ID   PAO2_VESOR              Reviewed;         139 AA.
AC   Q7M3V3;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=Orientotoxin-2;
DE            EC=3.1.1.4;
DE   AltName: Full=Orientotoxin II;
DE   AltName: Full=Phospholipase A2;
OS   Vespa orientalis (Oriental hornet).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC   Vespidae; Vespinae; Vespa.
OX   NCBI_TaxID=7447;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Venom;
RX   PubMed=2742606;
RA   Korneev A.S., Salikhov S.I., Tuychibaev M.U.;
RT   "Amino acid sequence of orientotoxin I and orientotoxin II from the hornet
RT   Vespa orientalis venom.";
RL   Bioorg. Khim. 15:127-129(1989).
CC   -!- FUNCTION: Has a highly toxic phospholipase A2 activity.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC         glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC         ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   PIR; JN0427; JN0427.
DR   AlphaFoldDB; Q7M3V3; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Secreted; Toxin.
FT   CHAIN           1..139
FT                   /note="Orientotoxin-2"
FT                   /id="PRO_0000058227"
SQ   SEQUENCE   139 AA;  15389 MW;  1AA0EF523CB843EE CRC64;
     FNPCPYSDDT VKMIILTEQN KKQDFYTLDT IGEHNQFNKL TAKSQVVFIV WQTGIGDAIT
     ARAASGLAML VDKYQMAPVA SDIKLCNAGC YCRPTAIQFA WEHKCVGIRC SDPGVPTDGL
     SGRPHYGETL HKVRSYNGK