PA11_VESAF
ID PA11_VESAF Reviewed; 334 AA.
AC P0DMB4;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 22-JAN-2014, sequence version 1.
DT 25-MAY-2022, entry version 21.
DE RecName: Full=Phospholipase A1 1 {ECO:0000305};
DE EC=3.1.1.32 {ECO:0000269|PubMed:23159790};
DE AltName: Full=Allergen Ves a 1.01 {ECO:0000303|PubMed:23159790};
DE AltName: Full=Vespapase {ECO:0000303|PubMed:23159790};
DE AltName: Allergen=Vesp a 1 {ECO:0000305};
DE Flags: Precursor;
OS Vespa affinis (Lesser banded hornet).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC Vespidae; Vespinae; Vespa.
OX NCBI_TaxID=882735;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR
RP LOCATION, BIOASSAY, BIOPHYSICOCHEMICAL PROPERTIES, TOXIC DOSE, 3D-STRUCTURE
RP MODELING, AND MASS SPECTROMETRY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=23159790; DOI=10.1016/j.toxicon.2012.10.024;
RA Sukprasert S., Rungsa P., Uawonggul N., Incamnoi P., Thammasirirak S.,
RA Daduang J., Daduang S.;
RT "Purification and structural characterisation of phospholipase A1
RT (Vespapase, Ves a 1) from Thai banded tiger wasp (Vespa affinis) venom.";
RL Toxicon 61:151-164(2013).
CC -!- FUNCTION: Catalyzes the hydrolysis of phosphatidylcholine with
CC phospholipase A1 (EC 3.1.1.32) activity (PubMed:23159790). Shows
CC hemolytic activity (By similarity). Shows a phospholipase A1 enzymatic
CC activity of 3.6 U/ml (PubMed:23159790). In vivo, a mixture of this
CC protein and Ves a 1.02 is able to paralyze crickets (PubMed:23159790).
CC {ECO:0000250|UniProtKB:P0DMB7, ECO:0000269|PubMed:23159790}.
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:0000269|PubMed:23159790};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Loses its activity after heat treatment.
CC {ECO:0000269|PubMed:23159790};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23159790}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:23159790}.
CC -!- PTM: Not glycosylated. {ECO:0000269|PubMed:23159790}.
CC -!- MASS SPECTROMETRY: Mass=33441.5; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:23159790};
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC {ECO:0000250|UniProtKB:A2VBC4}.
CC -!- TOXIC DOSE: 60 mg/kg body weight of a mixture of this protein and Ves a
CC 1.02 is able to paralyze 33% of the crickets.
CC {ECO:0000269|PubMed:23159790}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR AlphaFoldDB; P0DMB4; -.
DR SMR; P0DMB4; -.
DR Allergome; 11764; Vesp a 1.
DR ESTHER; vesaf-PA11; 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:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002334; Allerg_PlipaseA1.
DR InterPro; IPR013818; Lipase.
DR InterPro; IPR000734; TAG_lipase.
DR PANTHER; PTHR11610; PTHR11610; 1.
DR Pfam; PF00151; Lipase; 1.
DR PRINTS; PR00825; DOLALLERGEN.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW Allergen; Cytolysis; Disulfide bond; Hemolysis; Hydrolase;
KW Lipid degradation; Lipid metabolism; Neurotoxin; Secreted; Signal; Toxin.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..33
FT /evidence="ECO:0000305|PubMed:23159790"
FT /id="PRO_0000425192"
FT CHAIN 34..334
FT /note="Phospholipase A1 1"
FT /evidence="ECO:0000305|PubMed:23159790"
FT /id="PRO_0000425193"
FT ACT_SITE 170
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT ACT_SITE 198
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 263
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT DISULFID 37..120
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT DISULFID 209..214
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT DISULFID 252..261
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT DISULFID 278..302
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT DISULFID 279..327
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT DISULFID 295..300
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
SQ SEQUENCE 334 AA; 37318 MW; 8B8712D786F38B12 CRC64;
MMNLKYLLFF CLVQALHYCY AYGDPSLSNE LDRFNPCPYS DDTVKMIILT RENKKHDFYT
LNTIKNHNEF KKSTIKHQVV FITHGFTSTA TAENFLAMAE ALLDKGNYLV ILIDWRVAAC
TNEMAGVKLA YYSYAASNTR LVGNYIATVT KMLVQQYNVP MANIRLIGHS LGAHTSGFAG
KKVQELRLGK YSEIIGLDPA GPSFKSQECS QRICETDANY VQIIHTSNHL GTLVTLGTVD
FYMNNGYNQP GCGLPIIGET CSHTRAVKYF TECIRHECCL IGVPQSKNPQ PVSKCTRNEC
VCVGLNAKTY PKTGSFYVPV ESKAPYCNNK GKII
