ID   PA2_APIDO               Reviewed;         134 AA.
AC   Q7M4I5;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Phospholipase A2;
DE            Short=PLA2;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   AltName: Allergen=Api d 1;
OS   Apis dorsata (Giant honeybee).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea; Apidae;
OC   Apis.
OX   NCBI_TaxID=7462;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Venom;
RA   Hoffman D.R., Schmidt J.O.;
RL   Submitted (JUL-1999) to the PIR data bank.
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.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- ALLERGEN: Causes an allergic reaction in human. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group III
CC       subfamily. {ECO:0000305}.
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DR   PIR; B59055; B59055.
DR   AlphaFoldDB; Q7M4I5; -.
DR   SMR; Q7M4I5; -.
DR   Allergome; 1282; Api d 1.
DR   Allergome; 3085; Api d 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..134
FT                   /note="Phospholipase A2"
FT                   /id="PRO_0000161723"
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        13
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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..113
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   134 AA;  15246 MW;  2843633DA79ED27B CRC64;
     IIYPGTLWCG HGNVSSSPDE LGRFKHTDSC CRSHDMCPDV MSAGESKHGL TNTASHTRLS
     CDCDDKFYDC LKNSSDTISS YFVGEMYFNI LDTKCYKLEH PVTGCGKRTE GRCLNYTVDK
     SKPKVYQWFD LRKY