Detail Information for IndEnz0010001380
IED ID IndEnz0010001380
Enzyme Type ID esterase001380
Protein Name Platelet-activating factor acetylhydrolase 2, cytoplasmic
EC 3.1.1.47
PAF:lysophospholipid transacetylase
PAF:sphingosine transacetylase
Platelet-activating factor acetyltransferase PAFAH2
EC 2.3.1.149
Serine-dependent phospholipase A2
SD-PLA2
Gene Name Pafah2
Organism Mus musculus (Mouse)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse)
Enzyme Sequence MGAGQSVCFPPISGPHHIGCTDVMEGHSLEGSLFRLFYPCQASEKCEQPLWIPRYEYSMGLADYLQYNKRWVGLLFNVGIGSCRLPVSWNGPFKAKESGYPLIILSHGLGGFRASYSAFCMELASRGFVVAAVEHRDQSAAATYFCKPTSQESSPAESLEEEWLPFRRIKEGEKEFHVRNPQVHQRVKECVRVLRILQDASAGKTVVNVFPGGLDLMTLKGSIDRNRVAVMGHSFGGATAVLALTQEVQFRCAIALDAWMFPLERDFYPKARGPVFFINVEKFQTVESVNLMKKICAQHEQSRIVTVLGAVHRSQTDFAFVTGNLIAKFFSSNSRGTLDPYESQEVMVRAILAFLQKHLDLKEDYDQWSSFIEGVGPSLIQGAPHYLSSL
Enzyme Length 390
Uniprot Accession Number Q8VDG7
Absorption
Active Site ACT_SITE 234; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P79106; ACT_SITE 257; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037; ACT_SITE 312; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-alkyl-sn-glycero-3-phosphocholine + acetate + H(+); Xref=Rhea:RHEA:17777, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:30909, ChEBI:CHEBI:36707; EC=3.1.1.47; Evidence={ECO:0000250|UniProtKB:P83006};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17778; Evidence={ECO:0000250|UniProtKB:P83006}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-hexadecyl-sn-glycero-3-phosphocholine + acetate + H(+); Xref=Rhea:RHEA:40479, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:44811, ChEBI:CHEBI:64496; Evidence={ECO:0000250|UniProtKB:P83006};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40480; Evidence={ECO:0000250|UniProtKB:P83006}; CATALYTIC ACTIVITY: Reaction=1-O-(1Z-alkenyl)-sn-glycero-3-phosphoethanolamine + 1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphocholine = 1-O-(1Z-alkenyl)-2-acetyl-sn-glycero-3-phosphoethanolamine + 1-O-hexadecyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:41396, ChEBI:CHEBI:44811, ChEBI:CHEBI:64496, ChEBI:CHEBI:77288, ChEBI:CHEBI:78419; Evidence={ECO:0000250|UniProtKB:P83006};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41397; Evidence={ECO:0000250|UniProtKB:P83006}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphocholine + sphing-4-enine = 1-O-hexadecyl-sn-glycero-3-phosphocholine + H(+) + N-(acetyl)-sphing-4-enine; Xref=Rhea:RHEA:41408, ChEBI:CHEBI:15378, ChEBI:CHEBI:44811, ChEBI:CHEBI:46979, ChEBI:CHEBI:57756, ChEBI:CHEBI:64496; Evidence={ECO:0000250|UniProtKB:P83006};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41409; Evidence={ECO:0000250|UniProtKB:P83006}; CATALYTIC ACTIVITY: Reaction=1-organyl-2-lyso-sn-glycero-3-phospholipid + a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine = 1-O-alkyl-sn-glycero-3-phosphocholine + 1-organyl-2-acetyl-sn-glycero-3-phospholipid; Xref=Rhea:RHEA:11048, ChEBI:CHEBI:685, ChEBI:CHEBI:30909, ChEBI:CHEBI:36707, ChEBI:CHEBI:76590; EC=2.3.1.149; Evidence={ECO:0000250|UniProtKB:P83006};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11049; Evidence={ECO:0000250|UniProtKB:P83006}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-glutaryl-sn-glycero-3-phosphocholine + H2O = 1-O-hexadecyl-sn-glycero-3-phosphocholine + glutarate + H(+); Xref=Rhea:RHEA:41700, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30921, ChEBI:CHEBI:64496, ChEBI:CHEBI:78371; Evidence={ECO:0000250|UniProtKB:P79106};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41701; Evidence={ECO:0000250|UniProtKB:P79106}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-succinyl-sn-glycero-3-phosphocholine + H2O = 1-O-hexadecyl-sn-glycero-3-phosphocholine + H(+) + succinate; Xref=Rhea:RHEA:41696, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30031, ChEBI:CHEBI:64496, ChEBI:CHEBI:78369; Evidence={ECO:0000250|UniProtKB:P79106};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41697; Evidence={ECO:0000250|UniProtKB:P79106}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-butanoyl-sn-glycero-3-phosphocholine + H2O = 1-O-hexadecyl-sn-glycero-3-phosphocholine + butanoate + H(+); Xref=Rhea:RHEA:41692, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:64496, ChEBI:CHEBI:78368; Evidence={ECO:0000250|UniProtKB:P79106};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41693; Evidence={ECO:0000250|UniProtKB:P79106}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-propanoyl-sn-glycero-3-phosphocholine + H2O = 1-O-hexadecyl-sn-glycero-3-phosphocholine + H(+) + propanoate; Xref=Rhea:RHEA:41688, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17272, ChEBI:CHEBI:64496, ChEBI:CHEBI:78367; Evidence={ECO:0000250|UniProtKB:P79106};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41689; Evidence={ECO:0000250|UniProtKB:P79106};
DNA Binding
EC Number 3.1.1.47; 2.3.1.149
Enzyme Function FUNCTION: Catalyzes the hydrolyze of the acetyl group at the sn-2 position of platelet-activating factor (PAF) and its analogs, leading to their inactivation (By similarity). Hydrolyzes propionyl and butyroyl moieties approximately half as effectively as PAF (By similarity). Also catalyzes transacetylation of the acetyl group from platelet-activating factor (PAF) to lysoplasmalogen and to sphingosine, producing plasmalogen analogs of PAF and N-acetylsphingosine (C2-ceramide) respectively. Has a marked selectivity for phospholipids with short acyl chains at the sn-2 position (By similarity). {ECO:0000250|UniProtKB:P79106, ECO:0000250|UniProtKB:P83006}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Initiator methionine (1); Lipidation (1); Sequence conflict (3)
Keywords Cytoplasm;Endoplasmic reticulum;Hydrolase;Lipid degradation;Lipid metabolism;Lipoprotein;Membrane;Myristate;Reference proteome;Transferase
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P79106}. Membrane {ECO:0000250|UniProtKB:P79106}; Lipid-anchor {ECO:0000250|UniProtKB:P79106}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P79106}; Lipid-anchor {ECO:0000250|UniProtKB:P79106}. Note=In resting cells, localizes to intracellular membranes and cytoplasm. Translocates from the cytoplasm to intracellular membranes upon oxidative stress. {ECO:0000250|UniProtKB:P79106}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 11217851; 12466851; 14610273; 14681479; 16141072; 17488888; 18024956; 18799693; 29035365;
Motif
Gene Encoded By
Mass 43,562
Kinetics
Metal Binding
Rhea ID RHEA:17777; RHEA:17778; RHEA:40479; RHEA:40480; RHEA:41396; RHEA:41397; RHEA:41408; RHEA:41409; RHEA:11048; RHEA:11049; RHEA:41700; RHEA:41701; RHEA:41696; RHEA:41697; RHEA:41692; RHEA:41693; RHEA:41688; RHEA:41689
Cross Reference Brenda 3.1.1.47;