PAFA_HUMAN
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 03-AUG-2022, entry version 194.
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, AND INVOLVEMENT IN ASTHMA AND ATOPY.
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 1-hexadecanoyl-2-(5-oxopentanoyl)-sn-glycero-3-
CC phosphocholine {ECO:0000269|PubMed:2040620};
CC KM=15.5 uM for 1-hexadecanoyl-2-(9-oxononanoyl)-sn-glycero-3-
CC phosphocholine {ECO:0000269|PubMed:2040620};
CC KM=43.1 uM for 1-hexadecanoyl-2-(5-oxopentanoyl)-sn-glycero-3-
CC phosphocholine {ECO:0000269|PubMed:16371369};
CC Vmax=167 umol/h/mg enzyme toward 1-hexadecanoyl-2-acetyl-sn-glycero-
CC 3-phosphocholine {ECO:0000269|PubMed:2040620};
CC Vmax=36.1 umol/h/mg enzyme toward 1-hexadecanoyl-2-propionyl-sn-
CC glycero-3-phosphocholine {ECO:0000269|PubMed:2040620};
CC Vmax=43.4 umol/h/mg enzyme toward 1-hexadecanoyl-2-butanoyl-sn-
CC glycero-3-phosphocholine {ECO:0000269|PubMed:2040620};
CC Vmax=42.2 umol/h/mg enzyme toward 1-hexadecanoyl-2-pentanoyl-sn-
CC glycero-3-phosphocholine {ECO:0000269|PubMed:2040620};
CC Vmax=100 umol/h/mg enzyme toward 1-hexadecanoyl-2-(5-oxopentanoyl)-
CC sn-glycero-3-phosphocholine {ECO:0000269|PubMed:2040620};
CC Vmax=98.4 umol/h/mg enzyme toward 1-hexadecanoyl-2-(9-oxononanoyl)-
CC sn-glycero-3-phosphocholine {ECO:0000269|PubMed:2040620};
CC Vmax=5.0 umol/min/mg enzyme toward 1-hexadecanoyl-2-(5-oxopentanoyl)-
CC sn-glycero-3-phosphocholine {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 -!- DISEASE: Asthma (ASTHMA) [MIM:600807]: The most common chronic disease
CC affecting children and young adults. It is a complex genetic disorder
CC with a heterogeneous phenotype, largely attributed to the interactions
CC among many genes and between these genes and the environment. It is
CC characterized by recurrent attacks of paroxysmal dyspnea, with wheezing
CC due to spasmodic contraction of the bronchi.
CC {ECO:0000269|PubMed:10733466}. Note=Disease susceptibility is
CC associated with variants affecting the gene represented in this entry.
CC -!- DISEASE: Atopic hypersensitivity (ATOPY) [MIM:147050]: A condition
CC characterized by predisposition to develop hypersensitivity reactions.
CC Atopic individuals can develop eczema, allergic rhinitis and allergic
CC asthma. {ECO:0000269|PubMed:10733466}. Note=Disease susceptibility is
CC associated with variants affecting the gene represented in this 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 ---------------------------------------------------------------------------
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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 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; Q13093; -.
DR PeptideAtlas; Q13093; -.
DR PRIDE; Q13093; -.
DR ProteomicsDB; 59145; -.
DR Antibodypedia; 30742; 366 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 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; 147050; phenotype.
DR MIM; 600807; phenotype.
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; TYYFQDQ; -.
DR OrthoDB; 683132at2759; -.
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 BioGRID-ORCS; 7941; 16 hits in 1068 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 tissues.
DR Genevisible; Q13093; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
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; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR005065; PAF_acetylhydro-like.
DR InterPro; IPR016715; PAF_acetylhydro_eucaryote.
DR PANTHER; PTHR10272; PTHR10272; 1.
DR Pfam; PF03403; PAF-AH_p_II; 1.
DR PIRSF; PIRSF018169; PAF_acetylhydrolase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
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 (associated with asthma and atopy; retains
FT the ability to associate with HDL particles;
FT 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
