ID   PA1_POLGA               Reviewed;          42 AA.
AC   P83542;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Phospholipase A1 {ECO:0000303|PubMed:14572904};
DE            EC=3.1.1.32 {ECO:0000269|PubMed:14572904};
DE   AltName: Allergen=Pol g 1 {ECO:0000303|PubMed:14572904};
DE   Flags: Fragment;
OS   Polistes gallicus (Paper wasp).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC   Vespidae; Polistinae; Polistini; Polistes.
OX   NCBI_TaxID=34730;
RN   [1]
RP   PROTEIN SEQUENCE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MASS
RP   SPECTROMETRY, SUBCELLULAR LOCATION, AND ALLERGEN.
RC   TISSUE=Venom;
RX   PubMed=14572904; DOI=10.1016/j.bbagen.2003.07.001;
RA   Pantera B., Hoffman D.R., Carresi L., Cappugi G., Turillazzi S., Manao G.,
RA   Severino M., Spadolini I., Orsomando G., Moneti G., Pazzagli L.;
RT   "Characterization of the major allergens purified from the venom of the
RT   paper wasp Polistes gallicus.";
RL   Biochim. Biophys. Acta 1623:72-81(2003).
CC   -!- FUNCTION: Catalyzes the hydrolysis of phosphatidylcholine with
CC       phospholipase A1 (EC 3.1.1.32) activity (PubMed:14572904). Shows
CC       hemolytic activity (By similarity). {ECO:0000250|UniProtKB:P0DMB7,
CC       ECO:0000269|PubMed:14572904}.
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:14572904};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         Vmax=283.2 umol/min/mg enzyme {ECO:0000269|PubMed:14572904};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14572904}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:14572904}.
CC   -!- PTM: Contains six disulfide bonds. {ECO:0000250}.
CC   -!- MASS SPECTROMETRY: Mass=33475; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:14572904};
CC   -!- ALLERGEN: Causes an allergic reaction in human.
CC       {ECO:0000269|PubMed:14572904}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P83542; -.
DR   Allergome; 1208; Pol g 1.
DR   Allergome; 3443; Pol g 1.0101.
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: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..>42
FT                   /note="Phospholipase A1"
FT                   /id="PRO_0000090377"
FT   DISULFID        6..?
FT                   /evidence="ECO:0000250"
FT   NON_TER         42
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   42 AA;  4985 MW;  524589208F2113C3 CRC64;
     GITPDCTFNE KDIELHVYSR DKRNGIILKK EILKNYDLFK ES