ID   PA2_BUNCI               Reviewed;          39 AA.
AC   P86780;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Phospholipase A2 {ECO:0000303|PubMed:19463845};
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase {ECO:0000250|UniProtKB:Q9NZ20};
DE   Flags: Fragment;
OS   Bunodosoma caissarum (Sea anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Actiniidae; Bunodosoma.
OX   NCBI_TaxID=31165;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, TISSUE
RP   SPECIFICITY, AND MASS SPECTROMETRY.
RC   TISSUE=Tentacle;
RX   PubMed=19463845; DOI=10.1016/j.toxicon.2009.05.005;
RA   Martins R.D., Alves R.S., Martins A.M., Barbosa P.S., Evangelista J.S.,
RA   Evangelista J.J., Ximenes R.M., Toyama M.H., Toyama D.O., Souza A.J.,
RA   Orts D.J., Marangoni S., de Menezes D.B., Fonteles M.C., Monteiro H.S.;
RT   "Purification and characterization of the biological effects of
RT   phospholipase A(2) from sea anemone Bunodosoma caissarum.";
RL   Toxicon 54:413-420(2009).
CC   -!- FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC       groups in 3-sn-phosphoglycerides. Induces insulin secretion in isolated
CC       rat islets under high glucose concentration conditions, but not under
CC       low glucose concentration conditions. Increases perfusion pressure,
CC       renal vascular resistance, urinary flow, glomerular filtration rate,
CC       and potassium, sodium, and chloride excretion levels in rat kidney.
CC       Does not increase perfusion pressure in the rat mesenteric vascular
CC       bed. {ECO:0000269|PubMed:19463845}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC         glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC         ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-
CC         ProRule:PRU10036, ECO:0000269|PubMed:19463845};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:P14555};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P14555};
CC   -!- ACTIVITY REGULATION: Inhibited by morin and p-BPB.
CC       {ECO:0000269|PubMed:19463845}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19463845,
CC       ECO:0000305}. Nematocyst {ECO:0000269|PubMed:19463845, ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed uniformly in tentacles (at protein
CC       level). {ECO:0000269|PubMed:19463845}.
CC   -!- MASS SPECTROMETRY: Mass=14706; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:19463845};
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000255}.
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DR   AlphaFoldDB; P86780; -.
DR   SMR; P86780; -.
DR   GO; GO:0005576; C:extracellular region; TAS:UniProtKB.
DR   GO; GO:0042151; C:nematocyst; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004623; F:phospholipase A2 activity; IDA:UniProtKB.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR   Gene3D; 1.20.90.10; -; 1.
DR   InterPro; IPR016090; PLipase_A2_dom.
DR   InterPro; IPR036444; PLipase_A2_dom_sf.
DR   InterPro; IPR033113; PLipase_A2_His_AS.
DR   Pfam; PF05826; Phospholip_A2_2; 1.
DR   SUPFAM; SSF48619; SSF48619; 1.
DR   PROSITE; PS00118; PA2_HIS; 1.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Disulfide bond; Hydrolase;
KW   Lipid degradation; Lipid metabolism; Metal-binding; Nematocyst; Secreted;
KW   Toxin.
FT   CHAIN           1..>39
FT                   /note="Phospholipase A2"
FT                   /id="PRO_0000399441"
FT   ACT_SITE        36
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZ20,
FT                   ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-
FT                   ProRule:PRU10036"
FT   BINDING         10
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P14555"
FT   BINDING         12
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P14555"
FT   BINDING         14
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P14555"
FT   BINDING         37
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P14555"
FT   DISULFID        11..33
FT                   /evidence="ECO:0000250|UniProtKB:P14555"
FT   NON_TER         39
FT                   /evidence="ECO:0000303|PubMed:19463845"
SQ   SEQUENCE   39 AA;  4153 MW;  8AF51BA73E14272A CRC64;
     GATIMPGTLW CGKGNSAADY LQLGVWKDTA HCCRDHDGC