Detail Information for IndEnz0005000865
IED ID IndEnz0005000865
Enzyme Type ID lipase000865
Protein Name Phospholipase A1 member A
EC 3.1.1.111
Phosphatidylserine-specific phospholipase A1
PS-PLA1
Gene Name Pla1a Pspla1
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 MRPGLWETCFWLWGPLLWLSIGSSGNVPPTTQPKCTDFQSANLLRGTNLKVQFLLFTPSDPSCGQLVEEGSDIRSSEFNASLGTKVIIHGFRALGTKPSWIDKFISAVLRAADANVIAVDWVYGSTGVYYSAVENVVKLSLEISRFLSKLLELGVSESSIHIIGVSLGAHVGGMVGHFYKGQLGQITGLDPAGPEYTRASLEERLDAGDALFVEAIHTDTDNLGIRIPVGHVDYFVNGGQDQPGCPAFFHAGYNYLICDHMRAVHLYISALENTCPLMAFPCASYKAFLAGDCLDCFNPFLLSCPRIGLVERGGVMIEPLPKEVKVYLLTTSSAPYCVHHSLVEFYLKEKRKKDTSIEVTFLSNNVTSSVKITIPKQQLEGRGVMAHPNPQCQINQVKLKFQVSSRVWRKDRTPVVGTFCTAPLPVNDSKKTVCIPEPVRLQAGVPAFQDLKIACV
Enzyme Length 456
Uniprot Accession Number Q8VI78
Absorption
Active Site ACT_SITE 166; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 190; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037; ACT_SITE 260; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H2O = a 2-acyl-sn-glycero-3-phospho-L-serine + a fatty acid + H(+); Xref=Rhea:RHEA:42212, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57262, ChEBI:CHEBI:65214; EC=3.1.1.111; Evidence={ECO:0000250|UniProtKB:P97535};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42213; Evidence={ECO:0000250|UniProtKB:P97535}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z)-octadecenoyl-sn-glycero-3-phospho-L-serine + H2O = (9Z)-octadecenoate + 2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H(+); Xref=Rhea:RHEA:40491, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:74905, ChEBI:CHEBI:77342; Evidence={ECO:0000250|UniProtKB:P97535};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40492; Evidence={ECO:0000250|UniProtKB:P97535}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phospho-L-serine + H2O = 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phospho-L-serine + H(+) + hexadecanoate; Xref=Rhea:RHEA:41187, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:75032, ChEBI:CHEBI:77830; Evidence={ECO:0000250|UniProtKB:P97535};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41188; Evidence={ECO:0000250|UniProtKB:P97535}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phospho-L-serine + H2O = a fatty acid + H(+) + sn-glycero-3-phospho-L-serine; Xref=Rhea:RHEA:32979, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:64379, ChEBI:CHEBI:64765; EC=3.1.1.111; Evidence={ECO:0000250|UniProtKB:P97535};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32980; Evidence={ECO:0000250|UniProtKB:P97535}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O = (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-L-serine; Xref=Rhea:RHEA:40499, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:64765, ChEBI:CHEBI:74617; Evidence={ECO:0000250|UniProtKB:P97535};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40500; Evidence={ECO:0000250|UniProtKB:P97535};
DNA Binding
EC Number 3.1.1.111
Enzyme Function FUNCTION: Hydrolyzes the ester bond of the acyl group attached at the sn-1 position of phosphatidylserines (phospholipase A1 activity) and 1-acyl-2-lysophosphatidylserines (lysophospholipase activity) in the pathway of phosphatidylserines acyl chain remodeling (By similarity). Cleaves phosphatidylserines exposed on the outer leaflet of the plasma membrane of apoptotic cells producing 2-acyl-1-lysophosphatidylserines, which in turn enhance mast cell activation and histamine production. Has no activity toward other glycerophospholipids including phosphatidylcholines, phosphatidylethanolamines, phosphatidic acids or phosphatidylinositols, or glycerolipids such as triolein (By similarity). {ECO:0000250|UniProtKB:P97535, ECO:0000250|UniProtKB:Q53H76}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Disulfide bond (3); Glycosylation (1); Sequence conflict (3); Signal peptide (1)
Keywords Disulfide bond;Glycoprotein;Hydrolase;Lipid degradation;Lipid metabolism;Reference proteome;Secreted;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P97535}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..25; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 14610273; 14681479; 18799693; 21677750; 21857648; 23943622; 24006456;
Motif
Gene Encoded By
Mass 49,984
Kinetics
Metal Binding
Rhea ID RHEA:42212; RHEA:42213; RHEA:40491; RHEA:40492; RHEA:41187; RHEA:41188; RHEA:32979; RHEA:32980; RHEA:40499; RHEA:40500
Cross Reference Brenda