| IED ID | IndEnz0005000721 |
| Enzyme Type ID | lipase000721 |
| Protein Name |
Group IIF secretory phospholipase A2 GIIF sPLA2 sPLA2-IIF EC 3.1.1.4 Phosphatidylcholine 2-acylhydrolase 2F |
| Gene Name | Pla2g2f |
| 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 | MKKFFAIAVLAGSVVTTAHSSLLNLKSMVEAITHRNSILSFVGYGCYCGLGGRGHPMDEVDWCCHAHDCCYEKLFEQGCRPYVDHYDHRIENGTMIVCTELNETECDKQTCECDKSLTLCLKDHPYRNKYRGYFNVYCQGPTPNCSIYDPYPEEVTCGHGLPATPVST |
| Enzyme Length | 168 |
| Uniprot Accession Number | Q9QZT4 |
| Absorption | |
| Active Site | ACT_SITE 67; /evidence=ECO:0000255|PROSITE-ProRule:PRU10035; ACT_SITE 114; /evidence=ECO:0000255|PROSITE-ProRule:PRU10035 |
| 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:0000269|PubMed:11877435};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802; Evidence={ECO:0000305|PubMed:11877435}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) + H(+); Xref=Rhea:RHEA:40919, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72841, ChEBI:CHEBI:75158; Evidence={ECO:0000250|UniProtKB:Q9BZM2};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40920; Evidence={ECO:0000250|UniProtKB:Q9BZM2}; 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:11877435};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816; Evidence={ECO:0000305|PubMed:11877435}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40431, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:73004, ChEBI:CHEBI:73009; Evidence={ECO:0000269|PubMed:11877435};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432; Evidence={ECO:0000305|PubMed:11877435}; 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:Q9BZM2};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780; Evidence={ECO:0000250|UniProtKB:Q9BZM2}; 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:0000250|UniProtKB:Q9BZM2};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41753; Evidence={ECO:0000250|UniProtKB:Q9BZM2}; |
| DNA Binding | |
| EC Number | 3.1.1.4 |
| Enzyme Function | FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids (PubMed:10531313). Hydrolyzes the ester bond of the fatty acyl group attached at the sn-2 position of phospholipids (phospholipase A2 activity), the catalytic efficiency decreasing in the following order: phosphatidylglycerols > phosphatidylethanolamines > phosphatidylcholines > phosphatidylserines (PubMed:11877435, PubMed:10531313). May play a role in lipid mediator production in inflammatory conditions, by providing arachidonic acid to downstream cyclooxygenases and lipoxygenases (PubMed:10531313). {ECO:0000269|PubMed:10531313, ECO:0000269|PubMed:11877435}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0-7.0. {ECO:0000269|PubMed:10531313, ECO:0000269|PubMed:11877435}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Alternative sequence (1); Chain (1); Disulfide bond (7); Glycosylation (3); Metal binding (4); Mutagenesis (2); Region (1); Signal peptide (1) |
| Keywords | Alternative splicing;Calcium;Cell membrane;Disulfide bond;Glycoprotein;Hydrolase;Immunity;Innate immunity;Lipid degradation;Lipid metabolism;Membrane;Metal-binding;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | INDUCTION: Strongly up-regulated by lipopolysaccharide (LPS) in brain, heart, liver, colon and testis. {ECO:0000269|PubMed:11877435}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11877435}. Cell membrane; Peripheral membrane protein {ECO:0000269|PubMed:11877435}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10918573; 14681479; 16931517; 17626619; 18554416; 21267068; 21677750; 23624557; 24269828; 24732399; 26438362; 26828067; 27226632; 27226633; |
| Motif | |
| Gene Encoded By | |
| Mass | 18,880 |
| Kinetics | |
| Metal Binding | METAL 47; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 49; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 51; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 68; /note=Calcium; /evidence=ECO:0000250 |
| Rhea ID | RHEA:15801; RHEA:15802; RHEA:40919; RHEA:40920; RHEA:40815; RHEA:40816; RHEA:40431; RHEA:40432; RHEA:38779; RHEA:38780; RHEA:41752; RHEA:41753 |
| Cross Reference Brenda | 3.1.1.4; |