Detail Information for IndEnz0010001012
IED ID IndEnz0010001012
Enzyme Type ID esterase001012
Protein Name Group 10 secretory phospholipase A2
EC 3.1.1.4
Group X secretory phospholipase A2
GX sPLA2
sPLA2-X
Phosphatidylcholine 2-acylhydrolase 10
Gene Name Pla2g10
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 MLLLLLLLLLGPGPGFSEATRRSHVYKRGLLELAGTLDCVGPRSPMAYMNYGCYCGLGGHGEPRDAIDWCCYHHDCCYSRAQDAGCSPKLDRYPWKCMDHHILCGPAENKCQELLCRCDEELAYCLAGTEYHLKYLFFPSILCEKDSPKCN
Enzyme Length 151
Uniprot Accession Number Q9QXX3
Absorption
Active Site ACT_SITE 74; /evidence=ECO:0000250|UniProtKB:O15496; ACT_SITE 119; /evidence=ECO:0000250|UniProtKB:O15496
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036, ECO:0000269|PubMed:10531313, ECO:0000269|PubMed:12359733};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802; Evidence={ECO:0000305|PubMed:10531313, ECO:0000305|PubMed:12359733}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:38779, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72998, ChEBI:CHEBI:73001; Evidence={ECO:0000250|UniProtKB:O15496};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780; Evidence={ECO:0000250|UniProtKB:O15496}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-octadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40519, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:73858, ChEBI:CHEBI:74965; Evidence={ECO:0000269|PubMed:12359733};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40520; Evidence={ECO:0000305|PubMed:12359733}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999; Evidence={ECO:0000269|PubMed:10531313, ECO:0000269|PubMed:12359733};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224; Evidence={ECO:0000305|PubMed:10531313, ECO:0000305|PubMed:12359733}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-glycerol + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phospho-glycerol + H(+); Xref=Rhea:RHEA:44524, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:84472, ChEBI:CHEBI:84475; Evidence={ECO:0000269|PubMed:12359733};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44525; Evidence={ECO:0000305|PubMed:12359733}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) + H2O = 1-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) + H(+) + hexadecanoate; Xref=Rhea:RHEA:45472, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72829, ChEBI:CHEBI:75158; Evidence={ECO:0000269|PubMed:10531313};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45473; Evidence={ECO:0000305|PubMed:10531313}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phospho-L-serine + H(+); Xref=Rhea:RHEA:41752, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:75020, ChEBI:CHEBI:75029; Evidence={ECO:0000269|PubMed:12359733};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41753; Evidence={ECO:0000305|PubMed:12359733}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40815, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:73004, ChEBI:CHEBI:73008; Evidence={ECO:0000269|PubMed:12359733, ECO:0000269|PubMed:21266583};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816; Evidence={ECO:0000305|PubMed:12359733, ECO:0000305|PubMed:21266583}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phosphate + H(+); Xref=Rhea:RHEA:63996, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:57518, ChEBI:CHEBI:64839; Evidence={ECO:0000250|UniProtKB:O15496};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63997; Evidence={ECO:0000250|UniProtKB:O15496}; 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:O15496};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40480; Evidence={ECO:0000250|UniProtKB:O15496};
DNA Binding
EC Number 3.1.1.4
Enzyme Function FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids. Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids with preference for phosphatidylcholines and phosphatidylglycerols over phosphatidylethanolamines. Preferentially releases sn-2 omega-6 and omega-3 polyunsaturated fatty acyl (PUFA) chains over saturated fatty acyls (PubMed:12359733, PubMed:10531313). Contributes to phospholipid remodeling of very low-density lipoprotein (VLDL), low-density lipoprotein (LDL) and high-density lipoprotein (HDL) particles (By similarity). Hydrolyzes LDL phospholipids releasing unsaturated fatty acids that regulate macrophage differentiation toward foam cells (By similarity). Efficiently hydrolyzes and inactivates PAF, a potent lipid mediator present in oxidized LDL (By similarity). May act in an autocrine and paracrine manner. Secreted by lung epithelium, targets membrane phospholipids of infiltrating eosinophils, releasing arachidonate and boosting eicosanoid and cysteinyl leukotriene synthesis involved in airway inflammatory response (PubMed:29093264, PubMed:17403936). Secreted by gut epithelium, hydrolyzes dietary and biliary phosphatidylcholines in the gastrointestinal lumen, thereby regulating adipogenesis and body weight (PubMed:21266581). Plays a stem cell regulator role in colon epithelium. Within intracellular compartment, mediates Paneth-like cell differentiation and its stem cell supporting functions by inhibiting Wnt signaling pathway in intestinal stem cell (ISC). Secreted in the intestinal lumen upon inflammation, acts in an autocrine way and promotes prostaglandin E2 synthesis that stimulates the Wnt signaling pathway in ISCs and tissue regeneration (PubMed:27292189). May participate in hair follicle morphogenesis by regulating phosphatidylethanolamines metabolism at the outermost epithelial layer and facilitating melanin synthesis (PubMed:21266583). By generating lysophosphatidylcholines (LPCs) at sperm acrosome controls sperm cell capacitation, acrosome reaction and overall fertility (PubMed:20424324, PubMed:21266581). May promote neurite outgrowth in neuron fibers involved in nociception (PubMed:21266581). Contributes to lipid remodeling of cellular membranes and generation of lipid mediators involved in pathogen clearance. Cleaves sn-2 fatty acyl chains of phosphatidylglycerols and phosphatidylethanolamines, which are major components of membrane phospholipids in bacteria (PubMed:12359733). Displays bactericidal activity against Gram-positive bacteria by directly hydrolyzing phospholipids of the bacterial membrane (PubMed:11694541). In pulmonary epithelium, may contribute to host defense response against adenoviral infection. Prevents adenovirus entry into host cells by hydrolyzing host cell plasma membrane, releasing C16:0 LPCs that inhibit virus-mediated membrane fusion and viral infection. Likely prevents adenoviral entry into the endosomes of host cells (By similarity). May play a role in maturation and activation of innate immune cells including macrophages, group 2 innate lymphoid cells and mast cells (PubMed:29093264). {ECO:0000250|UniProtKB:O15496, ECO:0000269|PubMed:10531313, ECO:0000269|PubMed:11694541, ECO:0000269|PubMed:12359733, ECO:0000269|PubMed:17403936, ECO:0000269|PubMed:20424324, ECO:0000269|PubMed:21266581, ECO:0000269|PubMed:21266583, ECO:0000269|PubMed:27292189, ECO:0000269|PubMed:29093264}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Disulfide bond (8); Metal binding (4); Mutagenesis (1); Propeptide (1); Sequence conflict (1); Signal peptide (1)
Keywords Calcium;Cleavage on pair of basic residues;Cytoplasmic vesicle;Direct protein sequencing;Disulfide bond;Hydrolase;Lipid metabolism;Lysosome;Metal-binding;Phospholipid metabolism;Reference proteome;Secreted;Signal
Interact With
Induction INDUCTION: Up-regulated in alveolar macrophages upon allergen-induced airway inflammation (PubMed:17403936). Up-regulated in bronchoalveolar lavage fluid (BALF) in response to house dust mite proteolytic allergens (PubMed:29093264). {ECO:0000269|PubMed:17403936, ECO:0000269|PubMed:29093264}.
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10531313, ECO:0000269|PubMed:11741598, ECO:0000269|PubMed:20424324}. Lysosome {ECO:0000269|PubMed:11741598}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:20424324}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..17; /evidence=ECO:0000269|PubMed:11019817
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 12021277; 12050136; 12466851; 14610273; 14681479; 15781456; 15789617; 15927955; 16602821; 17008322; 18506007; 18511424; 18539905; 18799693; 20421306; 20424323; 20432503; 20439489; 20585029; 20833395; 20844270; 21267068; 21622863; 21652694; 21677750; 21792918; 21984544; 23349189; 23624557; 24194600; 24204651; 24287291; 24725934; 25122761; 26655718; 26828067; 27226632; 27626380; 9188469;
Motif
Gene Encoded By
Mass 17,005
Kinetics
Metal Binding METAL 54; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 56; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:O15496; METAL 58; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:O15496; METAL 75; /note=Calcium; /evidence=ECO:0000250|UniProtKB:O15496
Rhea ID RHEA:15801; RHEA:15802; RHEA:38779; RHEA:38780; RHEA:40519; RHEA:40520; RHEA:41223; RHEA:41224; RHEA:44524; RHEA:44525; RHEA:45472; RHEA:45473; RHEA:41752; RHEA:41753; RHEA:40815; RHEA:40816; RHEA:63996; RHEA:63997; RHEA:40479; RHEA:40480
Cross Reference Brenda