ID   PA1_VESMG               Reviewed;         337 AA.
AC   P0CH47;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   25-MAY-2022, entry version 24.
DE   RecName: Full=Probable phospholipase A1 magnifin {ECO:0000303|PubMed:18023835};
DE            EC=3.1.1.32 {ECO:0000250|UniProtKB:P0DMB4};
DE   Flags: Precursor;
OS   Vespa magnifica (Hornet).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC   Vespidae; Vespinae; Vespa.
OX   NCBI_TaxID=202807;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 34-48; 75-88; 169-180 AND
RP   238-257, FUNCTION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=18023835; DOI=10.1016/j.toxicon.2007.10.003;
RA   Yang H., Xu X., Ma D., Zhang K., Lai R.;
RT   "A phospholipase A1 platelet activator from the wasp venom of Vespa
RT   magnifica (Smith).";
RL   Toxicon 51:289-296(2008).
CC   -!- FUNCTION: Has phospholipase activity, probably a phospholipase A1
CC       activity as suggested by sequence similarity. In vivo, induces dose-
CC       dependently platelet aggregation at nanomolar concentration and induces
CC       thrombosis in vivo (PubMed:18023835). {ECO:0000250|UniProtKB:P0DMB4,
CC       ECO:0000269|PubMed:18023835}.
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:0000250|UniProtKB:P0DMB4};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18023835}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:18023835}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC       {ECO:0000250|UniProtKB:A2VBC4}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P0CH47; -.
DR   SMR; P0CH47; -.
DR   ESTHER; vesmg-pa1; Insect_Phospholipase.
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:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008970; F:phospholipase A1 activity; IEA:UniProtKB-EC.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00707; Pancreat_lipase_like; 1.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002334; Allerg_PlipaseA1.
DR   InterPro; IPR013818; Lipase.
DR   InterPro; IPR033906; Lipase_N.
DR   InterPro; IPR000734; TAG_lipase.
DR   PANTHER; PTHR11610; PTHR11610; 1.
DR   Pfam; PF00151; Lipase; 1.
DR   PRINTS; PR00825; DOLALLERGEN.
DR   PRINTS; PR00821; TAGLIPASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00120; LIPASE_SER; 1.
PE   1: Evidence at protein level;
KW   Allergen; Direct protein sequencing; Disulfide bond;
KW   Hemostasis impairing toxin; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Platelet aggregation activating toxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..33
FT                   /evidence="ECO:0000305|PubMed:18023835"
FT                   /id="PRO_0000425191"
FT   CHAIN           34..337
FT                   /note="Probable phospholipase A1 magnifin"
FT                   /evidence="ECO:0000269|PubMed:18023835"
FT                   /id="PRO_0000398340"
FT   ACT_SITE        173
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   ACT_SITE        201
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   ACT_SITE        266
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   DISULFID        39..123
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   DISULFID        212..217
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   DISULFID        255..264
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   DISULFID        281..305
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   DISULFID        282..330
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   DISULFID        298..303
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
SQ   SEQUENCE   337 AA;  37617 MW;  78339BBD7B346009 CRC64;
     MNLKYLLLFF CLVQVLHYCY SHGDPSLSNE LDRGLIPKCK LVPEQISFVL STRENQNGVF
     LTLDNLSKGG ILPKSDLSSI PVIFLIHGFI SSANNSNYVD MTKALLEKND CMVISIDWRD
     GACTHEFKIL KFIGYPNAVK NTRAVGKYIA DFTKLLMQKY KVSLANIRLI GHSLGAQIAG
     FAGKEYQKFK LGKYPEIIGL DPAGPLFKSN DCSERICETD AHYVQIIHTS NNLGTERTLG
     TVDFYVNNGY NQPGCYLSFL GEACSHTRAV KYFTECIRHE CCLIGVPQSK NPQPVSKCTR
     KECVCIGLNA KTYPKTGSFY VPVESKAPYC NNKGKKI