ID   PA22_OPICY              Reviewed;          27 AA.
AC   P86120;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Phospholipase A2 2 {ECO:0000303|PubMed:18502464};
DE            Short=OcyPLA2_2 {ECO:0000303|PubMed:18502464};
DE            EC=3.1.1.4;
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, AND CATALYTIC ACTIVITY.
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.
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:18502464};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000255}.
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DR   AlphaFoldDB; P86120; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
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.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Hydrolase; Lipid degradation;
KW   Lipid metabolism; Metal-binding; Secreted.
FT   CHAIN           1..>27
FT                   /note="Phospholipase A2 2"
FT                   /id="PRO_0000358860"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         11
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P00630"
FT   BINDING         13
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P00630"
FT   BINDING         15
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P00630"
FT   NON_TER         27
FT                   /evidence="ECO:0000303|PubMed:18502464"
SQ   SEQUENCE   27 AA;  2880 MW;  1C5C5E13BA252510 CRC64;
     FMKVIDPGTK WCGPGNKAAD DTDNGKN