| IED ID | IndEnz0005000697 |
| Enzyme Type ID | lipase000697 |
| Protein Name |
Phospholipase A1 member A EC 3.1.1.111 Phosphatidylserine-specific phospholipase A1 PS-PLA1 |
| Gene Name | PLA1A NMD PSPLA1 |
| 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 | MPPGPWESCFWVGGLILWLSVGSSGDAPPTPQPKCADFQSANLFEGTDLKVQFLLFVPSNPSCGQLVEGSSDLQNSGFNATLGTKLIIHGFRVLGTKPSWIDTFIRTLLRATNANVIAVDWIYGSTGVYFSAVKNVIKLSLEISLFLNKLLVLGVSESSIHIIGVSLGAHVGGMVGQLFGGQLGQITGLDPAGPEYTRASVEERLDAGDALFVEAIHTDTDNLGIRIPVGHVDYFVNGGQDQPGCPTFFYAGYSYLICDHMRAVHLYISALENSCPLMAFPCASYKAFLAGRCLDCFNPFLLSCPRIGLVEQGGVKIEPLPKEVKVYLLTTSSAPYCMHHSLVEFHLKELRNKDTNIEVTFLSSNITSSSKITIPKQQRYGKGIIAHATPQCQINQVKFKFQSSNRVWKKDRTTIIGKFCTALLPVNDREKMVCLPEPVNLQASVTVSCDLKIACV |
| Enzyme Length | 456 |
| Uniprot Accession Number | Q53H76 |
| 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:0000269|PubMed:10196188};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42213; Evidence={ECO:0000305|PubMed:10196188}; CATALYTIC ACTIVITY: [Isoform 1]: 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:0000269|PubMed:10196188};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40492; Evidence={ECO:0000305|PubMed:10196188}; 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:0000269|PubMed:10196188};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32980; Evidence={ECO:0000305|PubMed:10196188}; CATALYTIC ACTIVITY: [Isoform 1]: 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:0000269|PubMed:10196188};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40500; Evidence={ECO:0000305|PubMed:10196188}; CATALYTIC ACTIVITY: [Isoform 2]: 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:0000269|PubMed:10196188};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40500; Evidence={ECO:0000305|PubMed:10196188}; |
| 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 (PubMed:10196188). 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 (By similarity). 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:0000269|PubMed:10196188}.; FUNCTION: [Isoform 2]: Hydrolyzes lyso-PS but not PS. {ECO:0000269|PubMed:10196188}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (4); Chain (1); Disulfide bond (3); Glycosylation (2); Natural variant (3); Region (1); Sequence conflict (1); Signal peptide (1) |
| Keywords | Alternative splicing;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 | 17101204; 17620599; 19632984; 19913121; 20573295; 20628086; 24368210; 24886443; 25505071; 25750298; 28143894; 29500864; 30016790; 31161554; 31468739; 31978406; 32060356; 33723350; 34884486; |
| Motif | |
| Gene Encoded By | |
| Mass | 49,715 |
| 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 | 3.1.1.111;3.1.1.32; |