PAFA_CANLF
ID PAFA_CANLF Reviewed; 444 AA.
AC Q28262;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 113.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
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}.
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DR EMBL; U34246; AAC48484.1; -; mRNA.
DR RefSeq; NP_001003198.1; NM_001003198.1.
DR AlphaFoldDB; Q28262; -.
DR SMR; Q28262; -.
DR STRING; 9615.ENSCAFP00000058629; -.
DR ESTHER; canfa-pafa; PAF-Acetylhydrolase.
DR PaxDb; Q28262; -.
DR PRIDE; Q28262; -.
DR Ensembl; ENSCAFT00030011773; ENSCAFP00030010312; ENSCAFG00030006390.
DR GeneID; 403848; -.
DR KEGG; cfa:403848; -.
DR CTD; 7941; -.
DR eggNOG; KOG3847; Eukaryota.
DR InParanoid; Q28262; -.
DR OrthoDB; 1189747at2759; -.
DR Reactome; R-CFA-422085; Synthesis, secretion, and deacylation of Ghrelin.
DR Proteomes; UP000002254; 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_0000017831"
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"
SQ SEQUENCE 444 AA; 50136 MW; 814EF0AE38B074AC CRC64;
MLPPKLHALF CLCSCLTLVH PIDWQDLNPV AHIRSSAWAN KIQALMAAAS IRQSRIPKGN
GSYSVGCTDL MFDYTNKGTF LRLYYPSQED DHSDTLWIPN KEYFFGLSKY LGTPWLMGKI
LSFFFGSVTT PANWNSPLRT GEKYPLIVFS HGLGAFRTIY SAIGIDLASH GFIVAAIEHR
DGSASATYYF KDQSAAEIGN KSWSYLQELK PGDEEIHVRN EQVQKRAKEC SQALNLILDI
DHGRPIKNVL DLEFDVEQLK DSIDRDKIAV IGHSFGGATV LQALSEDQRF RCGIALDAWM
LPLDDAIYSR IPQPLFFINS ERFQFPENIK KMKKCYSPDK ERKMITIRGS VHQNFADFTF
TTGKIVGYIF TLKGDIDSNV AIDLCNKASL AFLQKHLGLR KDFDQWDSLI EGKDENLMPG
TNINITNEHD TLQNSPEAEK SNLD
