ID PA1_VESGE Reviewed; 300 AA.
AC Q3ZU95;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 22-FEB-2023, entry version 69.
DE RecName: Full=Phospholipase A1 {ECO:0000303|Ref.1};
DE Short=PLA1 {ECO:0000305};
DE EC=3.1.1.32 {ECO:0000250|UniProtKB:P0DMB4};
DE AltName: Allergen=Ves g 1 {ECO:0000303|Ref.1};
OS Vespula germanica (German yellow jacket) (Paravespula germanica).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC Vespidae; Vespinae; Vespula.
OX NCBI_TaxID=30212;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Suck R., Fiebig H., Cromwell O.;
RT "cDNA cloning of phospholipase A1 from Vespula germanica (Ves g 1).";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the hydrolysis of phosphatidylcholine with
CC phospholipase A1 activity (By similarity). May act as an allergen and
CC induce hemolytic activity (By similarity).
CC {ECO:0000250|UniProtKB:P0DMB4, 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:P0DMB4};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|Ref.1}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305|Ref.1}.
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; AM083318; CAJ28931.1; -; mRNA.
DR AlphaFoldDB; Q3ZU95; -.
DR SMR; Q3ZU95; -.
DR Allergome; 659; Ves g 1.
DR ESTHER; vesge-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: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 2: Evidence at transcript level;
KW Allergen; Disulfide bond; Hydrolase; Lipid degradation; Lipid metabolism;
KW Secreted.
FT CHAIN 1..300
FT /note="Phospholipase A1"
FT /evidence="ECO:0000305|Ref.1"
FT /id="PRO_5000076445"
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 229
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..227
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT DISULFID 244..268
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT DISULFID 245..293
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT DISULFID 261..266
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
SQ SEQUENCE 300 AA; 33240 MW; CC0E3A26CE8B7D04 CRC64;
GPKCPFNTDT VSMIIETREN RNRDLYTLQT LQNHPEFKEK TITRPVVFIT HGFTSSASET
NFINLSKALV DKDNYMVISI DWQTAACTNE AAGLKYLYYP TAASNTRLVG QYIATITQKL
VKQYKISMAN IRLIGHSLGA HVSGFAGKKV QELKLGKYSE IIGLDPAGPS FSSNKCSDRL
CETDAEYVQI LHTSNHLGTE RILGTVDFYM NNGKNQPGCG RFFTEVCSHS RAVIYMAECI
KHECCLIGIP KSKSSQPISS CTKQECVCVG LNAKKYPSRG SFYVPVESTA PFCNNKGKII
//
