PA12A_VESVE
ID PA12A_VESVE Reviewed; 25 AA.
AC P0DMB7;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 22-JAN-2014, sequence version 1.
DT 25-MAY-2022, entry version 19.
DE RecName: Full=Phospholipase A1 verutoxin-2a {ECO:0000303|PubMed:10484737};
DE Short=VT-2a {ECO:0000303|PubMed:10484737};
DE EC=3.1.1.32 {ECO:0000269|PubMed:10484737};
DE EC=3.1.1.5 {ECO:0000269|PubMed:10484737};
DE Flags: Fragment;
OS Vespa velutina (Asian yellow-legged hornet).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC Vespidae; Vespinae; Vespa.
OX NCBI_TaxID=202808;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, TOXIC
RP DOSE, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=10484737; DOI=10.1016/s0041-0101(98)00229-3;
RA Ho C.L., Lin Y.L., Li S.F.;
RT "Three toxins with phospholipase activity isolated from the yellow-legged
RT hornet (Vespa verutina) venom.";
RL Toxicon 37:1015-1024(1999).
CC -!- FUNCTION: Catalyzes the hydrolysis of glycerophospholipids such as
CC phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine) and has a
CC moderate activity to hydrolyze lysoglycerophospholipids such as
CC lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine), but is
CC unable to hydrolyze sphingomyelin. In addition to acting as allergens,
CC it possesses a potent hemolytic activity on red blood cells of mice
CC (98.8% of hemolysis at 3.0 ug/ml). {ECO:0000269|PubMed:10484737}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32;
CC Evidence={ECO:0000269|PubMed:10484737};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18690;
CC Evidence={ECO:0000269|PubMed:10484737};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-2-hexadecanoyl-sn-glycero-3-phosphocholine
CC + H2O = (9Z)-octadecenoate + 2-hexadecanoyl-sn-glycero-3-
CC phosphocholine + H(+); Xref=Rhea:RHEA:38787, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:74667,
CC ChEBI:CHEBI:76078; Evidence={ECO:0000269|PubMed:10484737};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38788;
CC Evidence={ECO:0000269|PubMed:10484737};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid +
CC H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
CC Evidence={ECO:0000269|PubMed:10484737};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178;
CC Evidence={ECO:0000269|PubMed:10484737};
CC -!- ACTIVITY REGULATION: Activity is maximal in the presence of calcium.
CC However, unlike phospholipases A2 whose catalytic activity is strictly
CC calcium-dependent, this enzyme shows considerable catalytic activity on
CC phosphatidylcholine emulsified in calcium free solution; the catalytic
CC activity of VT-2a assayed in the absence of calcium ions is 18-20% of
CC that assayed in solution containing calcium ions.
CC {ECO:0000269|PubMed:10484737}.
CC -!- PATHWAY: Phospholipid metabolism. {ECO:0000305|PubMed:10484737}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10484737}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:10484737}.
CC -!- PTM: Contains six disulfide bonds. {ECO:0000250}.
CC -!- MASS SPECTROMETRY: Mass=33360.0; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10484737};
CC -!- ALLERGEN: Causes an allergic reaction in human.
CC {ECO:0000305|PubMed:10484737}.
CC -!- TOXIC DOSE: LD(50) is 0.87 mg/kg by intravenous injection into mice
CC (tail vein). {ECO:0000269|PubMed:10484737}.
CC -!- MISCELLANEOUS: Is about 0.95% of the total proteins in the venom.
CC {ECO:0000305|PubMed:10484737}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR AlphaFoldDB; P0DMB7; -.
DR SMR; P0DMB7; -.
DR SwissLipids; SLP:000001929; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0004622; F:lysophospholipase activity; IEA:RHEA.
DR GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008970; F:phospholipase A1 activity; IEA:UniProtKB-EC.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Allergen; Cytolysis; Direct protein sequencing; Disulfide bond; Hemolysis;
KW Hydrolase; Lipid degradation; Lipid metabolism; Secreted.
FT CHAIN 1..>25
FT /note="Phospholipase A1 verutoxin-2a"
FT /id="PRO_0000425197"
FT NON_TER 25
SQ SEQUENCE 25 AA; 3012 MW; E25AB936D1BA744D CRC64;
FNPCPYSDDT VKMIILTREN KKHDF
