PAFAH2

PAFAH2
Identifiers
Aliases	PAFAH2, HSD-PLA2, platelet activating factor acetylhydrolase 2
External IDs	MGI: 2140321 HomoloGene: 37309 GeneCards: 5051
Gene ontology Molecular function • phospholipid binding • hydrolase activity • 1-alkyl-2-acetylglycerophosphocholine esterase activity Cellular component • cytoplasm Biological process • lipid catabolic process • negative regulation of apoptotic process • lipid metabolic process Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	5051	100163
Ensembl	ENSG00000158006	ENSMUSG00000037366
UniProt	Q99487 Q5SY00	Q8VDG7
RefSeq (mRNA)	NM_000437	NM_001285872 NM_001285874 NM_001285875 NM_001285877 NM_133880
RefSeq (protein)	NP_000428.2	NP_001272803.1 NP_598641.2
Location (UCSC)	Chr 1: 25.96 – 26 Mb	Chr 4: 134.4 – 134.43 Mb
PubMed search
Wikidata
View/Edit Human		View/Edit Mouse

Platelet-activating factor acetylhydrolase 2, cytoplasmic is an enzyme that in humans is encoded by the PAFAH2 gene. It is one of several PAF acetylhydrolases.

Function

This gene encodes platelet-activating factor acetylhydrolase isoform 2, a single-subunit intracellular enzyme that catalyzes the removal of the acetyl group at the SN-2 position of platelet-activating factor (identified as 1-O-alkyl-2-acetyl-sn-glyceryl-3-phosphorylcholine). However, this lipase exhibits a broader substrate specificity than simply platelet activating factor. Two other isoforms of intracellular platelet-activating factor acetylhydrolase exist, and both are multi-subunit enzymes. Additionally, there is a single-subunit serum isoform of this enzyme.

Further reading

• Stafforini DM, McIntyre TM, Zimmerman GA, Prescott SM (Jul 1997). "Platelet-activating factor acetylhydrolases". The Journal of Biological Chemistry. 272 (29): 17895–8. doi:10.1074/jbc.272.29.17895. PMID 9218411. 
• Umemura K, Kato I, Hirashima Y, Ishii Y, Inoue T, Aoki J, Kono N, Oya T, Hayashi N, Hamada H, Endo S, Oda M, Arai H, Kinouchi H, Hiraga K (Mar 2007). "Neuroprotective role of transgenic PAF-acetylhydrolase II in mouse models of focal cerebral ischemia". Stroke; A Journal of Cerebral Circulation. 38 (3): 1063–8. doi:10.1161/01.STR.0000257981.09329.d2. PMID 17272759. 
• Schmidt EB, Koenig W, Khuseyinova N, Christensen JH (Jan 2008). "Lipoprotein-associated phospholipase A2 concentrations in plasma are associated with the extent of coronary artery disease and correlate to adipose tissue levels of marine n-3 fatty acids". Atherosclerosis. 196 (1): 420–4. doi:10.1016/j.atherosclerosis.2006.11.027. PMID 17157859. 
• Unno N, Sakaguchi T, Nakamura T, Yamamoto N, Sugatani J, Miwa M, Konno H (Jul 2006). "A single nucleotide polymorphism in the plasma PAF acetylhydrolase gene and risk of atherosclerosis in Japanese patients with peripheral artery occlusive disease". The Journal of Surgical Research. 134 (1): 36–43. doi:10.1016/j.jss.2006.02.058. PMID 16650870. 
• Marques M, Pei Y, Southall MD, Johnston JM, Arai H, Aoki J, Inoue T, Seltmann H, Zouboulis CC, Travers JB (Oct 2002). "Identification of platelet-activating factor acetylhydrolase II in human skin". The Journal of Investigative Dermatology. 119 (4): 913–9. doi:10.1046/j.1523-1747.2002.01859.x. PMID 12406338. 
• Min JH, Wilder C, Aoki J, Arai H, Inoue K, Paul L, Gelb MH (Apr 2001). "Platelet-activating factor acetylhydrolases: broad substrate specificity and lipoprotein binding does not modulate the catalytic properties of the plasma enzyme". Biochemistry. 40 (15): 4539–49. doi:10.1021/bi002600g. PMID 11294621.