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   27-MAR-2024, entry version 122.
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   GlyCosmos; Q28262; 3 sites, No reported glycans.
DR   PaxDb; 9612-ENSCAFP00000030617; -.
DR   Ensembl; ENSCAFT00030011773.1; ENSCAFP00030010312.1; ENSCAFG00030006390.1.
DR   Ensembl; ENSCAFT00805027835; ENSCAFP00805021857; ENSCAFG00805015251.
DR   GeneID; 403848; -.
DR   KEGG; cfa:403848; -.
DR   CTD; 7941; -.
DR   eggNOG; KOG3847; Eukaryota.
DR   InParanoid; Q28262; -.
DR   OrthoDB; 3079661at2759; -.
DR   Proteomes; UP000002254; Unplaced.
DR   Proteomes; UP000694429; Chromosome 12.
DR   Proteomes; UP000694542; Unplaced.
DR   Proteomes; UP000805418; 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; 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   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
//