ID   Q8NI47_HUMAN            Unreviewed;        48 AA.
AC   Q8NI47;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   16-MAR-2016, entry version 75.
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:RU003654}.
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DR   EMBL; AF368841; AAM21271.1; -; Genomic_DNA.
DR   UniGene; Hs.466804; -.
DR   ProteinModelPortal; Q8NI47; -.
DR   STRING; 9606.ENSP00000364252; -.
DR   PaxDb; Q8NI47; -.
DR   eggNOG; KOG4087; Eukaryota.
DR   eggNOG; ENOG411283D; LUCA.
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:UniProtKB-EC.
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:SAAS00435610};
KW   Hydrolase {ECO:0000256|RuleBase:RU361236};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU361236};
KW   Secreted {ECO:0000256|RuleBase:RU361236}.
FT   DOMAIN        7     48       PA2c. {ECO:0000259|SMART:SM00085}.
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
//