ID   PA23_HELSU              Reviewed;         143 AA.
AC   P16354; P80004; P80005;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 3.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Phospholipase A2 isozymes PA3A/PA3B/PA5;
DE            Short=PLA2;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
OS   Heloderma suspectum (Gila monster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Anguimorpha; Neoanguimorpha; Helodermatidae; Heloderma.
OX   NCBI_TaxID=8554;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Venom;
RX   PubMed=2013276; DOI=10.1111/j.1432-1033.1991.tb15847.x;
RA   Vandermeers A., Vandermeers-Piret M.-C., Vigneron L., Rathe J.,
RA   Stievenart M., Christophe J.;
RT   "Differences in primary structure among five phospholipases A2 from
RT   Heloderma suspectum.";
RL   Eur. J. Biochem. 196:537-544(1991).
RN   [2]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Venom;
RX   PubMed=2480893; DOI=10.1111/j.1432-1033.1989.tb15172.x;
RA   Gomez F., Vandermeers A., Vandermeers-Piret M.-C., Herzog R., Rathe J.,
RA   Stievenart M., Winand J., Christophe J.;
RT   "Purification and characterization of five variants of phospholipase A2 and
RT   complete primary structure of the main phospholipase A2 variant in
RT   Heloderma suspectum (Gila monster) venom.";
RL   Eur. J. Biochem. 186:23-33(1989).
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 per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MISCELLANEOUS: The sequence of isozyme pa3b is shown.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group III
CC       subfamily. {ECO:0000305}.
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DR   PIR; S14764; PSGHA5.
DR   AlphaFoldDB; P16354; -.
DR   SMR; P16354; -.
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   Calcium; Direct protein sequencing; Disulfide bond; Hydrolase;
KW   Lipid degradation; Lipid metabolism; Metal-binding; Secreted.
FT   CHAIN           1..143
FT                   /note="Phospholipase A2 isozymes PA3A/PA3B/PA5"
FT                   /id="PRO_0000161648"
FT   ACT_SITE        36
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
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         14
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         37
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   DISULFID        11..33
FT                   /evidence="ECO:0000250"
FT   DISULFID        32..72
FT                   /evidence="ECO:0000250"
FT   DISULFID        39..65
FT                   /evidence="ECO:0000250"
FT   VARIANT         142..143
FT                   /note="Missing (in isozyme PA3A)"
FT   VARIANT         143
FT                   /note="Missing (in isozyme PA5)"
SQ   SEQUENCE   143 AA;  16048 MW;  75A3FFA0FA1CC9A7 CRC64;
     GAFIMPGTLW CGAGNAASDY SQLGTEKDTD MCCRDHDHCE NWISALEYKH GMRNYYPSTI
     SHCDCDNQFR SCLMKLKDGT ADYVGQTYFN VLKIPCFELE EGEGCVDWNF WLECTESKIM
     PVAKLVSAAP YQAQAETQSG EGR