ID   PA2_BOMTE               Reviewed;         136 AA.
AC   P82971;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Phospholipase A2;
DE            Short=PLA2;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   AltName: Allergen=Bom t 1;
OS   Bombus terrestris (Buff-tailed bumblebee) (Apis terrestris).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea; Apidae;
OC   Bombus; Bombus.
OX   NCBI_TaxID=30195;
RN   [1]
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND ALLERGEN.
RC   TISSUE=Venom;
RX   PubMed=11692115; DOI=10.1067/mai.2001.119029;
RA   Hoffman D.R., El-Choufani S.E., Smith M.M., de Groot H.;
RT   "Occupational allergy to bumblebees: allergens of Bombus terrestris.";
RL   J. Allergy Clin. Immunol. 108:855-860(2001).
CC   -!- FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC       groups in 3-sn-phosphoglycerides.
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         Evidence={ECO:0000255|PROSITE-ProRule:PRU10035};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11692115}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:11692115}.
CC   -!- ALLERGEN: Causes an allergic reaction in human.
CC       {ECO:0000269|PubMed:11692115}.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
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DR   AlphaFoldDB; P82971; -.
DR   SMR; P82971; -.
DR   Allergome; 155; Bom t 1.
DR   Allergome; 3159; Bom t 1.0101.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR   GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR   Gene3D; 1.20.90.10; -; 1.
DR   InterPro; IPR016090; PLipase_A2_dom.
DR   InterPro; IPR036444; PLipase_A2_dom_sf.
DR   InterPro; IPR033113; PLipase_A2_His_AS.
DR   Pfam; PF05826; Phospholip_A2_2; 1.
DR   SMART; SM00085; PA2c; 1.
DR   SUPFAM; SSF48619; SSF48619; 1.
DR   PROSITE; PS00118; PA2_HIS; 1.
PE   1: Evidence at protein level;
KW   Allergen; Calcium; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding; Secreted.
FT   CHAIN           1..136
FT                   /note="Phospholipase A2"
FT                   /id="PRO_0000161724"
FT   ACT_SITE        34
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT   ACT_SITE        64
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT   BINDING         8
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         10
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         12
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         35
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        16
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   DISULFID        9..31
FT                   /evidence="ECO:0000250"
FT   DISULFID        30..70
FT                   /evidence="ECO:0000250"
FT   DISULFID        37..63
FT                   /evidence="ECO:0000250"
FT   DISULFID        61..95
FT                   /evidence="ECO:0000250"
FT   DISULFID        105..117
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   136 AA;  15546 MW;  07797BDDEC74F20E CRC64;
     IIFPGTLWCG NGNLANGTNQ LGSWKETDSC CRTHDMCPDL IEAHGSKHGL TNAADYTRLS
     CECDEEFRRC LHNSGDTVSA GFVGRTYFTV LHTQCFRLDY PIVKCKVKST ILHRSKCYDF
     ETFAPKKYQW FDVLQY