ID   VEST1_VESTR             Reviewed;         301 AA.
AC   P0DPT0;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2019, sequence version 1.
DT   25-MAY-2022, entry version 8.
DE   RecName: Full=Phospholipase A1 VesT1.02 {ECO:0000303|PubMed:29605550};
DE            EC=3.1.1.32 {ECO:0000269|PubMed:29605550};
OS   Vespa tropica (Greater banded hornet) (Sphex tropica).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC   Vespidae; Vespinae; Vespa.
OX   NCBI_TaxID=7450;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-14, FUNCTION, CATALYTIC
RP   ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=29605550; DOI=10.1016/j.toxicon.2018.03.015;
RA   Rungsa P., Peigneur S., Daduang S., Tytgat J.;
RT   "Purification and biochemical characterization of VesT1s, a novel
RT   phospholipase A1 isoform isolated from the venom of the greater banded wasp
RT   Vespa tropica.";
RL   Toxicon 148:74-84(2018).
CC   -!- FUNCTION: Catalyzes the hydrolysis of phosphatidylcholine with
CC       phospholipase A1 activity (PubMed:29605550). Shows hemolytic activity
CC       (By similarity). {ECO:0000250|UniProtKB:P0DMB7,
CC       ECO:0000269|PubMed:29605550}.
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:29605550};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         Vmax=214.6 umol/min/ug enzyme {ECO:0000269|PubMed:29605550};
CC       Temperature dependence:
CC         Loses its activity after heat treatment.
CC         {ECO:0000269|PubMed:29605550};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29605550}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:29605550}.
CC   -!- PTM: Is not glycosylated. {ECO:0000269|PubMed:29605550}.
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   AlphaFoldDB; P0DPT0; -.
DR   SMR; P0DPT0; -.
DR   BRENDA; 3.1.1.32; 16387.
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:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00707; Pancreat_lipase_like; 1.
DR   Gene3D; 3.40.50.1820; -; 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; PTHR11610; 1.
DR   Pfam; PF00151; Lipase; 1.
DR   PRINTS; PR00825; DOLALLERGEN.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Allergen; Cytolysis; Direct protein sequencing; Disulfide bond; Hemolysis;
KW   Hydrolase; Lipid degradation; Lipid metabolism; Secreted.
FT   CHAIN           1..301
FT                   /note="Phospholipase A1 VesT1.02"
FT                   /evidence="ECO:0000269|PubMed:29605550"
FT                   /id="PRO_0000446187"
FT   ACT_SITE        137
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        165
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   ACT_SITE        230
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   DISULFID        87..294
FT                   /evidence="ECO:0000305|PubMed:29605550"
FT   DISULFID        176..245
FT                   /evidence="ECO:0000305|PubMed:29605550"
FT   DISULFID        181..262
FT                   /evidence="ECO:0000305|PubMed:29605550"
FT   DISULFID        219..228
FT                   /evidence="ECO:0000305|PubMed:29605550"
FT   DISULFID        240..246
FT                   /evidence="ECO:0000305|PubMed:29605550"
FT   DISULFID        267..269
FT                   /evidence="ECO:0000305|PubMed:29605550"
FT   CONFLICT        9
FT                   /note="D -> M (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305|PubMed:29605550"
SQ   SEQUENCE   301 AA;  33307 MW;  A3859BD1A5A91774 CRC64;
     FLPIPYSDDT VKMIILTSEN KKHDFYTLDT IKKHNELKES IIKHQVAFIT HGFTSSATAE
     HFLAVAEALL DKGNYLVIMI DWRVAACTNE IAGVKLAYYN YAVSNTRLVG NYIATVTKML
     VQKYNVPMAN IRLIGHSLGA HISGFAGKKV QELGLGKYSE IIGLDPAGPS FKSQECSQRI
     CETDANYVQI IHTSNHLGTE RTLGTVDFYM NNGKNQPGCG LPIIGETCSH TRAVKYFTEC
     IRHECCLIGV PQSKNPQPVS KCTRNECVCV GLNAKTYPKT GSFYVPVESK APYCNNKGKK
     I