ID   Q8NI47_HUMAN            Unreviewed;        48 AA.
AC   Q8NI47;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 98.
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}.
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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:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004623; F:phospholipase A2 activity; IEA:InterPro.
DR   GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
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
//