ID Q8NI47_HUMAN Unreviewed; 48 AA. AC Q8NI47; DT 01-OCT-2002, integrated into UniProtKB/TrEMBL. DT 01-OCT-2002, sequence version 1. DT 04-FEB-2015, entry version 69. DE RecName: Full=Phospholipase A(2) {ECO:0000256|RuleBase:RU361236}; DE EC=3.1.1.4 {ECO:0000256|RuleBase:RU361236}; DE Flags: Fragment; GN Name=PLA2G2A {ECO:0000313|EMBL:AAM21271.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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: Phosphatidylcholine + H(2)O = 1- CC acylglycerophosphocholine + a carboxylate. CC {ECO:0000256|RuleBase:RU361236}. CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|RuleBase:RU361236}; CC Note=Binds 1 Ca(2+) ion per subunit. CC {ECO:0000256|RuleBase:RU361236}; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU361236}. CC -!- SIMILARITY: Belongs to the phospholipase A2 family. CC {ECO:0000256|RuleBase:RU361236}. 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 UniGene; Hs.466804; -. DR ProteinModelPortal; Q8NI47; -. DR ChiTaRS; PLA2G2A; human. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0004623; F:phospholipase A2 activity; IEA:InterPro. DR GO; GO:0016042; P:lipid catabolic process; IEA:InterPro. DR Gene3D; 1.20.90.10; -; 1. DR InterPro; IPR001211; PLipase_A2. DR InterPro; IPR016090; PLipase_A2_dom. DR PANTHER; PTHR11716; PTHR11716; 1. DR Pfam; PF00068; Phospholip_A2_1; 1. DR PRINTS; PR00389; PHPHLIPASEA2. DR SMART; SM00085; PA2c; 1. DR SUPFAM; SSF48619; SSF48619; 1. PE 3: Inferred from homology; KW Calcium {ECO:0000256|RuleBase:RU361236}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00122668}; KW Hydrolase {ECO:0000256|RuleBase:RU361236}; KW Lipid metabolism {ECO:0000256|RuleBase:RU361236}; KW Secreted {ECO:0000256|RuleBase:RU361236, KW ECO:0000256|SAAS:SAAS00122677}. FT NON_TER 1 1 {ECO:0000313|EMBL:AAM21271.1}. FT NON_TER 48 48 {ECO:0000313|EMBL:AAM21271.1}. SQ SEQUENCE 48 AA; 5168 MW; 6297E410A0FAAD92 CRC64; LLQARGNLVN FHRMIKLTTG KEAALSYGFY GCHCGVGGRG SPKDATDR //