Detail Information for IndEnz0005000792
IED ID IndEnz0005000792
Enzyme Type ID lipase000792
Protein Name Platelet-activating factor acetylhydrolase IB subunit alpha1
EC 3.1.1.47
PAF acetylhydrolase 29 kDa subunit
PAF-AH 29 kDa subunit
PAF-AH subunit gamma
PAFAH subunit gamma
Gene Name PAFAH1B3 PAFAHG
Organism Homo sapiens (Human)
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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MSGEENPASKPTPVQDVQGDGRWMSLHHRFVADSKDKEPEVVFIGDSLVQLMHQCEIWRELFSPLHALNFGIGGDGTQHVLWRLENGELEHIRPKIVVVWVGTNNHGHTAEQVTGGIKAIVQLVNERQPQARVVVLGLLPRGQHPNPLREKNRQVNELVRAALAGHPRAHFLDADPGFVHSDGTISHHDMYDYLHLSRLGYTPVCRALHSLLLRLLAQDQGQGAPLLEPAP
Enzyme Length 231
Uniprot Accession Number Q15102
Absorption
Active Site ACT_SITE 47; /evidence=ECO:0000250|UniProtKB:Q29460; ACT_SITE 192; /evidence=ECO:0000250|UniProtKB:Q29460; ACT_SITE 195; /evidence=ECO:0000250|UniProtKB:Q29460
Activity Regulation ACTIVITY REGULATION: Beta subunit (PAFAH1B1) inhibits the acetylhydrolase activity of the alpha1/alpha1 catalytic homodimer. {ECO:0000250|UniProtKB:Q29460}.
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:Q29460};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17778; Evidence={ECO:0000250|UniProtKB:Q29460}; 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:Q29460};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40480; Evidence={ECO:0000250|UniProtKB:Q29460}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphate + H2O = 1-O-hexadecyl-sn-glycero-3-phosphate + acetate + H(+); Xref=Rhea:RHEA:41704, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:77580, ChEBI:CHEBI:78385; Evidence={ECO:0000250|UniProtKB:Q29460};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41705; Evidence={ECO:0000250|UniProtKB:Q29460};
DNA Binding
EC Number 3.1.1.47
Enzyme Function FUNCTION: Alpha1 catalytic subunit of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)) heterotetrameric enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and modulates the action of PAF. The activity and substrate specificity of PAF-AH (I) are affected by its subunit composition. Both alpha1/alpha1 homodimer (PAFAH1B3/PAFAH1B3 homodimer) and alpha1/alpha2 heterodimer(PAFAH1B3/PAFAH1B2 heterodimer) hydrolyze 1-O-alkyl-2-acetyl-sn-glycero-3-phosphoric acid (AAGPA) more efficiently than PAF, but they have little hydrolytic activity towards 1-O-alkyl-2-acetyl-sn-glycero-3-phosphorylethanolamine (AAGPE). Plays an important role during the development of brain. {ECO:0000250|UniProtKB:Q29460}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Initiator methionine (1); Modified residue (2); Natural variant (1)
Keywords Acetylation;Cytoplasm;Direct protein sequencing;Hydrolase;Lipid degradation;Lipid metabolism;Phosphoprotein;Reference proteome
Interact With Q8TBB1; A8MW99; Q9GZT8; P68402; Itself; Q9NRD5; Q9H190
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm.
Modified Residue MOD_RES 2; /note="N-acetylserine"; /evidence="ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"; MOD_RES 2; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10359595; 11080672; 12432908; 16169070; 16189514; 18641641; 19549727; 19622634; 19738201; 19753100; 20360068; 20420828; 21044950; 21516116; 21844189; 22130221; 22461910; 22623428; 24954006; 25416956; 25945974; 26496610; 9671731;
Motif
Gene Encoded By
Mass 25,734
Kinetics
Metal Binding
Rhea ID RHEA:17777; RHEA:17778; RHEA:40479; RHEA:40480; RHEA:41704; RHEA:41705
Cross Reference Brenda