PA2A1_LACMU
ID PA2A1_LACMU Reviewed; 50 AA.
AC P0C932;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Acidic phospholipase A2 1;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=LM-PLA2-I;
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=9408022;
RA Fuly A.L., Machado O.L., Alves E.W., Carlini C.R.;
RT "Mechanism of inhibitory action on platelet activation of a phospholipase
RT A2 isolated from Lachesis muta (Bushmaster) snake venom.";
RL Thromb. Haemost. 78:1372-1380(1997).
RN [2]
RP FUNCTION.
RC TISSUE=Venom;
RX PubMed=10728833; DOI=10.1016/s0041-0101(99)00208-1;
RA Fuly A.L., Calil-Elias S., Zingali R.B., Guimaraes J.A., Melo P.A.;
RT "Myotoxic activity of an acidic phospholipase A2 isolated from Lachesis
RT muta (Bushmaster) snake venom.";
RL Toxicon 38:961-972(2000).
RN [3]
RP FUNCTION.
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 displays a potent
CC enzymatic activity as measured by indirect hemolysis of red blood
CC cells. Is neither lethal when injected into mice nor does it present
CC anticoagulant activity. Displays a moderate inhibitory activity on the
CC aggregation of platelets induced by low levels of ADP, thrombin and
CC arachidonate. In contrast, strongly inhibits platelet aggregation
CC induced by high doses of collagen. Shows myotoxic activity, increases
CC the plasma creatine-kinase activity and induces edema and myonecrosis
CC of mouse skeletal muscles. PLA2 catalyzes the calcium-dependent
CC hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
CC {ECO:0000269|PubMed:10728833, ECO:0000269|PubMed:12007562,
CC ECO:0000269|PubMed:9408022}.
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:9408022}.
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; P0C932; -.
DR SMR; P0C932; -.
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; IDA:CACAO.
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..>50
FT /note="Acidic phospholipase A2 1"
FT /id="PRO_0000370688"
FT ACT_SITE 47
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10035,
FT ECO:0000255|PROSITE-ProRule:PRU10036"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 28..44
FT /evidence="ECO:0000250"
FT NON_TER 50
SQ SEQUENCE 50 AA; 5642 MW; 3CB009973459362B CRC64;
HLLQFGDLID KIAGRSGFWY YGFYGCYCGL GGRGRPQDAT DRCCFVHDCC
