ID   PA1_VESVU               Reviewed;         336 AA.
AC   P49369;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   22-FEB-2023, entry version 94.
DE   RecName: Full=Phospholipase A1 {ECO:0000305};
DE            Short=PLA1 {ECO:0000305};
DE            EC=3.1.1.32 {ECO:0000250|UniProtKB:P0DMB4};
DE   AltName: Full=Allergen Ves v I;
DE   AltName: Allergen=Ves v 1 {ECO:0000303|PubMed:8828537};
DE   Flags: Precursor;
OS   Vespula vulgaris (Yellow jacket) (Wasp).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC   Vespidae; Vespinae; Vespula.
OX   NCBI_TaxID=7454;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 37-65; 165-183; 247-263 AND
RP   273-294, SUBCELLULAR LOCATION, AND ALLERGEN.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=8828537; DOI=10.1016/s0091-6749(96)70093-3;
RA   King T.P., Lu G., Gonzalez M., Qian N., Soldatova L.;
RT   "Yellow jacket venom allergens, hyaluronidase and phospholipase: sequence
RT   similarity and antigenic cross-reactivity with their hornet and wasp
RT   homologs and possible implications for clinical allergy.";
RL   J. Allergy Clin. Immunol. 98:588-600(1996).
CC   -!- FUNCTION: Catalyzes the hydrolysis of phosphatidylcholine with
CC       phospholipase A1 activity (By similarity). Induces hemolytic activity
CC       (By similarity). Acts as an allergen (PubMed:8828537).
CC       {ECO:0000250|UniProtKB:P0DMB4, ECO:0000250|UniProtKB:P0DMB7,
CC       ECO:0000305|PubMed:8828537}.
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:8828537}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:8828537}.
CC   -!- ALLERGEN: Causes an allergic reaction in human (By similarity). It
CC       exhibits some cross-reactivity with antibodies from mouse immunizated
CC       to other Hymenoptera phospholipases (PubMed:8828537).
CC       {ECO:0000250|UniProtKB:A2VBC4, ECO:0000269|PubMed:8828537}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
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DR   EMBL; L43561; AAB48072.1; -; mRNA.
DR   AlphaFoldDB; P49369; -.
DR   SMR; P49369; -.
DR   Allergome; 3520; Ves v 1.0101.
DR   Allergome; 668; Ves v 1.
DR   ESTHER; vesvu-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:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00707; Pancreat_lipase_like; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 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; LIPASE; 1.
DR   Pfam; PF00151; Lipase; 1.
DR   PRINTS; PR00825; DOLALLERGEN.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS00120; LIPASE_SER; 1.
PE   1: Evidence at protein level;
KW   Allergen; Direct protein sequencing; Disulfide bond; Hydrolase;
KW   Lipid degradation; Lipid metabolism; Secreted; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   PROPEP          28..36
FT                   /evidence="ECO:0000269|PubMed:8828537"
FT                   /id="PRO_0000425190"
FT   CHAIN           37..336
FT                   /note="Phospholipase A1"
FT                   /id="PRO_0000017813"
FT   ACT_SITE        173
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   ACT_SITE        201
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   ACT_SITE        265
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   DISULFID        40..123
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   DISULFID        212..217
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   DISULFID        255..263
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   DISULFID        280..304
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   DISULFID        281..329
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   DISULFID        297..302
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   CONFLICT        37
FT                   /note="G -> F (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   336 AA;  37676 MW;  65548B7F5BE56456 CRC64;
     MEENMNLKYL LLFVYFVQVL NCCYGHGDPL SYELDRGPKC PFNSDTVSII IETRENRNRD
     LYTLQTLQNH PEFKKKTITR PVVFITHGFT SSASETNFIN LAKALVDKDN YMVISIDWQT
     AACTNEAAGL KYLYYPTAAR NTRLVGQYIA TITQKLVKHY KISMANIRLI GHSLGAHASG
     FAGKKVQELK LGKYSEIIGL DPARPSFDSN HCSERLCETD AEYVQIIHTS NYLGTEKTLG
     TVDFYMNNGK NQPGCGRFFS EVCSHSRAVI YMAECIKHEC CLIGIPKSKS SQPISSCTKQ
     ECVCVGLNAK KYPSRGSFYV PVESTAPFCN NKGKII
//