ID   PA1_POLAN               Reviewed;         301 AA.
AC   Q9U6W0;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Phospholipase A1 {ECO:0000305};
DE            EC=3.1.1.32 {ECO:0000250|UniProtKB:A2VBC4};
DE   AltName: Allergen=Pol a 1 {ECO:0000305};
OS   Polistes annularis (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=27505;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RA   King T.P., Lu G.;
RL   Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the hydrolysis of phosphatidylcholine with
CC       phospholipase A1 (EC 3.1.1.32) activity. Shows hemolytic activity (By
CC       similarity). {ECO:0000250|UniProtKB:A2VBC4,
CC       ECO:0000250|UniProtKB:P0DMB7}.
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:A2VBC4};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|Ref.1}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305|Ref.1}.
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   EMBL; AF174527; AAD52615.1; -; mRNA.
DR   AlphaFoldDB; Q9U6W0; -.
DR   SMR; Q9U6W0; -.
DR   Allergome; 3430; Pol a 1.0101.
DR   Allergome; 583; Pol a 1.
DR   ESTHER; polan-pla1; 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:0044179; P:hemolysis in another organism; 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   2: Evidence at transcript level;
KW   Allergen; Cytolysis; Disulfide bond; Hemolysis; Hydrolase;
KW   Lipid degradation; Lipid metabolism; Secreted.
FT   CHAIN           1..301
FT                   /note="Phospholipase A1"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000090376"
FT   ACT_SITE        138
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   ACT_SITE        166
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   ACT_SITE        227
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   DISULFID        5..88
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   DISULFID        177..182
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   DISULFID        220..225
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   DISULFID        242..269
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   DISULFID        243..294
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   DISULFID        262..267
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
SQ   SEQUENCE   301 AA;  33484 MW;  6A0B7DC76FDCC047 CRC64;
     MSPDCTFNEK DIVFYVYSRD KRDGIILKKE TLTNYDLFTK STISKQVVFL IHGFLSTGNN
     ENFVAMSKAL IEKDDFLVIS VDWKKGACNA FASTKDALGY SKAVGNTRHV GKFVADFTKL
     LVEKYKVLIS NIRLIGHSLG AHTSGFAGKE VQKLKLGKYK EIIGLDPAGP YFHRSDCPDR
     LCVTDAEYVQ VIHTSIILGV YYNVGSVDFY VNYGKNQPGC NEPSCSHTKA VKYLTECIKH
     ECCLIGTPWK KYFSTPKPIS QCRGDTCVCV GLNAKSYPAR GAFYAPVEAN APYCHNEGIK
     L