ID   PA1_VESCR               Reviewed;         301 AA.
AC   P0CH87;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   25-MAY-2022, entry version 29.
DE   RecName: Full=Phospholipase A1 {ECO:0000305};
DE            EC=3.1.1.32 {ECO:0000250|UniProtKB:P0DMB4};
DE   AltName: Allergen=Vesp c 1 {ECO:0000303|PubMed:15753912};
OS   Vespa crabro (European hornet).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC   Vespidae; Vespinae; Vespa.
OX   NCBI_TaxID=7445;
RN   [1]
RP   PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=15753912; DOI=10.1016/j.jaci.2004.11.020;
RA   Hoffman D.R., Sakell R.H., Schmidt M.;
RT   "Sol i 1, the phospholipase allergen of imported fire ant venom.";
RL   J. Allergy Clin. Immunol. 115:611-616(2005).
CC   -!- FUNCTION: Catalyzes the hydrolysis of phosphatidylcholine with
CC       phospholipase A1 (EC 3.1.1.32) activity (By similarity). Shows
CC       hemolytic activity (By similarity). {ECO:0000250|UniProtKB:P0DMB4}.
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:15753912}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. Binds to IgE.
CC       {ECO:0000250|UniProtKB:A2VBC4}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P0CH87; -.
DR   SMR; P0CH87; -.
DR   Allergome; 3525; Vesp c 1.0101.
DR   Allergome; 672; Vesp c 1.
DR   ESTHER; vescr-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: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   1: Evidence at protein level;
KW   Allergen; Cytolysis; Direct protein sequencing; Disulfide bond; Hemolysis;
KW   Hydrolase; Lipid degradation; Lipid metabolism; Secreted.
FT   CHAIN           1..301
FT                   /note="Phospholipase A1"
FT                   /evidence="ECO:0000269|PubMed:15753912"
FT                   /id="PRO_0000401920"
FT   ACT_SITE        137
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   ACT_SITE        165
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   ACT_SITE        230
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   DISULFID        4..87
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   DISULFID        176..181
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   DISULFID        219..228
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   DISULFID        245..269
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   DISULFID        246..294
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   DISULFID        262..267
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
SQ   SEQUENCE   301 AA;  33384 MW;  5F788492944BBEB4 CRC64;
     FNPCPYSDDT VKMIVLTREN KKYDFYTLDT IKNHNEFKDT ITLKPHVFIT HGFTSSATAE
     NFVVMAKALL DKGNYLVILT DWRMAACTNE IAGLKLAYYP YAASNTRLVG NYIATVTKML
     VQKYNVPMAN IRLIGHSLGA HISGFAGKKV QELGLGKYPE IIGLDPAGPS FKSNDCSQRI
     CETDANYVQI IHTSNRLGTE RTLGTVDFYM NNGYNQPGCG LPIIGETCSH TRAVKYFTEC
     IKHECCLIGV PKSKNPQPVS KCTRNECVCV GLNAKTYPKT GSFYVPVESK APYCNNKGKI
     I