ID Q8NI47_HUMAN Unreviewed; 48 AA. AC Q8NI47; DT 01-OCT-2002, integrated into UniProtKB/TrEMBL. DT 01-OCT-2002, sequence version 1. DT 29-MAY-2024, entry version 99. DE RecName: Full=Phospholipase A2, membrane associated {ECO:0000256|ARBA:ARBA00041125}; DE EC=3.1.1.4 {ECO:0000256|ARBA:ARBA00013278}; DE AltName: Full=GIIC sPLA2 {ECO:0000256|ARBA:ARBA00042021}; DE AltName: Full=Group IIA phospholipase A2 {ECO:0000256|ARBA:ARBA00041646}; DE AltName: Full=Phosphatidylcholine 2-acylhydrolase 2A {ECO:0000256|ARBA:ARBA00041844}; DE Flags: Fragment; GN Name=PLA2G2A {ECO:0000313|EMBL:AAM21271.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:AAM21271.1}; RN [1] {ECO:0000313|EMBL:AAM21271.1} RP NUCLEOTIDE SEQUENCE. RA Kostka H.; RT "New missense mutations in the PLA2G2A gene."; RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) + H2O CC = 1-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) + H(+) + CC hexadecanoate; Xref=Rhea:RHEA:45472, ChEBI:CHEBI:7896, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72829, CC ChEBI:CHEBI:75158; Evidence={ECO:0000256|ARBA:ARBA00036461}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45473; CC Evidence={ECO:0000256|ARBA:ARBA00036461}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn- CC glycero-3-phosphocholine + H2O = (4Z,7Z,10Z,13Z,16Z,19Z)- CC docosahexaenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); CC Xref=Rhea:RHEA:41231, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:72998, ChEBI:CHEBI:74963, ChEBI:CHEBI:77016; CC Evidence={ECO:0000256|ARBA:ARBA00036719}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41232; CC Evidence={ECO:0000256|ARBA:ARBA00036719}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero- CC 3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1- CC hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+); CC Xref=Rhea:RHEA:40431, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:32395, ChEBI:CHEBI:73004, ChEBI:CHEBI:73009; CC Evidence={ECO:0000256|ARBA:ARBA00036113}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432; CC Evidence={ECO:0000256|ARBA:ARBA00036113}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3- CC phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn- CC glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40811, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, CC ChEBI:CHEBI:72998, ChEBI:CHEBI:73002; CC Evidence={ECO:0000256|ARBA:ARBA00023408}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812; CC Evidence={ECO:0000256|ARBA:ARBA00023408}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3- CC phosphoethanolamine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn- CC glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40911, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, CC ChEBI:CHEBI:73004, ChEBI:CHEBI:73007; CC Evidence={ECO:0000256|ARBA:ARBA00023391}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40912; CC Evidence={ECO:0000256|ARBA:ARBA00023391}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3- CC phosphoglycerol + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn- CC glycero-3-phosphoglycerol + H(+); Xref=Rhea:RHEA:44524, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, CC ChEBI:CHEBI:84472, ChEBI:CHEBI:84475; CC Evidence={ECO:0000256|ARBA:ARBA00043731}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44525; CC Evidence={ECO:0000256|ARBA:ARBA00043731}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + H2O = a 1- CC acyl-sn-glycero-3-phosphoethanolamine + a fatty acid + H(+); CC Xref=Rhea:RHEA:44604, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:28868, ChEBI:CHEBI:64381, ChEBI:CHEBI:64612; CC Evidence={ECO:0000256|ARBA:ARBA00036775}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44605; CC Evidence={ECO:0000256|ARBA:ARBA00036775}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|PIRSR:PIRSR601211-2}; CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR601211-2}; CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane CC {ECO:0000256|ARBA:ARBA00004450}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004450}. Secreted CC {ECO:0000256|ARBA:ARBA00004613}. CC -!- SIMILARITY: Belongs to the phospholipase A2 family. CC {ECO:0000256|ARBA:ARBA00007056}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF368841; AAM21271.1; -; Genomic_DNA. DR AlphaFoldDB; Q8NI47; -. DR PeptideAtlas; Q8NI47; -. DR ChiTaRS; PLA2G2A; human. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; IEA:TreeGrafter. DR GO; GO:0005543; F:phospholipid binding; IEA:TreeGrafter. DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro. DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW. DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW. DR GO; GO:0016042; P:lipid catabolic process; IEA:InterPro. DR GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro. DR Gene3D; 1.20.90.10; Phospholipase A2 domain; 1. DR InterPro; IPR001211; PLipase_A2. DR InterPro; IPR016090; PLipase_A2_dom. DR InterPro; IPR036444; PLipase_A2_dom_sf. DR PANTHER; PTHR11716; PHOSPHOLIPASE A2 FAMILY MEMBER; 1. DR PANTHER; PTHR11716:SF9; PHOSPHOLIPASE A2, MEMBRANE ASSOCIATED; 1. DR Pfam; PF00068; Phospholip_A2_1; 1. DR PRINTS; PR00389; PHPHLIPASEA2. DR SUPFAM; SSF48619; Phospholipase A2, PLA2; 1. PE 3: Inferred from homology; KW Antimicrobial {ECO:0000256|ARBA:ARBA00022638}; KW Bacteriolytic enzyme {ECO:0000256|ARBA:ARBA00022638}; KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR601211-2}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR601211-2}; KW Secreted {ECO:0000256|ARBA:ARBA00022525}. FT DOMAIN 8..48 FT /note="Phospholipase A2" FT /evidence="ECO:0000259|Pfam:PF00068" FT BINDING 35 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR601211-2" FT BINDING 37 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR601211-2" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AAM21271.1" FT NON_TER 48 FT /evidence="ECO:0000313|EMBL:AAM21271.1" SQ SEQUENCE 48 AA; 5168 MW; 6297E410A0FAAD92 CRC64; LLQARGNLVN FHRMIKLTTG KEAALSYGFY GCHCGVGGRG SPKDATDR //