ID PAFA_HUMAN Reviewed; 441 AA. AC Q13093; A5HTT5; Q15692; Q5VTT1; Q8IVA2; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 27-MAR-2024, entry version 203. DE RecName: Full=Platelet-activating factor acetylhydrolase; DE Short=PAF acetylhydrolase; DE EC=3.1.1.47 {ECO:0000269|PubMed:10066756, ECO:0000269|PubMed:16371369, ECO:0000269|PubMed:18434304, ECO:0000269|PubMed:7592717, ECO:0000269|PubMed:7700381, ECO:0000269|PubMed:8624782, ECO:0000269|PubMed:8675689}; DE AltName: Full=1-alkyl-2-acetylglycerophosphocholine esterase; DE AltName: Full=2-acetyl-1-alkylglycerophosphocholine esterase; DE AltName: Full=Group-VIIA phospholipase A2; DE Short=gVIIA-PLA2; DE AltName: Full=LDL-associated phospholipase A2; DE Short=LDL-PLA(2); DE AltName: Full=PAF 2-acylhydrolase; DE Flags: Precursor; GN Name=PLA2G7; Synonyms=PAFAH; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 42-57, FUNCTION, AND RP CATALYTIC ACTIVITY. RC TISSUE=Myeloid; RX PubMed=7700381; DOI=10.1038/374549a0; RA Tjoelker L.W., Wilder C., Eberhardt C., Stafforini D.M., Dietsch G., RA Schimpf B., Hooper S., le Trong H., Cousens L.S., Zimmerman G.A., RA Yamada Y., McIntyre T.M., Prescott S.M., Gray P.W.; RT "Anti-inflammatory properties of a platelet-activating factor RT acetylhydrolase."; RL Nature 374:549-553(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, AND RP CATALYTIC ACTIVITY. RC TISSUE=Lymphoma; RX PubMed=8624782; DOI=10.1161/01.atv.16.4.591; RA Tew D.G., Southan C., Rice S.Q.J., Lawrence M.P., Li H., Boyd H.F., RA Moores K., Gloger I.S., Macphee C.H.; RT "Purification, properties, sequencing, and cloning of a lipoprotein- RT associated, serine-dependent phospholipase involved in the oxidative RT modification of low-density lipoproteins."; RL Arterioscler. Thromb. Vasc. Biol. 16:591-599(1996). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PRO-45; HIS-92; ASN-191; RP THR-198 AND ALA-379. RG SeattleSNPs variation discovery resource; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-379. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-379. RC TISSUE=Blood; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=2040620; DOI=10.1016/s0021-9258(18)99132-5; RA Stremler K.E., Stafforini D.M., Prescott S.M., McIntyre T.M.; RT "Human plasma platelet-activating factor acetylhydrolase. Oxidatively RT fragmented phospholipids as substrates."; RL J. Biol. Chem. 266:11095-11103(1991). RN [8] RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF SER-108; SER-273; ASP-286; ASP-296; RP ASP-304; ASP-338 AND HIS-351. RX PubMed=7592717; DOI=10.1074/jbc.270.43.25481; RA Tjoelker L.W., Eberhardt C., Unger J., le Trong H., Zimmerman G.A., RA McIntyre T.M., Stafforini D.M., Prescott S.M., Gray P.W.; RT "Plasma platelet-activating factor acetylhydrolase is a secreted RT phospholipase A2 with a catalytic triad."; RL J. Biol. Chem. 270:25481-25487(1995). RN [9] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=10504265; DOI=10.1021/bi991149u; RA Min J.H., Jain M.K., Wilder C., Paul L., Apitz-Castro R., Aspleaf D.C., RA Gelb M.H.; RT "Membrane-bound plasma platelet activating factor acetylhydrolase acts on RT substrate in the aqueous phase."; RL Biochemistry 38:12935-12942(1999). RN [10] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF RP HIS-114; TRP-115; LEU-116; MET-117 AND TYR-205. RX PubMed=10066756; DOI=10.1074/jbc.274.11.7018; RA Stafforini D.M., Tjoelker L.W., McCormick S.P., Vaitkus D., McIntyre T.M., RA Gray P.W., Young S.G., Prescott S.M.; RT "Molecular basis of the interaction between plasma platelet-activating RT factor acetylhydrolase and low density lipoprotein."; RL J. Biol. Chem. 274:7018-7024(1999). RN [11] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, GLYCOSYLATION, TISSUE RP SPECIFICITY, AND INDUCTION. RX PubMed=11590221; RA Tselepis A.D., Karabina S.A., Stengel D., Piedagnel R., Chapman M.J., RA Ninio E.; RT "N-linked glycosylation of macrophage-derived PAF-AH is a major determinant RT of enzyme association with plasma HDL."; RL J. Lipid Res. 42:1645-1654(2001). RN [12] RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=12821559; DOI=10.1161/01.cir.0000072791.40232.8f; RA Benitez S., Sanchez-Quesada J.L., Ribas V., Jorba O., Blanco-Vaca F., RA Gonzalez-Sastre F., Ordonez-Llanos J.; RT "Platelet-activating factor acetylhydrolase is mainly associated with RT electronegative low-density lipoprotein subfraction."; RL Circulation 108:92-96(2003). RN [13] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND VARIANT RP PHE-279. RX PubMed=16371369; DOI=10.1074/jbc.m507340200; RA Stafforini D.M., Sheller J.R., Blackwell T.S., Sapirstein A., Yull F.E., RA McIntyre T.M., Bonventre J.V., Prescott S.M., Roberts L.J. II; RT "Release of free F2-isoprostanes from esterified phospholipids is catalyzed RT by intracellular and plasma platelet-activating factor acetylhydrolases."; RL J. Biol. Chem. 281:4616-4623(2006). RN [14] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=17090529; DOI=10.1074/jbc.m608135200; RA Kriska T., Marathe G.K., Schmidt J.C., McIntyre T.M., Girotti A.W.; RT "Phospholipase action of platelet-activating factor acetylhydrolase, but RT not paraoxonase-1, on long fatty acyl chain phospholipid hydroperoxides."; RL J. Biol. Chem. 282:100-108(2007). RN [15] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-367; RP MET-368; LEU-369 AND LYS-370, AND VARIANTS HIS-92; THR-198 AND ALA-379. RX PubMed=18434304; DOI=10.1074/jbc.m802394200; RA Gardner A.A., Reichert E.C., Topham M.K., Stafforini D.M.; RT "Identification of a domain that mediates association of platelet- RT activating factor acetylhydrolase with high density lipoprotein."; RL J. Biol. Chem. 283:17099-17106(2008). RN [16] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 47-429 ALONE AND IN COMPLEX WITH RP PARAOXON, AND ACTIVE SITE. RX PubMed=18784071; DOI=10.1074/jbc.m804750200; RA Samanta U., Bahnson B.J.; RT "Crystal structure of human plasma platelet-activating factor RT acetylhydrolase: structural implication to lipoprotein binding and RT catalysis."; RL J. Biol. Chem. 283:31617-31624(2008). RN [17] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 47-429 IN COMPLEX WITH RP ORGANOPHOSPHORUS NERVE AGENTS. RX PubMed=19394314; DOI=10.1016/j.bcp.2009.04.018; RA Samanta U., Kirby S.D., Srinivasan P., Cerasoli D.M., Bahnson B.J.; RT "Crystal structures of human group-VIIA phospholipase A2 inhibited by RT organophosphorus nerve agents exhibit non-aged complexes."; RL Biochem. Pharmacol. 78:420-429(2009). RN [18] RP VARIANT PAFAD PHE-279, FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=8675689; DOI=10.1172/jci118733; RA Stafforini D.M., Satoh K., Atkinson D.L., Tjoelker L.W., Eberhardt C., RA Yoshida H., Imaizumi T., Takamatsu S., Zimmerman G.A., McIntyre T.M., RA Gray P.W., Prescott S.M.; RT "Platelet-activating factor acetylhydrolase deficiency. A missense mutation RT near the active site of an anti-inflammatory phospholipase."; RL J. Clin. Invest. 97:2784-2791(1996). RN [19] RP VARIANT PAFAD ARG-281. RX PubMed=9245731; DOI=10.1006/bbrc.1997.7047; RA Yamada Y., Yokota M.; RT "Loss of activity of plasma platelet-activating factor acetylhydrolase due RT to a novel Gln281-->Arg mutation."; RL Biochem. Biophys. Res. Commun. 236:772-775(1997). RN [20] RP VARIANT PAFAD PHE-279. RX PubMed=9412624; DOI=10.1161/01.str.28.12.2417; RA Hiramoto M., Yoshida H., Imaizumi T., Yoshimizu N., Satoh K.; RT "A mutation in plasma platelet-activating factor acetylhydrolase RT (Val279-->Phe) is a genetic risk factor for stroke."; RL Stroke 28:2417-2420(1997). RN [21] RP VARIANT PAFAD PHE-279. RX PubMed=9472966; DOI=10.1016/s0026-0495(98)90216-5; RA Yamada Y., Ichihara S., Fujimura T., Yokota M.; RT "Identification of the G994--> T missense in exon 9 of the plasma platelet- RT activating factor acetylhydrolase gene as an independent risk factor for RT coronary artery disease in Japanese men."; RL Metabolism 47:177-181(1998). RN [22] RP VARIANT PAFAD PHE-279. RX PubMed=9759612; RA Yoshida H., Imaizumi T., Fujimoto K., Itaya H., Hiramoto M., Yoshimizu N., RA Fukushi K., Satoh K.; RT "A mutation in plasma platelet-activating factor acetylhydrolase RT (Val279Phe) is a genetic risk factor for cerebral hemorrhage but not for RT hypertension."; RL Thromb. Haemost. 80:372-375(1998). RN [23] RP VARIANTS HIS-92; THR-198 AND ALA-379. RX PubMed=10733466; DOI=10.1086/302901; RA Kruse S., Mao X.-Q., Heinzmann A., Blattmann S., Roberts M.H., Braun S., RA Gao P.-S., Forster J., Kuehr J., Hopkin J.M., Shirakawa T., Deichmann K.A.; RT "The Ile198Thr and Ala379Val variants of plasmatic PAF-acetylhydrolase RT impair catalytical activities and are associated with atopy and asthma."; RL Am. J. Hum. Genet. 66:1522-1530(2000). CC -!- FUNCTION: Lipoprotein-associated calcium-independent phospholipase A2 CC involved in phospholipid catabolism during inflammatory and oxidative CC stress response (PubMed:7700381, PubMed:8624782, PubMed:2040620, CC PubMed:16371369, PubMed:17090529, PubMed:10066756). At the lipid- CC aqueous interface, hydrolyzes the ester bond of fatty acyl group CC attached at sn-2 position of phospholipids (phospholipase A2 activity) CC (PubMed:2040620, PubMed:10504265). Specifically targets phospholipids CC with a short-chain fatty acyl group at sn-2 position (PubMed:2040620). CC Can hydrolyze phospholipids with long fatty acyl chains, only if they CC carry oxidized functional groups (PubMed:2040620, PubMed:8624782). CC Hydrolyzes and inactivates platelet-activating factor (PAF, 1-O-alkyl- CC 2-acetyl-sn-glycero-3-phosphocholine), a potent pro-inflammatory CC signaling lipid that acts through PTAFR on various innate immune cells CC (PubMed:10504265, PubMed:10066756, PubMed:7592717, PubMed:11590221, CC PubMed:7700381, PubMed:18434304, PubMed:16371369, PubMed:8675689, CC PubMed:8624782). Hydrolyzes oxidatively truncated phospholipids CC carrying an aldehyde group at omega position, preventing their CC accumulation in low-density lipoprotein (LDL) particles and CC uncontrolled pro-inflammatory effects (PubMed:2040620, PubMed:7700381). CC As part of high-density lipoprotein (HDL) particles, can hydrolyze CC phospholipids having long-chain fatty acyl hydroperoxides at sn-2 CC position and protect against potential accumulation of these oxylipins CC in the vascular wall (PubMed:17090529). Catalyzes the release from CC membrane phospholipids of F2-isoprostanes, lipid biomarkers of cellular CC oxidative damage (PubMed:16371369). {ECO:0000269|PubMed:10066756, CC ECO:0000269|PubMed:10504265, ECO:0000269|PubMed:11590221, CC ECO:0000269|PubMed:16371369, ECO:0000269|PubMed:17090529, CC ECO:0000269|PubMed:18434304, ECO:0000269|PubMed:2040620, CC ECO:0000269|PubMed:7592717, ECO:0000269|PubMed:7700381, CC ECO:0000269|PubMed:8624782, ECO:0000269|PubMed:8675689}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O- CC alkyl-sn-glycero-3-phosphocholine + acetate + H(+); CC Xref=Rhea:RHEA:17777, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30089, ChEBI:CHEBI:30909, ChEBI:CHEBI:36707; EC=3.1.1.47; CC Evidence={ECO:0000269|PubMed:10066756, ECO:0000269|PubMed:16371369, CC ECO:0000269|PubMed:18434304, ECO:0000269|PubMed:7592717, CC ECO:0000269|PubMed:7700381, ECO:0000269|PubMed:8624782, CC ECO:0000269|PubMed:8675689}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17778; CC Evidence={ECO:0000305|PubMed:8675689}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-O-decyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O- CC decyl-sn-glycero-3-phosphocholine + acetate + H(+); CC Xref=Rhea:RHEA:41376, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30089, ChEBI:CHEBI:78108, ChEBI:CHEBI:78109; CC Evidence={ECO:0000269|PubMed:10504265}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41377; CC Evidence={ECO:0000305|PubMed:10504265}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-O-dodecyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O- CC dodecyl-sn-glycero-3-phosphocholine + acetate + H(+); CC Xref=Rhea:RHEA:41372, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30089, ChEBI:CHEBI:78103, ChEBI:CHEBI:78104; CC Evidence={ECO:0000269|PubMed:10504265}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41373; CC Evidence={ECO:0000305|PubMed:10504265}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-O-tetradecyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1- CC O-tetradecyl-sn-glycero-3-phosphocholine + acetate + H(+); CC Xref=Rhea:RHEA:41368, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30089, ChEBI:CHEBI:78101, ChEBI:CHEBI:78102; CC Evidence={ECO:0000269|PubMed:10504265}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41369; CC Evidence={ECO:0000305|PubMed:10504265}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1- CC O-hexadecyl-sn-glycero-3-phosphocholine + acetate + H(+); CC Xref=Rhea:RHEA:40479, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30089, ChEBI:CHEBI:44811, ChEBI:CHEBI:64496; CC Evidence={ECO:0000269|PubMed:10504265, ECO:0000269|PubMed:11590221}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40480; CC Evidence={ECO:0000305|PubMed:10504265}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-O-octadecyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1- CC O-octadecyl-sn-glycero-3-phosphocholine + acetate + H(+); CC Xref=Rhea:RHEA:41183, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30089, ChEBI:CHEBI:52450, ChEBI:CHEBI:75216; CC Evidence={ECO:0000269|PubMed:10504265}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41184; CC Evidence={ECO:0000305|PubMed:10504265}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1- CC hexadecanoyl-sn-glycero-3-phosphocholine + acetate + H(+); CC Xref=Rhea:RHEA:41203, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30089, ChEBI:CHEBI:72998, ChEBI:CHEBI:75219; CC Evidence={ECO:0000269|PubMed:2040620}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41204; CC Evidence={ECO:0000305|PubMed:2040620}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-propionyl-sn-glycero-3-phosphocholine + H2O = CC 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + propanoate; CC Xref=Rhea:RHEA:41191, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17272, ChEBI:CHEBI:72998, ChEBI:CHEBI:77831; CC Evidence={ECO:0000269|PubMed:2040620}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41192; CC Evidence={ECO:0000305|PubMed:2040620}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-butanoyl-sn-glycero-3-phosphocholine + H2O = CC 1-hexadecanoyl-sn-glycero-3-phosphocholine + butanoate + H(+); CC Xref=Rhea:RHEA:41195, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17968, ChEBI:CHEBI:72998, ChEBI:CHEBI:77832; CC Evidence={ECO:0000269|PubMed:2040620}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41196; CC Evidence={ECO:0000305|PubMed:2040620}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-pentanoyl-sn-glycero-3-phosphocholine + H2O = CC 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + pentanoate; CC Xref=Rhea:RHEA:41199, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:31011, ChEBI:CHEBI:72998, ChEBI:CHEBI:77833; CC Evidence={ECO:0000269|PubMed:2040620}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41200; CC Evidence={ECO:0000305|PubMed:2040620}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-glutaroyl-sn-glycero-3-phosphocholine + H2O = CC 1-hexadecanoyl-sn-glycero-3-phosphocholine + glutarate + H(+); CC Xref=Rhea:RHEA:41159, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30921, ChEBI:CHEBI:72998, ChEBI:CHEBI:77756; CC Evidence={ECO:0000269|PubMed:2040620, ECO:0000269|PubMed:7700381}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41160; CC Evidence={ECO:0000305|PubMed:2040620, ECO:0000305|PubMed:7700381}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-(5-oxopentanoyl)-sn-glycero-3-phosphocholine CC + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + 5-oxopentanoate CC + H(+); Xref=Rhea:RHEA:40483, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16120, ChEBI:CHEBI:72998, ChEBI:CHEBI:77890; CC Evidence={ECO:0000269|PubMed:16371369, ECO:0000269|PubMed:2040620}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40484; CC Evidence={ECO:0000305|PubMed:16371369, ECO:0000305|PubMed:2040620}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-(9-oxononanoyl)-sn-glycero-3-phosphocholine + CC H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + 9-oxononanoate + CC H(+); Xref=Rhea:RHEA:41179, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:61042, ChEBI:CHEBI:72998, ChEBI:CHEBI:77812; CC Evidence={ECO:0000269|PubMed:2040620}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41180; CC Evidence={ECO:0000305|PubMed:2040620}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-[9-hydroperoxy-(10E-octadecenoyl)]-sn- CC glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3- CC phosphocholine + 9-hydroperoxy-10E-octadecenoate + H(+); CC Xref=Rhea:RHEA:41151, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:72998, ChEBI:CHEBI:77753, ChEBI:CHEBI:77754; CC Evidence={ECO:0000269|PubMed:16371369, ECO:0000269|PubMed:17090529}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41152; CC Evidence={ECO:0000305|PubMed:16371369, ECO:0000305|PubMed:17090529}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-(10-hydroperoxy-8E-octadecenoyl)-sn-glycero- CC 3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + CC 10-hydroperoxy-(8E)-octadecenoate + H(+); Xref=Rhea:RHEA:41155, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, CC ChEBI:CHEBI:77749, ChEBI:CHEBI:77755; CC Evidence={ECO:0000269|PubMed:17090529}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41156; CC Evidence={ECO:0000305|PubMed:17090529}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=12.5 uM for 1-hexadecanoyl-2-acetyl-sn-glycero-3-phosphocholine CC {ECO:0000269|PubMed:2040620}; CC KM=3.1 uM for 1-hexadecanoyl-2-propionyl-sn-glycero-3-phosphocholine CC {ECO:0000269|PubMed:2040620}; CC KM=7.9 uM for 1-hexadecanoyl-2-butanoyl-sn-glycero-3-phosphocholine CC {ECO:0000269|PubMed:2040620}; CC KM=6.2 uM for 1-hexadecanoyl-2-pentanoyl-sn-glycero-3-phosphocholine CC {ECO:0000269|PubMed:2040620}; CC KM=11.3 uM for CC 1-hexadecanoyl-2-(5-oxopentanoyl)-sn-glycero-3-phosphocholine CC {ECO:0000269|PubMed:2040620}; CC KM=15.5 uM for CC 1-hexadecanoyl-2-(9-oxononanoyl)-sn-glycero-3-phosphocholine CC {ECO:0000269|PubMed:2040620}; CC KM=43.1 uM for CC 1-hexadecanoyl-2-(5-oxopentanoyl)-sn-glycero-3-phosphocholine CC {ECO:0000269|PubMed:16371369}; CC Vmax=167 umol/h/mg enzyme toward CC 1-hexadecanoyl-2-acetyl-sn-glycero-3-phosphocholine CC {ECO:0000269|PubMed:2040620}; CC Vmax=36.1 umol/h/mg enzyme toward CC 1-hexadecanoyl-2-propionyl-sn-glycero-3-phosphocholine CC {ECO:0000269|PubMed:2040620}; CC Vmax=43.4 umol/h/mg enzyme toward CC 1-hexadecanoyl-2-butanoyl-sn-glycero-3-phosphocholine CC {ECO:0000269|PubMed:2040620}; CC Vmax=42.2 umol/h/mg enzyme toward CC 1-hexadecanoyl-2-pentanoyl-sn-glycero-3-phosphocholine CC {ECO:0000269|PubMed:2040620}; CC Vmax=100 umol/h/mg enzyme toward CC 1-hexadecanoyl-2-(5-oxopentanoyl)-sn-glycero-3-phosphocholine CC {ECO:0000269|PubMed:2040620}; CC Vmax=98.4 umol/h/mg enzyme toward CC 1-hexadecanoyl-2-(9-oxononanoyl)-sn-glycero-3-phosphocholine CC {ECO:0000269|PubMed:2040620}; CC Vmax=5 umol/min/mg enzyme toward CC 1-hexadecanoyl-2-(5-oxopentanoyl)-sn-glycero-3-phosphocholine CC {ECO:0000269|PubMed:16371369}; CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space CC {ECO:0000269|PubMed:10066756, ECO:0000269|PubMed:11590221, CC ECO:0000269|PubMed:12821559, ECO:0000269|PubMed:18434304}. CC Note=Associates with both LDL and HDL particles in plasma CC (PubMed:11590221, PubMed:12821559, PubMed:18434304, PubMed:10066756). CC Mainly associates with pro-inflammatory electronegative LDL particles CC (PubMed:12821559). {ECO:0000269|PubMed:10066756, CC ECO:0000269|PubMed:11590221, ECO:0000269|PubMed:12821559, CC ECO:0000269|PubMed:18434304}. CC -!- TISSUE SPECIFICITY: Plasma (PubMed:11590221, PubMed:12821559). Secreted CC by macrophages (at protein level) (PubMed:11590221). CC {ECO:0000269|PubMed:11590221, ECO:0000269|PubMed:12821559}. CC -!- INDUCTION: Up-regulated upon monocyte differentiation toward macrophage CC lineage. {ECO:0000269|PubMed:11590221}. CC -!- PTM: N-glycosylated. Macrophage-derived PLA2G7 carries sialylated CC complex-type N-glycans that hinder its binding to HDL particles. CC {ECO:0000269|PubMed:11590221}. CC -!- DISEASE: Platelet-activating factor acetylhydrolase deficiency (PAFAD) CC [MIM:614278]: An enzymatic deficiency that results in exacerbated CC bodily response to inflammatory agents. It can be associated with CC several disease states including inflammatory gastrointestinal CC disorders, asthma and atopy. Asthmatic individuals with PAFAD may CC manifest aggravated respiratory symptoms. {ECO:0000269|PubMed:8675689, CC ECO:0000269|PubMed:9245731, ECO:0000269|PubMed:9412624, CC ECO:0000269|PubMed:9472966, ECO:0000269|PubMed:9759612}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/pla2g7/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U20157; AAC50126.1; -; mRNA. DR EMBL; U24577; AAB04170.1; -; mRNA. DR EMBL; EF568110; ABQ01234.1; -; Genomic_DNA. DR EMBL; AL591242; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471081; EAX04301.1; -; Genomic_DNA. DR EMBL; BC038452; AAH38452.1; -; mRNA. DR CCDS; CCDS4917.1; -. DR PIR; S60247; S60247. DR RefSeq; NP_001161829.1; NM_001168357.1. DR RefSeq; NP_005075.3; NM_005084.3. DR RefSeq; XP_005249465.1; XM_005249408.4. DR PDB; 3D59; X-ray; 1.50 A; A/B=47-429. DR PDB; 3D5E; X-ray; 2.10 A; A/B=47-429. DR PDB; 3F96; X-ray; 2.10 A; A/B=47-429. DR PDB; 3F97; X-ray; 1.70 A; A/B=47-429. DR PDB; 3F98; X-ray; 1.70 A; A/B/C=47-429. DR PDB; 3F9C; X-ray; 2.30 A; A/B=47-429. DR PDB; 5I8P; X-ray; 2.37 A; A/B=47-429. DR PDB; 5I9I; X-ray; 2.70 A; A/B=47-429. DR PDB; 5JAD; X-ray; 2.05 A; A=46-428. DR PDB; 5JAH; X-ray; 2.06 A; A=46-428. DR PDB; 5JAL; X-ray; 2.06 A; A=46-428. DR PDB; 5JAN; X-ray; 2.12 A; A=46-428. DR PDB; 5JAO; X-ray; 2.06 A; A=46-428. DR PDB; 5JAP; X-ray; 2.46 A; A=46-428. DR PDB; 5JAR; X-ray; 2.11 A; A=46-428. DR PDB; 5JAS; X-ray; 2.06 A; A=46-428. DR PDB; 5JAT; X-ray; 2.04 A; A=46-428. DR PDB; 5JAU; X-ray; 1.95 A; A=46-428. DR PDB; 5LP1; X-ray; 1.91 A; A=46-428. DR PDB; 5LYY; X-ray; 2.17 A; A=46-428. DR PDB; 5LZ2; X-ray; 2.10 A; A=46-428. DR PDB; 5LZ4; X-ray; 2.07 A; A=46-428. DR PDB; 5LZ5; X-ray; 2.05 A; A=46-428. DR PDB; 5LZ7; X-ray; 2.10 A; A=46-428. DR PDB; 5LZ8; X-ray; 2.11 A; A=46-428. DR PDB; 5LZ9; X-ray; 2.06 A; A=46-428. DR PDB; 5YE7; X-ray; 2.31 A; A/B=47-429. DR PDB; 5YE8; X-ray; 1.85 A; A/B=47-429. DR PDB; 5YE9; X-ray; 1.88 A; A/B=47-429. DR PDB; 5YEA; X-ray; 1.80 A; A/B=47-429. DR PDB; 6M06; X-ray; 2.10 A; A/B=54-424. DR PDB; 6M07; X-ray; 2.64 A; A/B=54-422. DR PDB; 6M08; X-ray; 2.19 A; A/B=54-424. DR PDBsum; 3D59; -. DR PDBsum; 3D5E; -. DR PDBsum; 3F96; -. DR PDBsum; 3F97; -. DR PDBsum; 3F98; -. DR PDBsum; 3F9C; -. DR PDBsum; 5I8P; -. DR PDBsum; 5I9I; -. DR PDBsum; 5JAD; -. DR PDBsum; 5JAH; -. DR PDBsum; 5JAL; -. DR PDBsum; 5JAN; -. DR PDBsum; 5JAO; -. DR PDBsum; 5JAP; -. DR PDBsum; 5JAR; -. DR PDBsum; 5JAS; -. DR PDBsum; 5JAT; -. DR PDBsum; 5JAU; -. DR PDBsum; 5LP1; -. DR PDBsum; 5LYY; -. DR PDBsum; 5LZ2; -. DR PDBsum; 5LZ4; -. DR PDBsum; 5LZ5; -. DR PDBsum; 5LZ7; -. DR PDBsum; 5LZ8; -. DR PDBsum; 5LZ9; -. DR PDBsum; 5YE7; -. DR PDBsum; 5YE8; -. DR PDBsum; 5YE9; -. DR PDBsum; 5YEA; -. DR PDBsum; 6M06; -. DR PDBsum; 6M07; -. DR PDBsum; 6M08; -. DR AlphaFoldDB; Q13093; -. DR SMR; Q13093; -. DR BioGRID; 113667; 3. DR IntAct; Q13093; 4. DR STRING; 9606.ENSP00000274793; -. DR BindingDB; Q13093; -. DR ChEMBL; CHEMBL3514; -. DR DrugBank; DB07821; (1R)-1,2,2-trimethylpropyl (R)-methylphosphinate. DR DrugBank; DB05119; Rilapladib. DR DrugCentral; Q13093; -. DR GuidetoPHARMACOLOGY; 1432; -. DR SwissLipids; SLP:000000204; -. DR ESTHER; human-PLA2G7; PAF-Acetylhydrolase. DR GlyCosmos; Q13093; 2 sites, No reported glycans. DR GlyGen; Q13093; 2 sites. DR iPTMnet; Q13093; -. DR PhosphoSitePlus; Q13093; -. DR BioMuta; PLA2G7; -. DR DMDM; 2497687; -. DR jPOST; Q13093; -. DR MassIVE; Q13093; -. DR MaxQB; Q13093; -. DR PaxDb; 9606-ENSP00000274793; -. DR PeptideAtlas; Q13093; -. DR ProteomicsDB; 59145; -. DR Pumba; Q13093; -. DR Antibodypedia; 30742; 426 antibodies from 31 providers. DR DNASU; 7941; -. DR Ensembl; ENST00000274793.12; ENSP00000274793.7; ENSG00000146070.17. DR Ensembl; ENST00000537365.1; ENSP00000445666.1; ENSG00000146070.17. DR GeneID; 7941; -. DR KEGG; hsa:7941; -. DR MANE-Select; ENST00000274793.12; ENSP00000274793.7; NM_005084.4; NP_005075.3. DR UCSC; uc010jzf.4; human. DR AGR; HGNC:9040; -. DR CTD; 7941; -. DR DisGeNET; 7941; -. DR GeneCards; PLA2G7; -. DR HGNC; HGNC:9040; PLA2G7. DR HPA; ENSG00000146070; Tissue enhanced (lymphoid tissue, placenta). DR MalaCards; PLA2G7; -. DR MIM; 601690; gene. DR MIM; 614278; phenotype. DR neXtProt; NX_Q13093; -. DR OpenTargets; ENSG00000146070; -. DR PharmGKB; PA33368; -. DR VEuPathDB; HostDB:ENSG00000146070; -. DR eggNOG; KOG3847; Eukaryota. DR GeneTree; ENSGT00390000005233; -. DR HOGENOM; CLU_022501_0_1_1; -. DR InParanoid; Q13093; -. DR OMA; GSVHHNF; -. DR OrthoDB; 3079661at2759; -. DR PhylomeDB; Q13093; -. DR TreeFam; TF313831; -. DR BRENDA; 3.1.1.4; 2681. DR BRENDA; 3.1.1.47; 2681. DR PathwayCommons; Q13093; -. DR Reactome; R-HSA-422085; Synthesis, secretion, and deacylation of Ghrelin. DR SABIO-RK; Q13093; -. DR SignaLink; Q13093; -. DR SIGNOR; Q13093; -. DR BioGRID-ORCS; 7941; 16 hits in 1146 CRISPR screens. DR EvolutionaryTrace; Q13093; -. DR GeneWiki; Lipoprotein-associated_phospholipase_A2; -. DR GenomeRNAi; 7941; -. DR Pharos; Q13093; Tchem. DR PRO; PR:Q13093; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q13093; Protein. DR Bgee; ENSG00000146070; Expressed in amniotic fluid and 134 other cell types or tissues. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0034364; C:high-density lipoprotein particle; IDA:UniProtKB. DR GO; GO:0034362; C:low-density lipoprotein particle; IDA:UniProtKB. DR GO; GO:0003847; F:1-alkyl-2-acetylglycerophosphocholine esterase activity; IDA:UniProtKB. DR GO; GO:0047499; F:calcium-independent phospholipase A2 activity; IDA:UniProtKB. DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; TAS:Reactome. DR GO; GO:0005543; F:phospholipid binding; IDA:BHF-UCL. DR GO; GO:0034440; P:lipid oxidation; IDA:BHF-UCL. DR GO; GO:0034374; P:low-density lipoprotein particle remodeling; IDA:BHF-UCL. DR GO; GO:0016486; P:peptide hormone processing; TAS:Reactome. DR GO; GO:0034638; P:phosphatidylcholine catabolic process; IDA:UniProtKB. DR GO; GO:0034441; P:plasma lipoprotein particle oxidation; IDA:BHF-UCL. DR GO; GO:0062234; P:platelet activating factor catabolic process; IDA:UniProtKB. DR GO; GO:0046469; P:platelet activating factor metabolic process; IDA:UniProtKB. DR GO; GO:0050729; P:positive regulation of inflammatory response; TAS:BHF-UCL. DR GO; GO:0090026; P:positive regulation of monocyte chemotaxis; IDA:BHF-UCL. DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR016715; PAF_acetylhydro_eukaryote. DR PANTHER; PTHR10272; PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE; 1. DR PANTHER; PTHR10272:SF12; PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE; 1. DR Pfam; PF03403; PAF-AH_p_II; 1. DR PIRSF; PIRSF018169; PAF_acetylhydrolase; 1. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1. DR PROSITE; PS00120; LIPASE_SER; 1. DR Genevisible; Q13093; HS. PE 1: Evidence at protein level; KW 3D-structure; Asthma; Direct protein sequencing; Disease variant; KW Glycoprotein; HDL; Hydrolase; LDL; Lipid degradation; Lipid metabolism; KW Phospholipid degradation; Phospholipid metabolism; Reference proteome; KW Secreted; Signal. FT SIGNAL 1..21 FT CHAIN 22..441 FT /note="Platelet-activating factor acetylhydrolase" FT /id="PRO_0000017833" FT ACT_SITE 273 FT /note="Nucleophile" FT /evidence="ECO:0000269|PubMed:18784071" FT ACT_SITE 296 FT /note="Charge relay system" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037, FT ECO:0000269|PubMed:18784071" FT ACT_SITE 351 FT /note="Charge relay system" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037, FT ECO:0000269|PubMed:18784071" FT CARBOHYD 423 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 433 FT /note="N-linked (GlcNAc...) asparagine" FT VARIANT 45 FT /note="L -> P (in dbSNP:rs45521937)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_047970" FT VARIANT 92 FT /note="R -> H (retains the ability to associate with HDL FT particles; dbSNP:rs1805017)" FT /evidence="ECO:0000269|PubMed:10733466, FT ECO:0000269|PubMed:18434304, ECO:0000269|Ref.3" FT /id="VAR_011583" FT VARIANT 191 FT /note="K -> N (in dbSNP:rs45454695)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_047971" FT VARIANT 198 FT /note="I -> T (retains the ability to associate with HDL FT particles; dbSNP:rs1805018)" FT /evidence="ECO:0000269|PubMed:10733466, FT ECO:0000269|PubMed:18434304, ECO:0000269|Ref.3" FT /id="VAR_011584" FT VARIANT 279 FT /note="V -> F (in PAFAD; loss of function; risk factor for FT coronary arthery disease and stroke; dbSNP:rs76863441)" FT /evidence="ECO:0000269|PubMed:16371369, FT ECO:0000269|PubMed:8675689, ECO:0000269|PubMed:9412624, FT ECO:0000269|PubMed:9472966, ECO:0000269|PubMed:9759612" FT /id="VAR_004268" FT VARIANT 281 FT /note="Q -> R (in PAFAD; loss of function; FT dbSNP:rs201256712)" FT /evidence="ECO:0000269|PubMed:9245731" FT /id="VAR_011585" FT VARIANT 379 FT /note="V -> A (retains the ability to associate with HDL FT particles; dbSNP:rs1051931)" FT /evidence="ECO:0000269|PubMed:10733466, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:18434304, FT ECO:0000269|Ref.3, ECO:0000269|Ref.5" FT /id="VAR_011586" FT MUTAGEN 108 FT /note="S->A: Activity is higher than wild-type." FT /evidence="ECO:0000269|PubMed:7592717" FT MUTAGEN 114 FT /note="H->A,Q,E: Impairs the association with LDL FT particles." FT /evidence="ECO:0000269|PubMed:10066756" FT MUTAGEN 115 FT /note="W->A: Impairs the association with LDL particles." FT /evidence="ECO:0000269|PubMed:10066756" FT MUTAGEN 116 FT /note="L->A: Reduces the association with LDL particles." FT /evidence="ECO:0000269|PubMed:10066756" FT MUTAGEN 117 FT /note="M->A: Reduces the association with LDL particles." FT /evidence="ECO:0000269|PubMed:10066756" FT MUTAGEN 205 FT /note="Y->A: Impairs the association with LDL particles." FT /evidence="ECO:0000269|PubMed:10066756" FT MUTAGEN 273 FT /note="S->A: Loss of activity." FT /evidence="ECO:0000269|PubMed:7592717" FT MUTAGEN 286 FT /note="D->A: Almost no activity." FT /evidence="ECO:0000269|PubMed:7592717" FT MUTAGEN 286 FT /note="D->N: Diminishes activity." FT /evidence="ECO:0000269|PubMed:7592717" FT MUTAGEN 296 FT /note="D->A: Loss of activity." FT /evidence="ECO:0000269|PubMed:7592717" FT MUTAGEN 296 FT /note="D->N: Loss of activity." FT /evidence="ECO:0000269|PubMed:7592717" FT MUTAGEN 304 FT /note="D->A: No change in activity." FT /evidence="ECO:0000269|PubMed:7592717" FT MUTAGEN 338 FT /note="D->A: Activity is higher than wild-type." FT /evidence="ECO:0000269|PubMed:7592717" FT MUTAGEN 351 FT /note="H->A: Loss of activity." FT /evidence="ECO:0000269|PubMed:7592717" FT MUTAGEN 367 FT /note="H->N: Reduces the association with HDL particles." FT /evidence="ECO:0000269|PubMed:18434304" FT MUTAGEN 368 FT /note="M->K: Impairs the association with HDL particles." FT /evidence="ECO:0000269|PubMed:18434304" FT MUTAGEN 369 FT /note="L->A: Impairs the association with HDL particles." FT /evidence="ECO:0000269|PubMed:18434304" FT MUTAGEN 370 FT /note="K->T: Reduces the association with HDL particles." FT /evidence="ECO:0000269|PubMed:18434304" FT STRAND 54..56 FT /evidence="ECO:0007829|PDB:3F98" FT STRAND 61..75 FT /evidence="ECO:0007829|PDB:3D59" FT STRAND 78..88 FT /evidence="ECO:0007829|PDB:3D59" FT STRAND 95..98 FT /evidence="ECO:0007829|PDB:3D59" FT HELIX 101..111 FT /evidence="ECO:0007829|PDB:3D59" FT HELIX 115..125 FT /evidence="ECO:0007829|PDB:3D59" FT STRAND 129..134 FT /evidence="ECO:0007829|PDB:3D59" FT STRAND 144..150 FT /evidence="ECO:0007829|PDB:3D59" FT TURN 157..160 FT /evidence="ECO:0007829|PDB:3D59" FT HELIX 161..169 FT /evidence="ECO:0007829|PDB:3D59" FT STRAND 173..177 FT /evidence="ECO:0007829|PDB:3D59" FT STRAND 184..189 FT /evidence="ECO:0007829|PDB:3D59" FT HELIX 193..198 FT /evidence="ECO:0007829|PDB:3D59" FT STRAND 202..205 FT /evidence="ECO:0007829|PDB:3D59" FT HELIX 211..213 FT /evidence="ECO:0007829|PDB:3D59" FT HELIX 214..240 FT /evidence="ECO:0007829|PDB:3D59" FT HELIX 255..258 FT /evidence="ECO:0007829|PDB:3D59" FT STRAND 262..272 FT /evidence="ECO:0007829|PDB:3D59" FT HELIX 274..285 FT /evidence="ECO:0007829|PDB:3D59" FT STRAND 291..296 FT /evidence="ECO:0007829|PDB:3D59" FT HELIX 304..308 FT /evidence="ECO:0007829|PDB:3D59" FT STRAND 314..319 FT /evidence="ECO:0007829|PDB:3D59" FT TURN 320..322 FT /evidence="ECO:0007829|PDB:3D59" FT HELIX 325..332 FT /evidence="ECO:0007829|PDB:3D59" FT STRAND 337..339 FT /evidence="ECO:0007829|PDB:3F96" FT STRAND 341..346 FT /evidence="ECO:0007829|PDB:3D59" FT HELIX 351..354 FT /evidence="ECO:0007829|PDB:3D59" FT HELIX 356..359 FT /evidence="ECO:0007829|PDB:3D59" FT HELIX 363..368 FT /evidence="ECO:0007829|PDB:3D59" FT HELIX 377..396 FT /evidence="ECO:0007829|PDB:3D59" FT HELIX 402..405 FT /evidence="ECO:0007829|PDB:3D59" FT HELIX 406..409 FT /evidence="ECO:0007829|PDB:3D59" FT STRAND 416..419 FT /evidence="ECO:0007829|PDB:3D59" SQ SEQUENCE 441 AA; 50077 MW; 3BA9EEA9E8094A57 CRC64; MVPPKLHVLF CLCGCLAVVY PFDWQYINPV AHMKSSAWVN KIQVLMAAAS FGQTKIPRGN GPYSVGCTDL MFDHTNKGTF LRLYYPSQDN DRLDTLWIPN KEYFWGLSKF LGTHWLMGNI LRLLFGSMTT PANWNSPLRP GEKYPLVVFS HGLGAFRTLY SAIGIDLASH GFIVAAVEHR DRSASATYYF KDQSAAEIGD KSWLYLRTLK QEEETHIRNE QVRQRAKECS QALSLILDID HGKPVKNALD LKFDMEQLKD SIDREKIAVI GHSFGGATVI QTLSEDQRFR CGIALDAWMF PLGDEVYSRI PQPLFFINSE YFQYPANIIK MKKCYSPDKE RKMITIRGSV HQNFADFTFA TGKIIGHMLK LKGDIDSNVA IDLSNKASLA FLQKHLGLHK DFDQWDCLIE GDDENLIPGT NINTTNQHIM LQNSSGIEKY N //