ID PAFA_MOUSE Reviewed; 440 AA.
AC Q60963; Q8BKM3; Q921T4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 2.
DT 27-MAR-2024, entry version 166.
DE RecName: Full=Platelet-activating factor acetylhydrolase;
DE Short=PAF acetylhydrolase;
DE EC=3.1.1.47 {ECO:0000269|PubMed:10066756, ECO:0000269|PubMed:18434304};
DE AltName: Full=1-alkyl-2-acetylglycerophosphocholine esterase;
DE AltName: Full=2-acetyl-1-alkylglycerophosphocholine esterase;
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Spleen;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [6]
RP FUNCTION AND CATALYTIC ACTIVITY.
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 [7]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=20531249; DOI=10.1203/pdr.0b013e3181eb2efe;
RA Lu J., Pierce M., Franklin A., Jilling T., Stafforini D.M., Caplan M.;
RT "Dual roles of endogenous platelet-activating factor acetylhydrolase in a
RT murine model of necrotizing enterocolitis.";
RL Pediatr. Res. 68:225-230(2010).
CC -!- FUNCTION: Lipoprotein-associated calcium-independent phospholipase A2
CC involved in phospholipid catabolism during inflammatory and oxidative
CC stress response (PubMed:10066756, PubMed:18434304). 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:10066756, PubMed:18434304). Specifically targets phospholipids
CC with a short-chain fatty acyl group at sn-2 position. Can hydrolyze
CC phospholipids with long fatty acyl chains, only if they carry oxidized
CC functional groups (By similarity). Hydrolyzes and inactivates platelet-
CC activating factor (PAF, 1-O-alkyl-2-acetyl-sn-glycero-3-
CC phosphocholine), a potent pro-inflammatory signaling lipid that acts
CC through PTAFR on various innate immune cells (PubMed:10066756,
CC PubMed:18434304). Hydrolyzes oxidatively truncated phospholipids
CC carrying an aldehyde group at omega position, preventing their
CC accumulation in lipoprotein particles and uncontrolled pro-inflammatory
CC effects (By similarity). As part of high-density lipoprotein (HDL)
CC particles, can hydrolyze phospholipids having long-chain fatty acyl
CC hydroperoxides at sn-2 position and protect against potential
CC accumulation of these oxylipins in the vascular wall (By similarity).
CC Catalyzes the release from membrane phospholipids of F2-isoprostanes,
CC lipid biomarkers of cellular oxidative damage (By similarity).
CC {ECO:0000250|UniProtKB:Q13093, ECO:0000269|PubMed:10066756,
CC ECO:0000269|PubMed:18434304}.
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:18434304};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17778;
CC Evidence={ECO:0000305|PubMed:10066756, ECO:0000305|PubMed:18434304};
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:0000250|UniProtKB:Q13093};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41377;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
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:0000250|UniProtKB:Q13093};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41373;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
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:0000250|UniProtKB:Q13093};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41369;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
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:0000250|UniProtKB:Q13093};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40480;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
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:0000250|UniProtKB:Q13093};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41184;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
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:0000250|UniProtKB:Q13093};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41204;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
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:0000250|UniProtKB:Q13093};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41192;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
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:0000250|UniProtKB:Q13093};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41196;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
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:0000250|UniProtKB:Q13093};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41200;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
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:0000250|UniProtKB:Q13093};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41160;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
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:0000250|UniProtKB:Q13093};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40484;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
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:0000250|UniProtKB:Q13093};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41180;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
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:0000250|UniProtKB:Q13093};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41152;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
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:0000250|UniProtKB:Q13093};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41156;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000269|PubMed:18434304}. Note=Associates with HDL particles in
CC plasma. {ECO:0000269|PubMed:18434304}.
CC -!- TISSUE SPECIFICITY: Plasma. {ECO:0000269|PubMed:18434304}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q13093}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice show increased susceptibility to
CC neonatal necrotizing enterocolitis in response to formula feeding,
CC bacterial colonization, and asphyxia/ cold stress.
CC {ECO:0000269|PubMed:20531249}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC52274.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U34277; AAC52274.1; ALT_FRAME; mRNA.
DR EMBL; AK051454; BAC34647.1; -; mRNA.
DR EMBL; CT010585; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466559; EDL23404.1; -; Genomic_DNA.
DR EMBL; CH466559; EDL23406.1; -; Genomic_DNA.
DR EMBL; BC010726; AAH10726.1; -; mRNA.
DR CCDS; CCDS28796.1; -.
DR RefSeq; NP_038765.2; NM_013737.5.
DR RefSeq; XP_006524428.1; XM_006524365.3.
DR RefSeq; XP_006524429.1; XM_006524366.3.
DR AlphaFoldDB; Q60963; -.
DR SMR; Q60963; -.
DR BioGRID; 205147; 4.
DR IntAct; Q60963; 2.
DR STRING; 10090.ENSMUSP00000024706; -.
DR BindingDB; Q60963; -.
DR ChEMBL; CHEMBL5383; -.
DR ESTHER; mouse-pafa; PAF-Acetylhydrolase.
DR GlyCosmos; Q60963; 3 sites, No reported glycans.
DR GlyGen; Q60963; 3 sites.
DR iPTMnet; Q60963; -.
DR MetOSite; Q60963; -.
DR PhosphoSitePlus; Q60963; -.
DR CPTAC; non-CPTAC-3928; -.
DR MaxQB; Q60963; -.
DR PaxDb; 10090-ENSMUSP00000024706; -.
DR PeptideAtlas; Q60963; -.
DR ProteomicsDB; 293996; -.
DR Antibodypedia; 30742; 426 antibodies from 31 providers.
DR DNASU; 27226; -.
DR Ensembl; ENSMUST00000024706.12; ENSMUSP00000024706.6; ENSMUSG00000023913.18.
DR GeneID; 27226; -.
DR KEGG; mmu:27226; -.
DR UCSC; uc008cpd.1; mouse.
DR AGR; MGI:1351327; -.
DR CTD; 7941; -.
DR MGI; MGI:1351327; Pla2g7.
DR VEuPathDB; HostDB:ENSMUSG00000023913; -.
DR eggNOG; KOG3847; Eukaryota.
DR GeneTree; ENSGT00390000005233; -.
DR HOGENOM; CLU_022501_0_1_1; -.
DR InParanoid; Q60963; -.
DR OMA; GSVHHNF; -.
DR OrthoDB; 3079661at2759; -.
DR PhylomeDB; Q60963; -.
DR TreeFam; TF313831; -.
DR Reactome; R-MMU-422085; Synthesis, secretion, and deacylation of Ghrelin.
DR BioGRID-ORCS; 27226; 4 hits in 80 CRISPR screens.
DR ChiTaRS; Pla2g7; mouse.
DR PRO; PR:Q60963; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q60963; Protein.
DR Bgee; ENSMUSG00000023913; Expressed in stroma of bone marrow and 253 other cell types or tissues.
DR ExpressionAtlas; Q60963; baseline and differential.
DR Genevisible; Q60963; MM.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0034364; C:high-density lipoprotein particle; ISS:UniProtKB.
DR GO; GO:0034362; C:low-density lipoprotein particle; ISS:UniProtKB.
DR GO; GO:0003847; F:1-alkyl-2-acetylglycerophosphocholine esterase activity; ISS:UniProtKB.
DR GO; GO:0047499; F:calcium-independent phospholipase A2 activity; ISS:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; ISO:MGI.
DR GO; GO:0006954; P:inflammatory response; TAS:MGI.
DR GO; GO:0034440; P:lipid oxidation; ISO:MGI.
DR GO; GO:0034374; P:low-density lipoprotein particle remodeling; ISO:MGI.
DR GO; GO:0034638; P:phosphatidylcholine catabolic process; ISS:UniProtKB.
DR GO; GO:0034441; P:plasma lipoprotein particle oxidation; ISO:MGI.
DR GO; GO:0062234; P:platelet activating factor catabolic process; ISS:UniProtKB.
DR GO; GO:0046469; P:platelet activating factor metabolic process; ISS:UniProtKB.
DR GO; GO:0090026; P:positive regulation of monocyte chemotaxis; ISO:MGI.
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.
PE 1: Evidence at protein level;
KW Glycoprotein; HDL; Hydrolase; Lipid degradation; Lipid metabolism;
KW Phospholipid degradation; Phospholipid metabolism; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000250"
FT CHAIN 22..440
FT /note="Platelet-activating factor acetylhydrolase"
FT /id="PRO_0000017834"
FT ACT_SITE 272
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 295
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 350
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 427
FT /note="V -> A (in Ref. 3; EDL23404/EDL23406 and 4;
FT AAH10726)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 440 AA; 49258 MW; 17C8B4D28F1ADC94 CRC64;
MVPLKLQALF CLLCCLPWVH PFHWQDTSSF DFRPSVMFHK LQSVMSAAGS GHSKIPKGNG
SYPVGCTDLM FGYGNESVFV RLYYPAQDQG RLDTVWIPNK EYFLGLSIFL GTPSIVGNIL
HLLYGSLTTP ASWNSPLRTG EKYPLIVFSH GLGAFRTIYS AIGIGLASNG FIVATVEHRD
RSASATYFFE DQVAAKVENR SWLYLRKVKQ EESESVRKEQ VQQRAIECSR ALSAILDIEH
GDPKENVLGS AFDMKQLKDA IDETKIALMG HSFGGATVLQ ALSEDQRFRC GVALDPWMYP
VNEELYSRTL QPLLFINSAK FQTPKDIAKM KKFYQPDKER KMITIKGSVH QNFDDFTFVT
GKIIGNKLTL KGEIDSRVAI DLTNKASMAF LQKHLGLQKD FDQWDPLVEG DDENLIPGSP
FDAVTQVPAQ QHSPGSQTQN
//
