ID   PAFA2_RAT               Reviewed;         390 AA.
AC   P83006; Q80Z89;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   31-AUG-2004, sequence version 2.
DT   02-SEP-2026, entry version 129.
DE   RecName: Full=Platelet-activating factor acetylhydrolase 2, cytoplasmic {ECO:0000303|PubMed:10085103};
DE            EC=3.1.1.47 {ECO:0000269|PubMed:10085103};
DE   AltName: Full=PAF:lysophospholipid transacetylase {ECO:0000303|PubMed:10085103};
DE   AltName: Full=PAF:sphingosine transacetylase {ECO:0000303|PubMed:10085103};
DE   AltName: Full=Platelet-activating factor acetyltransferase PAFAH2 {ECO:0000305};
DE            EC=2.3.1.149 {ECO:0000269|PubMed:10085103};
DE   AltName: Full=Serine-dependent phospholipase A2 {ECO:0000250|UniProtKB:Q99487};
DE            Short=SD-PLA2 {ECO:0000305};
GN   Name=Pafah2 {ECO:0000312|RGD:631399};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000305};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar; TISSUE=Brain;
RA   Bonin F., Moffat T.C., Renaud N., Franks D.J., Bennett S.A.L.;
RT   "Kinetics of platelet-activating factor binding, internalization,
RT   degradation, and apoptotic signaling in neural precursors.";
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 84-96; 169-179 AND 329-357, FUNCTION, CATALYTIC
RP   ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=Sprague-Dawley; TISSUE=Kidney;
RX   PubMed=10085103; DOI=10.1074/jbc.274.13.8655;
RA   Karasawa K., Qiu X., Lee T.-C.;
RT   "Purification and characterization from rat kidney membranes of a novel
RT   platelet-activating factor (PAF)-dependent transacetylase that catalyzes
RT   the hydrolysis of PAF, formation of PAF analogs, and C2-ceramide.";
RL   J. Biol. Chem. 274:8655-8661(1999).
CC   -!- FUNCTION: Catalyzes the hydrolyze of the acetyl group at the sn-2
CC       position of platelet-activating factor (PAF) and its analogs, leading
CC       to their inactivation (PubMed:10085103). Hydrolyzes propionyl and
CC       butyroyl moieties approximately half as effectively as PAF (By
CC       similarity). Also catalyzes transacetylation of the acetyl group from
CC       platelet-activating factor (PAF) to lysoplasmalogen and to sphingosine,
CC       producing plasmalogen analogs of PAF and N-acetylsphingosine (C2-
CC       ceramide) respectively (PubMed:10085103). Has a marked selectivity for
CC       phospholipids with short acyl chains at the sn-2 position
CC       (PubMed:10085103). {ECO:0000250|UniProtKB:P79106,
CC       ECO:0000269|PubMed:10085103}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = a 1-
CC         O-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:10085103};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17778;
CC         Evidence={ECO:0000305|PubMed:10085103};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-O-alkyl-2-acyl-sn-glycero-3-phosphocholine + H2O = a 1-O-
CC         alkyl-sn-glycero-3-phosphocholine + a fatty acid + H(+);
CC         Xref=Rhea:RHEA:36231, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28868, ChEBI:CHEBI:30909, ChEBI:CHEBI:36702;
CC         Evidence={ECO:0000250|UniProtKB:P79106};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36232;
CC         Evidence={ECO:0000250|UniProtKB:P79106};
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:0000269|PubMed:10085103};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40480;
CC         Evidence={ECO:0000305|PubMed:10085103};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphocholine + a 1-O-
CC         (1Z-alkenyl)-sn-glycero-3-phosphoethanolamine = 1-O-(1Z-alkenyl)-2-
CC         acetyl-sn-glycero-3-phosphoethanolamine + 1-O-hexadecyl-sn-glycero-3-
CC         phosphocholine; Xref=Rhea:RHEA:41396, ChEBI:CHEBI:44811,
CC         ChEBI:CHEBI:64496, ChEBI:CHEBI:77288, ChEBI:CHEBI:78419;
CC         Evidence={ECO:0000269|PubMed:10085103};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41397;
CC         Evidence={ECO:0000305|PubMed:10085103};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphocholine + sphing-4-
CC         enine = 1-O-hexadecyl-sn-glycero-3-phosphocholine + N-(acetyl)-
CC         sphing-4-enine + H(+); Xref=Rhea:RHEA:41408, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:44811, ChEBI:CHEBI:46979, ChEBI:CHEBI:57756,
CC         ChEBI:CHEBI:64496; Evidence={ECO:0000269|PubMed:10085103};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41409;
CC         Evidence={ECO:0000305|PubMed:10085103};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-organyl-2-lyso-sn-glycero-3-phospholipid + a 1-O-alkyl-2-
CC         acetyl-sn-glycero-3-phosphocholine = a 1-organyl-2-acetyl-sn-glycero-
CC         3-phospholipid + a 1-O-alkyl-sn-glycero-3-phosphocholine;
CC         Xref=Rhea:RHEA:11048, ChEBI:CHEBI:685, ChEBI:CHEBI:30909,
CC         ChEBI:CHEBI:36707, ChEBI:CHEBI:76590; EC=2.3.1.149;
CC         Evidence={ECO:0000269|PubMed:10085103};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11049;
CC         Evidence={ECO:0000305|PubMed:10085103};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-O-hexadecyl-2-glutaryl-sn-glycero-3-phosphocholine + H2O =
CC         1-O-hexadecyl-sn-glycero-3-phosphocholine + glutarate + H(+);
CC         Xref=Rhea:RHEA:41700, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30921, ChEBI:CHEBI:64496, ChEBI:CHEBI:78371;
CC         Evidence={ECO:0000250|UniProtKB:P79106};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41701;
CC         Evidence={ECO:0000250|UniProtKB:P79106};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-O-hexadecyl-2-succinyl-sn-glycero-3-phosphocholine + H2O =
CC         1-O-hexadecyl-sn-glycero-3-phosphocholine + succinate + H(+);
CC         Xref=Rhea:RHEA:41696, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:64496, ChEBI:CHEBI:78369;
CC         Evidence={ECO:0000250|UniProtKB:P79106};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41697;
CC         Evidence={ECO:0000250|UniProtKB:P79106};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-O-hexadecyl-2-butanoyl-sn-glycero-3-phosphocholine + H2O =
CC         1-O-hexadecyl-sn-glycero-3-phosphocholine + butanoate + H(+);
CC         Xref=Rhea:RHEA:41692, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17968, ChEBI:CHEBI:64496, ChEBI:CHEBI:78368;
CC         Evidence={ECO:0000250|UniProtKB:P79106};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41693;
CC         Evidence={ECO:0000250|UniProtKB:P79106};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-O-hexadecyl-2-propanoyl-sn-glycero-3-phosphocholine + H2O =
CC         1-O-hexadecyl-sn-glycero-3-phosphocholine + propanoate + H(+);
CC         Xref=Rhea:RHEA:41688, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17272, ChEBI:CHEBI:64496, ChEBI:CHEBI:78367;
CC         Evidence={ECO:0000250|UniProtKB:P79106};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41689;
CC         Evidence={ECO:0000250|UniProtKB:P79106};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=227 uM for 1-O-(1Z-alkenyl)-sn-glycero-3-phosphoethanolamine
CC         {ECO:0000269|PubMed:10085103};
CC         KM=4.1 uM for sphing-4-enine {ECO:0000269|PubMed:10085103};
CC         Vmax=81 umol/min/mg enzyme toward
CC         1-O-(1Z-alkenyl)-sn-glycero-3-phosphoethanolamine
CC         {ECO:0000269|PubMed:10085103};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10085103}.
CC   -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000269|PubMed:10085103};
CC       Lipid-anchor {ECO:0000250|UniProtKB:P79106}. Mitochondrion membrane
CC       {ECO:0000269|PubMed:10085103}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P79106}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P79106}. Endoplasmic reticulum membrane
CC       {ECO:0000305|PubMed:10085103}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P79106}. Note=In resting cells, localizes to
CC       intracellular membranes and cytoplasm. Translocates from the cytoplasm
CC       to intracellular membranes upon oxidative stress.
CC       {ECO:0000250|UniProtKB:P79106}.
CC   -!- TISSUE SPECIFICITY: Expressed in kidney. {ECO:0000269|PubMed:10085103}.
CC   -!- SIMILARITY: Belongs to the serine esterase family. {ECO:0000305}.
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DR   EMBL; AY225592; AAO62314.1; -; mRNA.
DR   RefSeq; NP_808793.1; NM_177932.2.
DR   RefSeq; XP_006239189.1; XM_006239127.5.
DR   RefSeq; XP_017448893.1; XM_017593404.3.
DR   RefSeq; XP_038965969.1; XM_039110041.2.
DR   AlphaFoldDB; P83006; -.
DR   SMR; P83006; -.
DR   FunCoup; P83006; 462.
DR   STRING; 10116.ENSRNOP00000034439; -.
DR   SwissLipids; SLP:000000697; -.
DR   ESTHER; ratno-paf2; PAF-Acetylhydrolase.
DR   iPTMnet; P83006; -.
DR   PhosphoSitePlus; P83006; -.
DR   jPOST; P83006; -.
DR   PaxDb; 10116-ENSRNOP00000034439; -.
DR   Ensembl; ENSRNOT00000166584.1; ENSRNOP00000103411.1; ENSRNOG00000022288.4.
DR   GeneID; 313611; -.
DR   KEGG; rno:313611; -.
DR   UCSC; RGD:631399; rat.
DR   AGR; RGD:631399; -.
DR   CTD; 5051; -.
DR   RGD; 631399; Pafah2.
DR   eggNOG; KOG3847; Eukaryota.
DR   GeneTree; ENSGT00390000005233; -.
DR   HOGENOM; CLU_022501_0_0_1; -.
DR   InParanoid; P83006; -.
DR   OrthoDB; 15950at9989; -.
DR   PhylomeDB; P83006; -.
DR   BRENDA; 3.1.1.47; 5301.
DR   Reactome; R-RNO-418346; Platelet homeostasis.
DR   PRO; PR:P83006; -.
DR   Proteomes; UP000002494; Chromosome 5.
DR   Bgee; ENSRNOG00000022288; Expressed in lung and 18 other cell types or tissues.
DR   ExpressionAtlas; P83006; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031966; C:mitochondrial membrane; EXP:UniProtKB.
DR   GO; GO:0003847; F:1-alkyl-2-acetylglycerophosphocholine esterase activity; IDA:UniProtKB.
DR   GO; GO:0047179; F:platelet-activating factor acetyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR   FunFam; 3.40.50.1820:FF:000062; Platelet-activating factor acetylhydrolase; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase_fold.
DR   InterPro; IPR016715; PAF_acetylhydro_eukaryote.
DR   PANTHER; PTHR10272; PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE; 1.
DR   PANTHER; PTHR10272:SF6; PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE 2, CYTOPLASMIC; 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   Cytoplasm; Direct protein sequencing; Endoplasmic reticulum; Hydrolase;
KW   Lipid degradation; Lipid metabolism; Lipoprotein; Membrane; Microsome;
KW   Mitochondrion; Myristate; Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..390
FT                   /note="Platelet-activating factor acetylhydrolase 2,
FT                   cytoplasmic"
FT                   /id="PRO_0000090385"
FT   ACT_SITE        234
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P79106"
FT   ACT_SITE        257
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   ACT_SITE        312
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000250|UniProtKB:P79106"
FT   CONFLICT        84
FT                   /note="R -> L (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        95
FT                   /note="T -> K (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   390 AA;  43492 MW;  313FAC9553416373 CRC64;
     MGAGQSICFP PISGPHHIGC TDVMEGHSLE GSLFRLFYPC EASETCEQPL WIPRYEYCVG
     LADYLQYNKR WVGLLFNVGI GSCRLPVSWN GPFKTKESGY PLIILSHGLG GFRVSYSAFC
     MELASRGFVV AAIEHRDQSA AATYFCKQTS QESSPTESLE EEWIPFRRIK EGEKEFHVRN
     PQVHQRAKEC VRVLQILQDA SAGKPVINVF PGGLDLMTLK GSIDMSRVAV MGHSFGGATA
     ILALTQEAQF RCAIALDAWM FPLEHDFYPK ARGPVFFINV EKFQTVESVN LMKKICAQHE
     QSRIVTVLGA VHRSQTDFAF VTGNMIGKLF SSGTRGTLDP YEGQEVMVRA MLAFLQKHLD
     LKEDYDQWNS FIEGIGPSLI QGAPHYLSSL
//