ID   PA2H_POLOC              Reviewed;          58 AA.
AC   P0DUN9;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   02-JUN-2021, sequence version 1.
DT   25-MAY-2022, entry version 4.
DE   RecName: Full=Basic phospholipase A2 homolog PocTX {ECO:0000303|PubMed:29467796};
DE   AltName: Full=Lys49 PLA2-like;
DE   Flags: Fragment;
OS   Polybia occidentalis (Paper wasp).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC   Vespidae; Polistinae; Epiponini; Polybia.
OX   NCBI_TaxID=91432;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=29467796; DOI=10.1186/s40409-018-0143-1;
RA   Diniz-Sousa R., Kayano A.M., Caldeira C.A., Simoes-Silva R., Monteiro M.C.,
RA   Moreira-Dill L.S., Grabner F.P., Calderon L.A., Zuliani J.P., Stabeli R.G.,
RA   Soares A.M.;
RT   "Biochemical characterization of a phospholipase A2 homologue from the
RT   venom of the social wasp Polybia occidentalis.";
RL   J. Venom. Anim. Toxins Incl. Trop. Dis. 24:5-5(2018).
CC   -!- FUNCTION: Wasp venom phospholipase A2 homolog that lacks enzymatic
CC       activity. {ECO:0000269|PubMed:29467796}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29467796}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:29467796}.
CC   -!- MASS SPECTROMETRY: Mass=13896.47; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:29467796};
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC       K49 sub-subfamily. {ECO:0000305}.
CC   -!- CAUTION: Does not bind calcium as one of the calcium-binding sites is
CC       lost (Asp->Lys which corresponds to 'Lys-49' in the current
CC       nomenclature). {ECO:0000305}.
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DR   AlphaFoldDB; P0DUN9; -.
DR   SMR; P0DUN9; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004623; F:phospholipase A2 activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:InterPro.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR   Gene3D; 1.20.90.10; -; 1.
DR   InterPro; IPR001211; PLipase_A2.
DR   InterPro; IPR016090; PLipase_A2_dom.
DR   InterPro; IPR036444; PLipase_A2_dom_sf.
DR   InterPro; IPR033113; PLipase_A2_His_AS.
DR   PANTHER; PTHR11716; PTHR11716; 1.
DR   Pfam; PF00068; Phospholip_A2_1; 1.
DR   PRINTS; PR00389; PHPHLIPASEA2.
DR   SMART; SM00085; PA2c; 1.
DR   SUPFAM; SSF48619; SSF48619; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Myotoxin; Secreted; Toxin.
FT   CHAIN           1..>58
FT                   /note="Basic phospholipase A2 homolog PocTX"
FT                   /evidence="ECO:0000269|PubMed:29467796"
FT                   /id="PRO_0000452900"
FT   DISULFID        27..?
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        29..45
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        44..?
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        50..?
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        51..?
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        58..?
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   NON_TER         58
FT                   /evidence="ECO:0000305|PubMed:29467796"
SQ   SEQUENCE   58 AA;  6310 MW;  09C394D9EC1E2FB2 CRC64;
     SLFELEGKMI LQETGKNPAK SYGVYGCNCG VGGRGKPKDA TDRCCYVHKC CYKKLTGC