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   16-JUN-2009, entry version 58.
DE   RecName: Full=Phospholipase A1;
DE            EC=3.1.1.32;
DE            EC=3.1.1.4;
DE   AltName: Full=Allergen Ves v I;
DE   AltName: Allergen=Ves v 1;
DE   Flags: Precursor;
OS   Vespula vulgaris (Yellow jacket) (Wasp).
OC   Eukaryota; Metazoa; 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], AND PROTEIN SEQUENCE OF 37-65; 165-183;
RP   247-263 AND 273-294.
RC   TISSUE=Venom, and Venom gland;
RX   MEDLINE=96426243; 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:
RT   sequence similarity and antigenic cross-reactivity with their hornet
RT   and wasp homologs and possible implications for clinical allergy.";
RL   J. Allergy Clin. Immunol. 98:588-600(1996).
CC   -!- FUNCTION: Hydrolysis of phosphatidylcholine with phospholipase A2
CC       (EC 3.1.1.4) and phospholipase A1 (EC 3.1.1.32) activities (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Phosphatidylcholine + H(2)O = 2-
CC       acylglycerophosphocholine + a carboxylate.
CC   -!- CATALYTIC ACTIVITY: Phosphatidylcholine + H(2)O = 1-
CC       acylglycerophosphocholine + a carboxylate.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- PTM: Contains six disulfide bonds (By similarity).
CC   -!- ALLERGEN: Causes an allergic reaction in human.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase
CC       family.
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DR   EMBL; L43561; AAB48072.1; -; mRNA.
DR   HSSP; P16233; 1LPB.
DR   BRENDA; 3.1.1.32; 299027.
DR   BRENDA; 3.1.1.4; 299027.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008970; F:phospholipase A1 activity; IEA:EC.
DR   GO; GO:0004623; F:phospholipase A2 activity; IEA:EC.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR002334; Dol/Ves_allerg.
DR   InterPro; IPR000734; Lipase.
DR   InterPro; IPR013818; Lipase_N.
DR   PANTHER; PTHR11610; Lipase; 1.
DR   Pfam; PF00151; Lipase; 1.
DR   PRINTS; PR00825; DOLALLERGEN.
DR   PROSITE; PS00120; LIPASE_SER; 1.
PE   1: Evidence at protein level;
KW   Allergen; Direct protein sequencing; Disulfide bond; Hydrolase;
KW   Lipid degradation; Secreted; Signal.
FT   SIGNAL        1     36
FT   CHAIN        37    336       Phospholipase A1.
FT                                /FTId=PRO_0000017813.
FT   ACT_SITE    173    173       Nucleophile (By similarity).
FT   ACT_SITE    201    201       Charge relay system (By similarity).
FT   ACT_SITE    265    265       Charge relay system (By similarity).
FT   CONFLICT     37     37       G -> F (in Ref. 1; AA sequence).
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
//