ID   PA12_DOLMA              Reviewed;         303 AA.
AC   P53357;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-JUN-2009, entry version 53.
DE   RecName: Full=Phospholipase A1 2;
DE            EC=3.1.1.32;
DE            EC=3.1.1.4;
DE   AltName: Full=Allergen Dol m I;
DE   AltName: Allergen=Dol m 1.02;
OS   Dolichovespula maculata (Bald-faced hornet) (Vespula maculata).
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC   Vespidae; Vespinae; Dolichovespula.
OX   NCBI_TaxID=7441;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Venom;
RX   MEDLINE=94257972; PubMed=8199462;
RA   Hoffman D.R.;
RT   "Allergens in hymenoptera venom. XXVI: the complete amino acid
RT   sequences of two vespid venom phospholipases.";
RL   Int. Arch. Allergy Immunol. 104:184-190(1994).
CC   -!- FUNCTION: Hydrolysis of phosphatidylcholine with phospholipase A2
CC       (EC 3.1.1.4) and phospholipase A1 (EC 3.1.1.32) activities.
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   PIR; A44563; A44563.
DR   HSSP; P54318; 1BU8.
DR   BRENDA; 3.1.1.32; 299019.
DR   BRENDA; 3.1.1.4; 299019.
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   PRINTS; PR00821; TAGLIPASE.
DR   PROSITE; PS00120; LIPASE_SER; 1.
PE   1: Evidence at protein level;
KW   Allergen; Direct protein sequencing; Disulfide bond; Hydrolase;
KW   Lipid degradation; Secreted.
FT   CHAIN         1    303       Phospholipase A1 2.
FT                                /FTId=PRO_0000090375.
FT   ACT_SITE    140    140       Nucleophile (By similarity).
FT   ACT_SITE    168    168       Charge relay system (By similarity).
FT   ACT_SITE    232    232       Charge relay system (By similarity).
FT   VARIANT      55     55       G -> E.
FT   VARIANT     295    295       F -> Y.
SQ   SEQUENCE   303 AA;  33782 MW;  85816A837C0F3AF8 CRC64;
     GILPECKLVP EEISFVLSTR ENRDGVYLTL QKLKNGKMFK NSDLSSKKVP FLIHGFISSA
     TNKNYADMTR ALLDKDDIMV ISIDWRDGAC SNEFALLKFI GYPKAVENTR AVGKYIADFS
     KILIQKYKVL LENIRLIGHS LGAQIAGFAG KEFQRFKLGK YPEIIGLDPA GPSFKKKDCP
     ERICETDAHY VQILHTSSNL GTERTLGTVD FYINDGSNQP GCTYIIGETC SHTRAVKYLT
     ECIRRECCLI GVPQSKNPQP VSKCTRNECV CVGLNAKEYP KKGSFYVPVE AKAPFCNNNG
     KII
//