ID   PA2_RHONO               Reviewed;          32 AA.
AC   P43318;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Toxic phospholipase A2 {ECO:0000303|PubMed:7777053};
DE            Short=PLA2;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   Flags: Fragment;
OS   Rhopilema nomadica (Mediteranean medusa).
OC   Eukaryota; Metazoa; Cnidaria; Scyphozoa; Rhizostomeae; Rhizostomatidae;
OC   Rhopilema.
OX   NCBI_TaxID=42738;
RN   [1]
RP   PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC   TISSUE=Tentacle;
RX   PubMed=7777053; DOI=10.1038/375456a0;
RA   Lotan A., Fishman L., Loya Y., Zlotkin E.;
RT   "Delivery of a nematocyst toxin.";
RL   Nature 375:456-456(1995).
CC   -!- FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC       groups in 3-sn-phosphoglycerides. {ECO:0000250}.
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};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7777053}. Nematocyst
CC       {ECO:0000269|PubMed:7777053}.
CC   -!- TOXIC DOSE: LD(50) is 6 ug/g by injection.
CC       {ECO:0000269|PubMed:7777053}.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group III
CC       subfamily. {ECO:0000305}.
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   PIR; S58413; S58413.
DR   AlphaFoldDB; P43318; -.
DR   SMR; P43318; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042151; C:nematocyst; IEA:UniProtKB-SubCell.
DR   GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
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   Pfam; PF05826; Phospholip_A2_2; 1.
DR   SUPFAM; SSF48619; SSF48619; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Nematocyst; Secreted; Toxin.
FT   CHAIN           1..>32
FT                   /note="Toxic phospholipase A2"
FT                   /evidence="ECO:0000269|PubMed:7777053"
FT                   /id="PRO_0000161721"
FT   NON_TER         32
FT                   /evidence="ECO:0000305|PubMed:7777053"
SQ   SEQUENCE   32 AA;  3402 MW;  EFA92AB8CCEB2F59 CRC64;
     GLIKPGTLWC GMGNNAETYD QLGPFADVDS CK