ID   PA21_OPICY              Reviewed;          16 AA.
AC   P86119;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   25-MAY-2022, entry version 15.
DE   RecName: Full=Phospholipase A2 1;
DE            Short=PLA2;
DE            EC=3.1.1.4;
DE   AltName: Full=Phospholipase OcyPLA2_1 {ECO:0000303|PubMed:18502464};
DE   Flags: Fragment;
OS   Opisthacanthus cayaporum (South American scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Iurida; Scorpionoidea; Hemiscorpiidae; Opisthacanthus.
OX   NCBI_TaxID=573324;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, CATALYTIC ACTIVITY, AND MASS SPECTROMETRY.
RC   TISSUE=Venom {ECO:0000269|PubMed:18502464};
RX   PubMed=18502464; DOI=10.1016/j.toxicon.2008.03.029;
RA   Schwartz E.F., Camargos T.S., Zamudio F.Z., Silva L.P., Bloch C. Jr.,
RA   Caixeta F., Schwartz C.A., Possani L.D.;
RT   "Mass spectrometry analysis, amino acid sequence and biological activity of
RT   venom components from the Brazilian scorpion Opisthacanthus cayaporum.";
RL   Toxicon 51:1499-1508(2008).
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:0000269|PubMed:18502464};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=14237.0; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:18502464};
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DR   AlphaFoldDB; P86119; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Secreted.
FT   CHAIN           1..>16
FT                   /note="Phospholipase A2 1"
FT                   /id="PRO_0000358859"
FT   NON_TER         16
FT                   /evidence="ECO:0000303|PubMed:18502464"
SQ   SEQUENCE   16 AA;  1659 MW;  7BB1BE9B61AB132E CRC64;
     DFTGVKFDNT IGCGKG