIANT ALA-379;

Identification of a domain that mediates association of platelet-activating factor acetylhydrolase with high density lipoprotein.
Gardner A.A.; Reichert E.C.; Topham M.K.; Stafforini D.M.;
J. Biol. Chem. 283:17099-17106(2008)
Cited for: FUNCTION; CATALYTIC ACTIVITY; SUBCELLULAR LOCATION; MUTAGENESIS OF HIS-367; MET-368; LEU-369 AND LYS-370; VARIANTS HIS-92; THR-198 AND ALA-379;

The Ile198Thr and Ala379Val variants of plasmatic PAF-acetylhydrolase impair catalytical activities and are associated with atopy and asthma.
Kruse S.; Mao X.-Q.; Heinzmann A.; Blattmann S.; Roberts M.H.; Braun S.; Gao P.-S.; Forster J.; Kuehr J.; Hopkin J.M.; Shirakawa T.; Deichmann K.A.;
Am. J. Hum. Genet. 66:1522-1530(2000)
Cited for: VARIANTS HIS-92; THR-198 AND ALA-379; INVOLVEMENT IN ASTHMA AND ATOPY;

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.