PAFA2_RAT
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 03-AUG-2022, entry version 117.
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 = 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:0000269|PubMed:10085103};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17778;
CC Evidence={ECO:0000305|PubMed:10085103};
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-(1Z-alkenyl)-sn-glycero-3-phosphoethanolamine + 1-O-
CC hexadecyl-2-acetyl-sn-glycero-3-phosphocholine = 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 + H(+) + N-
CC (acetyl)-sphing-4-enine; 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=1-organyl-2-lyso-sn-glycero-3-phospholipid + a 1-O-alkyl-2-
CC acetyl-sn-glycero-3-phosphocholine = 1-O-alkyl-sn-glycero-3-
CC phosphocholine + 1-organyl-2-acetyl-sn-glycero-3-phospholipid;
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 + H(+) + succinate;
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 + H(+) + propanoate;
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 1-O-(1Z-alkenyl)-sn-glycero-3-
CC phosphoethanolamine {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_006239127.3.
DR RefSeq; XP_017448893.1; XM_017593404.1.
DR AlphaFoldDB; P83006; -.
DR SMR; P83006; -.
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; P83006; -.
DR PRIDE; P83006; -.
DR GeneID; 313611; -.
DR KEGG; rno:313611; -.
DR UCSC; RGD:631399; rat.
DR CTD; 5051; -.
DR RGD; 631399; Pafah2.
DR eggNOG; KOG3847; Eukaryota.
DR HOGENOM; CLU_022501_0_0_1; -.
DR InParanoid; P83006; -.
DR OMA; GNWIGKF; -.
DR OrthoDB; 1189747at2759; -.
DR PhylomeDB; P83006; -.
DR TreeFam; TF313831; -.
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 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; IEA:UniProtKB-SubCell.
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:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
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 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
