ID   PA14_POLDO              Reviewed;         316 AA.
AC   Q6Q249;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Phospholipase A1 4 {ECO:0000303|PubMed:16196201};
DE            EC=3.1.1.32 {ECO:0000250|UniProtKB:P0DMB7};
DE   AltName: Allergen=Pol d 1 {ECO:0000303|PubMed:16196201};
DE   Flags: Precursor; Fragment;
OS   Polistes dominula (European paper wasp) (Vespa dominula).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC   Vespidae; Polistinae; Polistini; Polistes.
OX   NCBI_TaxID=743375;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=16196201; DOI=10.1556/abiol.56.2005.3-4.9;
RA   Moawad T.I., Hoffman D.R., Zalat S.;
RT   "Isolation, cloning and characterization of Polistes dominulus venom
RT   phospholipase A1 and its isoforms.";
RL   Acta Biol. Hung. 56:261-274(2005).
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: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:P0DMB7};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:16196201}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:16196201}.
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; AY566649; AAS67044.1; -; mRNA.
DR   AlphaFoldDB; Q6Q249; -.
DR   SMR; Q6Q249; -.
DR   Allergome; 3436; Pol d 1.0104.
DR   Allergome; 586; Pol d 1.
DR   ESTHER; poldo-q6q252; 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   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; Signal.
FT   SIGNAL          <1..4
FT                   /evidence="ECO:0000255"
FT   PROPEP          5..14
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000425189"
FT   CHAIN           15..316
FT                   /note="Phospholipase A1 4"
FT                   /id="PRO_5000093094"
FT   ACT_SITE        153
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   ACT_SITE        181
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   ACT_SITE        242
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   DISULFID        20..103
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   DISULFID        192..197
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   DISULFID        235..240
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   DISULFID        257..284
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   DISULFID        258..309
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   DISULFID        277..282
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   NON_TER         1
SQ   SEQUENCE   316 AA;  35023 MW;  12CB3A74BB368405 CRC64;
     ADDLTTLRNG TLDRGITPDC TFNEKDIELH VYSRDKRNGI ILKKEILKNY DLFQKSQISH
     QIAILIHGFL STGNNENFDA MAKALIEIDN FLVISVDWKK GACNAFASTN DVLGYSQAVG
     NTRHVGKYVA DFTKLLVEQY KVPMSNIRLI GHSLGAHTSG FAGKEVQRLK LGKYKEIIGL
     DPAGPSFLTS KCPDRLCETD AEYVQAIHTS AILGVYYNVG SVDFYVNYGK SQPGCSEPSC
     SHTKAVKYLT ECIKRECCLI GTPWKSYFST PKSISQCKRD TCVCVGLNAQ SYPAKGSFYV
     PVEKDAPYCH NEGIKL