Sequence information
Variant position: 279 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:
KDSIDREKIAVIGHSFGGAT
V IQTLSEDQRFRCGIALDAWM
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 KDSIDREKIAVIGHSFGGATV IQTLSEDQRFRCGIALDAWM
KDSIDRDKIAVIGHSFGGATV LQALSEDQRFRCGIALDAWM
Mouse KDAIDETKIALMGHSFGGATV LQALSEDQRFRCGVALDPWM
Bovine KDSIDRDKIAIIGHSFGGATV IQTLSEDQRFRCGIALDAWM
Chicken KDSVDTSRIAVMGHSFGGATV IESLSKEIRFRCGIALDAWM
Caenorhabditis elegans KNKLVMSSASVIGHSFGGATS LASSAYTTDFQKAIVFDGWM
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
22 – 441
Platelet-activating factor acetylhydrolase
Active site
273 – 273
Nucleophile
Active site
296 – 296
Charge relay system
Mutagenesis
273 – 273
S -> A. Loss of activity.
Mutagenesis
286 – 286
D -> A. Almost no activity.
Mutagenesis
286 – 286
D -> N. Diminishes activity.
Mutagenesis
296 – 296
D -> A. Loss of activity.
Mutagenesis
296 – 296
D -> N. Loss of activity.
Helix
274 – 285
Literature citations
Release of free F2-isoprostanes from esterified phospholipids is catalyzed by intracellular and plasma platelet-activating factor acetylhydrolases.
Stafforini D.M.; Sheller J.R.; Blackwell T.S.; Sapirstein A.; Yull F.E.; McIntyre T.M.; Bonventre J.V.; Prescott S.M.; Roberts L.J. II;
J. Biol. Chem. 281:4616-4623(2006)
Cited for: FUNCTION; CATALYTIC ACTIVITY; BIOPHYSICOCHEMICAL PROPERTIES; VARIANT PHE-279;
Platelet-activating factor acetylhydrolase deficiency. A missense mutation near the active site of an anti-inflammatory phospholipase.
Stafforini D.M.; Satoh K.; Atkinson D.L.; Tjoelker L.W.; Eberhardt C.; Yoshida H.; Imaizumi T.; Takamatsu S.; Zimmerman G.A.; McIntyre T.M.; Gray P.W.; Prescott S.M.;
J. Clin. Invest. 97:2784-2791(1996)
Cited for: VARIANT PAFAD PHE-279; FUNCTION; CATALYTIC ACTIVITY;
A mutation in plasma platelet-activating factor acetylhydrolase (Val279-->Phe) is a genetic risk factor for stroke.
Hiramoto M.; Yoshida H.; Imaizumi T.; Yoshimizu N.; Satoh K.;
Stroke 28:2417-2420(1997)
Cited for: VARIANT PAFAD PHE-279;
Identification of the G994--> T missense in exon 9 of the plasma platelet-activating factor acetylhydrolase gene as an independent risk factor for coronary artery disease in Japanese men.
Yamada Y.; Ichihara S.; Fujimura T.; Yokota M.;
Metabolism 47:177-181(1998)
Cited for: VARIANT PAFAD PHE-279;
A mutation in plasma platelet-activating factor acetylhydrolase (Val279Phe) is a genetic risk factor for cerebral hemorrhage but not for hypertension.
Yoshida H.; Imaizumi T.; Fujimoto K.; Itaya H.; Hiramoto M.; Yoshimizu N.; Fukushi K.; Satoh K.;
Thromb. Haemost. 80:372-375(1998)
Cited for: VARIANT PAFAD PHE-279;
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.