ID   PA11_POLDO              Reviewed;         337 AA.
AC   Q6Q252;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Phospholipase A1 1 {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;
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], PROTEIN SEQUENCE OF 36-64; 70-82; 86-91;
RP   105-212; 252-265 AND 270-337, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom, and 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:0000269|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; AY566645; AAS67041.1; -; mRNA.
DR   RefSeq; XP_015187185.1; XM_015331699.1.
DR   AlphaFoldDB; Q6Q252; -.
DR   SMR; Q6Q252; -.
DR   Allergome; 3433; Pol d 1.0101.
DR   Allergome; 586; Pol d 1.
DR   ESTHER; poldo-q6q252; Insect_Phospholipase.
DR   GeneID; 107072087; -.
DR   BRENDA; 3.1.1.32; 8173.
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   1: Evidence at protein level;
KW   Allergen; Cytolysis; Direct protein sequencing; Disulfide bond; Hemolysis;
KW   Hydrolase; Lipid degradation; Lipid metabolism; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..35
FT                   /evidence="ECO:0000305|PubMed:16196201"
FT                   /id="PRO_5000093090"
FT   CHAIN           36..337
FT                   /note="Phospholipase A1 1"
FT                   /evidence="ECO:0000269|PubMed:16196201"
FT                   /id="PRO_5000093091"
FT   ACT_SITE        174
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   ACT_SITE        202
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   ACT_SITE        263
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   DISULFID        41..124
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   DISULFID        213..218
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   DISULFID        256..261
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   DISULFID        278..305
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   DISULFID        279..330
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   DISULFID        298..303
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
SQ   SEQUENCE   337 AA;  37559 MW;  C0A7E0E5EBDE448C CRC64;
     MNFKYSILFI CFVKVLDNCY AADDLTTLRN GTLDRGITPD CTFNEKDIEL HVYSRDKRNG
     IILKKEILKN YDLFQKSQIS HQIAILIHGF LSTGNNENFD AMAKALIEID NFLVISVDWK
     KGACNAFAST NDVLGYSQAV GNTRHVGKYV ADFTKLLVEQ YKVPMSNIRL IGHSLGAHTS
     GFAGKEVQRL KLGKYKEIIG LDPAGPSFLT NKCPNRLCET DAEYVQAIHT SAILGVYYNV
     GSVDFYVNYG KSQPGCSEPS CSHTKAVKYL TECIKRECCL IGTPWKSYFS TPKPISQCKR
     DTCVCVGLNA QSYPAKGSFY VPVDKDAPYC HNEGIKL