ID   PAFA_CHICK              Reviewed;         422 AA.
AC   Q90678;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Platelet-activating factor acetylhydrolase;
DE            Short=PAF acetylhydrolase;
DE            EC=3.1.1.47;
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   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
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: Modulates the action of platelet-activating factor (PAF) by
CC       hydrolyzing the sn-2 ester bond to yield the biologically inactive
CC       lyso-PAF. Has a specificity for substrates with a short residue at the
CC       sn-2 position. It is inactive against long-chain phospholipids.
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   -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC   -!- TISSUE SPECIFICITY: Plasma.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
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DR   EMBL; U34278; AAC59717.1; -; mRNA.
DR   RefSeq; NP_990300.1; NM_204969.1.
DR   AlphaFoldDB; Q90678; -.
DR   SMR; Q90678; -.
DR   STRING; 9031.ENSGALP00000026919; -.
DR   ESTHER; chick-pafa; PAF-Acetylhydrolase.
DR   PaxDb; Q90678; -.
DR   GeneID; 395816; -.
DR   KEGG; gga:395816; -.
DR   CTD; 7941; -.
DR   VEuPathDB; HostDB:geneid_395816; -.
DR   eggNOG; KOG3847; Eukaryota.
DR   InParanoid; Q90678; -.
DR   OrthoDB; 1189747at2759; -.
DR   PhylomeDB; Q90678; -.
DR   PRO; PR:Q90678; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0003847; F:1-alkyl-2-acetylglycerophosphocholine esterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000250"
FT   CHAIN           22..422
FT                   /note="Platelet-activating factor acetylhydrolase"
FT                   /id="PRO_0000017835"
FT   ACT_SITE        266
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        289
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   ACT_SITE        345
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   CARBOHYD        331
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   422 AA;  47046 MW;  15A5C794376E9141 CRC64;
     MASLWVRARR VFMKSRASGF SAKAATEMGS GGAEKGYRIP AGKGPHAVGC TDLMTGDAAE
     GSFLRLYYLS CDDTDTEETP WIPDKEYYQG LSDFLNVYRA LGERLFQYYV GSVTCPAKSN
     AAFKPGEKYP LLVFSHGLGA FRTIYSAICI EMASQGFLVA AVEHRDESAS ATYFCKKKAD
     SEPEEDQTSG VEKEWIYYRK LRAGEEERCL RHKQVQQRAQ ECIKALNLIL KISSGEEVMN
     VLNSDFDWNH LKDSVDTSRI AVMGHSFGGA TVIESLSKEI RFRCGIALDA WMLPVGDDTY
     QSSVQQPLLF INSEKFQWAA NILKMKKLSS NDTNKKMITI KGSVHQSFPD FTFVSGEIIG
     KFFKLKGEID PNEAIDICNH ASLAFLQKHL SLKRDFDKWD SLVDGIGPNV ISGTNIDLSP
     TE