PAFA2_MOUSE
ID PAFA2_MOUSE Reviewed; 390 AA.
AC Q8VDG7; E9QNW7; Q8R0Y7;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Platelet-activating factor acetylhydrolase 2, cytoplasmic {ECO:0000250|UniProtKB:P79106};
DE EC=3.1.1.47 {ECO:0000250|UniProtKB:P83006};
DE AltName: Full=PAF:lysophospholipid transacetylase {ECO:0000250|UniProtKB:P83006};
DE AltName: Full=PAF:sphingosine transacetylase {ECO:0000250|UniProtKB:P83006};
DE AltName: Full=Platelet-activating factor acetyltransferase PAFAH2 {ECO:0000250|UniProtKB:P83006};
DE EC=2.3.1.149 {ECO:0000250|UniProtKB:P83006};
DE AltName: Full=Serine-dependent phospholipase A2 {ECO:0000250|UniProtKB:Q99487};
DE Short=SD-PLA2 {ECO:0000305};
GN Name=Pafah2 {ECO:0000312|MGI:MGI:2140321};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver, and Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity). 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. Has a marked selectivity for phospholipids with
CC short acyl chains at the sn-2 position (By similarity).
CC {ECO:0000250|UniProtKB:P79106, ECO:0000250|UniProtKB:P83006}.
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:P83006};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17778;
CC Evidence={ECO:0000250|UniProtKB:P83006};
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:P83006};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40480;
CC Evidence={ECO:0000250|UniProtKB:P83006};
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:0000250|UniProtKB:P83006};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41397;
CC Evidence={ECO:0000250|UniProtKB:P83006};
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:0000250|UniProtKB:P83006};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41409;
CC Evidence={ECO:0000250|UniProtKB:P83006};
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:0000250|UniProtKB:P83006};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11049;
CC Evidence={ECO:0000250|UniProtKB:P83006};
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 -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P79106}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P79106}.
CC Membrane {ECO:0000250|UniProtKB:P79106}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P79106}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P79106}; 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 -!- SIMILARITY: Belongs to the serine esterase family. {ECO:0000305}.
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DR EMBL; AL669982; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC021890; AAH21890.1; -; mRNA.
DR EMBL; BC025495; AAH25495.1; -; mRNA.
DR EMBL; BC025938; AAH25938.1; -; mRNA.
DR CCDS; CCDS18771.1; -.
DR RefSeq; NP_001272803.1; NM_001285874.1.
DR RefSeq; NP_598641.2; NM_133880.3.
DR RefSeq; XP_006538518.1; XM_006538455.2.
DR RefSeq; XP_011248473.1; XM_011250171.2.
DR RefSeq; XP_017175376.1; XM_017319887.1.
DR AlphaFoldDB; Q8VDG7; -.
DR SMR; Q8VDG7; -.
DR STRING; 10090.ENSMUSP00000101495; -.
DR ChEMBL; CHEMBL1795095; -.
DR ESTHER; mouse-paf2; PAF-Acetylhydrolase.
DR PhosphoSitePlus; Q8VDG7; -.
DR EPD; Q8VDG7; -.
DR jPOST; Q8VDG7; -.
DR MaxQB; Q8VDG7; -.
DR PaxDb; Q8VDG7; -.
DR PRIDE; Q8VDG7; -.
DR ProteomicsDB; 294150; -.
DR Antibodypedia; 622; 143 antibodies from 22 providers.
DR DNASU; 100163; -.
DR Ensembl; ENSMUST00000105869; ENSMUSP00000101495; ENSMUSG00000037366.
DR GeneID; 100163; -.
DR KEGG; mmu:100163; -.
DR UCSC; uc008vey.3; mouse.
DR CTD; 5051; -.
DR MGI; MGI:2140321; Pafah2.
DR VEuPathDB; HostDB:ENSMUSG00000037366; -.
DR eggNOG; KOG3847; Eukaryota.
DR GeneTree; ENSGT00390000005233; -.
DR HOGENOM; CLU_022501_0_0_1; -.
DR InParanoid; Q8VDG7; -.
DR TreeFam; TF313831; -.
DR BRENDA; 3.1.1.47; 3474.
DR Reactome; R-MMU-418346; Platelet homeostasis.
DR BioGRID-ORCS; 100163; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Pafah2; mouse.
DR PRO; PR:Q8VDG7; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8VDG7; protein.
DR Bgee; ENSMUSG00000037366; Expressed in left lobe of liver and 196 other tissues.
DR ExpressionAtlas; Q8VDG7; baseline and differential.
DR Genevisible; Q8VDG7; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003847; F:1-alkyl-2-acetylglycerophosphocholine esterase activity; ISS:UniProtKB.
DR GO; GO:0047179; F:platelet-activating factor acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
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; Endoplasmic reticulum; Hydrolase; Lipid degradation;
KW Lipid metabolism; Lipoprotein; Membrane; Myristate; Reference proteome;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..390
FT /note="Platelet-activating factor acetylhydrolase 2,
FT cytoplasmic"
FT /id="PRO_0000090384"
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 223..226
FT /note="IDRN -> VDTS (in Ref. 2; AAH21890/AAH25495/
FT AAH25938)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 390 AA; 43562 MW; 28AE6D00A25ED029 CRC64;
MGAGQSVCFP PISGPHHIGC TDVMEGHSLE GSLFRLFYPC QASEKCEQPL WIPRYEYSMG
LADYLQYNKR WVGLLFNVGI GSCRLPVSWN GPFKAKESGY PLIILSHGLG GFRASYSAFC
MELASRGFVV AAVEHRDQSA AATYFCKPTS QESSPAESLE EEWLPFRRIK EGEKEFHVRN
PQVHQRVKEC VRVLRILQDA SAGKTVVNVF PGGLDLMTLK GSIDRNRVAV MGHSFGGATA
VLALTQEVQF RCAIALDAWM FPLERDFYPK ARGPVFFINV EKFQTVESVN LMKKICAQHE
QSRIVTVLGA VHRSQTDFAF VTGNLIAKFF SSNSRGTLDP YESQEVMVRA ILAFLQKHLD
LKEDYDQWSS FIEGVGPSLI QGAPHYLSSL
