ID   PA1_VESVE               Reviewed;         304 AA.
AC   C0HLL3;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   17-JUN-2020, sequence version 1.
DT   25-MAY-2022, entry version 7.
DE   RecName: Full=Phospholipase A1 {ECO:0000305};
DE            EC=3.1.1.32 {ECO:0000250|UniProtKB:P0DMB4};
DE   AltName: Full=Vesp v 1 {ECO:0000303|PubMed:31923175};
OS   Vespa velutina (Asian yellow-legged hornet).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC   Vespidae; Vespinae; Vespa.
OX   NCBI_TaxID=202808 {ECO:0000303|PubMed:31923175};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Venom gland {ECO:0000303|PubMed:25896434};
RX   PubMed=25896434; DOI=10.1038/srep09454;
RA   Liu Z., Chen S., Zhou Y., Xie C., Zhu B., Zhu H., Liu S., Wang W., Chen H.,
RA   Ji Y.;
RT   "Deciphering the venomic transcriptome of killer-wasp Vespa velutina.";
RL   Sci. Rep. 5:9454-9454(2015).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 1-5, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS
RP   SPECTROMETRY, AND GLYCOSYLATION AT ASN-61.
RC   TISSUE=Venom {ECO:0000303|PubMed:25896434};
RX   PubMed=31923175; DOI=10.1371/journal.pone.0225672;
RA   Monsalve R.I., Gutierrez R., Hoof I., Lombardero M.;
RT   "Purification and molecular characterization of phospholipase, antigen 5
RT   and hyaluronidases from the venom of the Asian hornet (Vespa velutina).";
RL   PLoS ONE 15:E0225672-E0225672(2020).
CC   -!- FUNCTION: Catalyzes the hydrolysis of phosphatidylcholine with
CC       phospholipase A1 activity (By similarity). Shows hemolytic activity (By
CC       similarity). {ECO:0000250|UniProtKB:A0A0M3KKW3,
CC       ECO:0000250|UniProtKB:P0DMB4}.
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:0000269|PubMed:31923175}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:31923175}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; C0HLL3; -.
DR   SMR; C0HLL3; -.
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:0006629; P:lipid metabolic process; IEA:InterPro.
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   PRINTS; PR00821; TAGLIPASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW   Secreted.
FT   CHAIN           1..304
FT                   /note="Phospholipase A1"
FT                   /id="PRO_0000449969"
FT   ACT_SITE        140
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   ACT_SITE        168
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   ACT_SITE        233
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   CARBOHYD        61
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT                   ECO:0000269|PubMed:31923175"
FT   DISULFID        6..90
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   DISULFID        179..184
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   DISULFID        222..231
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   DISULFID        248..272
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   DISULFID        249..297
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   DISULFID        265..270
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
SQ   SEQUENCE   304 AA;  33957 MW;  FD482D3F076F3902 CRC64;
     GLLPKCKLVP EQISFILSTR ENRNGVFLTL DSLKKGGILN KSDLSSTQVV FLIHGFISSA
     NNSNYMDMTK ALLEKNDCMV ISIDWRNGAC TNEFQILKFI GYPKAVENTR TVGKYIADFS
     KLLMQKYKVS LANIRLIGHS LGAQIAGFAG KEYQKFKLGK YPEIIGLDPA GPLFKSNDCS
     QRICETDAHY VQIIHTSNNL GTERTLGTVD FYMNNGYNQP GCYYSFIGET CSHTRAVQYF
     TECIRHECCL IGVPQSKNPQ PVSKCTRNEC VCVGLNAKRY PKTGSFYVPV ESKAPYCNNK
     GKKI