ID   PA22_LACMU              Reviewed;          49 AA.
AC   P0C933;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Phospholipase A2 2;
DE            Short=svPLA2;
DE            EC=3.1.1.4;
DE   AltName: Full=LM-PLA2-II;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   Flags: Fragment;
OS   Lachesis muta muta (Bushmaster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Lachesis.
OX   NCBI_TaxID=8753;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND SUBUNIT.
RC   TISSUE=Venom;
RX   PubMed=12007562; DOI=10.1016/s0006-2952(02)00873-0;
RA   Fuly A.L., de Miranda A.L.P., Zingali R.B., Guimaraes J.A.;
RT   "Purification and characterization of a phospholipase A2 isoenzyme isolated
RT   from Lachesis muta snake venom.";
RL   Biochem. Pharmacol. 63:1589-1597(2002).
CC   -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that has a high indirect
CC       hemolytic activity and a potent inhibitory effect on platelet
CC       aggregation induced by ADP and collagen. Also produces a significant
CC       paw edema reaction in rats. This edematous response is abolished by
CC       pretreatment with either indomethacin or dexamethasone, suggesting the
CC       involvement of cyclo-oxygenase. May be myotoxic. PLA2 catalyzes the
CC       calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-
CC       phosphoglycerides. {ECO:0000269|PubMed:12007562}.
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. {ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12007562}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC       D49 sub-subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0C933; -.
DR   SMR; P0C933; -.
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: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; IPR001211; PLipase_A2.
DR   InterPro; IPR016090; PLipase_A2_dom.
DR   InterPro; IPR036444; PLipase_A2_dom_sf.
DR   InterPro; IPR033113; PLipase_A2_His_AS.
DR   PANTHER; PTHR11716; PTHR11716; 1.
DR   Pfam; PF00068; Phospholip_A2_1; 1.
DR   PRINTS; PR00389; PHPHLIPASEA2.
DR   SMART; SM00085; PA2c; 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;
KW   Hemostasis impairing toxin; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Metal-binding; Myotoxin; Platelet aggregation inhibiting toxin; Secreted;
KW   Toxin.
FT   CHAIN           1..>49
FT                   /note="Phospholipase A2 2"
FT                   /id="PRO_0000370689"
FT   ACT_SITE        46
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10035,
FT                   ECO:0000255|PROSITE-ProRule:PRU10036"
FT   BINDING         26
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         28
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         30
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         47
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   DISULFID        27..43
FT                   /evidence="ECO:0000250"
FT   NON_TER         49
SQ   SEQUENCE   49 AA;  5623 MW;  C60353331BFBAB0E CRC64;
     HLLQFEQLIR KIAGRGFRYY GFYGCYCGLG GQGRPQDATD RCCFVHDCC