PAFA_BOVIN
ID PAFA_BOVIN Reviewed; 444 AA.
AC Q28017;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Platelet-activating factor acetylhydrolase;
DE Short=PAF acetylhydrolase;
DE EC=3.1.1.47 {ECO:0000250|UniProtKB:Q13093};
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
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).
CC -!- FUNCTION: Lipoprotein-associated calcium-independent phospholipase A2
CC involved in phospholipid catabolism during inflammatory and oxidative
CC stress response (By similarity). At the lipid-aqueous interface,
CC hydrolyzes the ester bond of fatty acyl group attached at sn-2 position
CC of phospholipids (phospholipase A2 activity) (By similarity).
CC Specifically targets phospholipids with a short-chain fatty acyl group
CC at sn-2 position. Can hydrolyze phospholipids with long fatty acyl
CC chains, only if they carry oxidized functional groups (By similarity).
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 (By similarity). 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 (By similarity). As part of high-
CC density lipoprotein (HDL) particles, can hydrolyze phospholipids having
CC long-chain fatty acyl hydroperoxides at sn-2 position and protect
CC against potential accumulation of these oxylipins in the vascular wall
CC (By similarity). Catalyzes the release from membrane phospholipids of
CC F2-isoprostanes, lipid biomarkers of cellular oxidative damage (By
CC similarity). {ECO:0000250|UniProtKB:Q13093}.
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:0000250|UniProtKB:Q13093};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17778;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
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:0000250|UniProtKB:Q13093}. Note=Associates with both LDL and HDL
CC particles in plasma. Mainly associates with pro-inflammatory
CC electronegative LDL particles. {ECO:0000250|UniProtKB:Q13093}.
CC -!- TISSUE SPECIFICITY: Plasma. {ECO:0000250|UniProtKB:Q13093}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q13093}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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; U34247; AAC48483.1; -; mRNA.
DR AlphaFoldDB; Q28017; -.
DR SMR; Q28017; -.
DR STRING; 9913.ENSBTAP00000025719; -.
DR ChEMBL; CHEMBL2441; -.
DR ESTHER; bovin-pafa; PAF-Acetylhydrolase.
DR PaxDb; Q28017; -.
DR PRIDE; Q28017; -.
DR eggNOG; KOG3847; Eukaryota.
DR InParanoid; Q28017; -.
DR Proteomes; UP000009136; Unplaced.
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:0034638; P:phosphatidylcholine catabolic process; ISS:UniProtKB.
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 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 2: Evidence at transcript level;
KW Glycoprotein; HDL; Hydrolase; LDL; 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..444
FT /note="Platelet-activating factor acetylhydrolase"
FT /id="PRO_0000017830"
FT ACT_SITE 274
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 297
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 352
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 444 AA; 50133 MW; 97689917BE2F4C38 CRC64;
MLPSKLHALF CLCTCLALVY PFDWQDLNPV AYIESPAWVS KIQALMAAAN IGQSKIPRGN
GSYSVGCTDL MFDYTNKGTF LRLYYPSQDD DHSDTLWIPN KEYFLGLSKF LGTHWLVGKI
MGLFFGSMTT PAAWNAHLRT GEKYPLIIFS HGLGAFRTIY SAIGIDLASH GFIVAAVEHR
DGSASSTYYF KDQSAVEIGN KSWLYLRTLK RGEEEFPLRN EQLRQRAKEC SQALSLILDI
DHGRPVTNVL DLEFDVEQLK DSIDRDKIAI IGHSFGGATV IQTLSEDQRF RCGIALDAWM
FPVGDEVYSR IPQPLFFINS ERFQYPSNII RMKKCFLPDR ERKMITIRGS VHQNFVDFTF
ATSKIIGYLF TLKGDIDSNV AISLSNKASL AFLQKHLGLQ KDFDQWDSLV EGEDHNLIPG
TNINTTNHQA ILQNSTGIER PNLD
