ID   PA2BE_PSEAU             Reviewed;         118 AA.
AC   P20257;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   02-SEP-2026, entry version 117.
DE   RecName: Full=Basic phospholipase A2 PA-15;
DE            Short=svPLA2;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
OS   Pseudechis australis (Mulga snake) (King brown snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Hydrophiinae; Pseudechis.
OX   NCBI_TaxID=8670;
RN   [1]
RP   PROTEIN SEQUENCE, AND TOXIC DOSE.
RC   TISSUE=Venom;
RX   PubMed=2343466; DOI=10.1016/0041-0101(90)90068-i;
RA   Takasaki C., Yutani F., Kajiyashiki T.;
RT   "Amino acid sequences of eight phospholipases A2 from the venom of
RT   Australian king brown snake, Pseudechis australis.";
RL   Toxicon 28:329-339(1990).
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, ECO:0000255|PROSITE-
CC         ProRule:PRU10036};
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   -!- TOXIC DOSE: LD(50) is 3.4 mg/kg by intravenous injection.
CC       {ECO:0000269|PubMed:2343466}.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC       D49 sub-subfamily. {ECO:0000305}.
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DR   PIR; H34860; H34860.
DR   AlphaFoldDB; P20257; -.
DR   SMR; P20257; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004623; F:A2-type glycerophospholipase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005543; F:phospholipid binding; IEA:TreeGrafter.
DR   GO; GO:0050482; P:arachidonate secretion; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:InterPro.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR   CDD; cd00125; PLA2c; 1.
DR   FunFam; 1.20.90.10:FF:000007; Acidic phospholipase A2; 1.
DR   Gene3D; 1.20.90.10; Phospholipase A2 domain; 1.
DR   InterPro; IPR001211; PLA2.
DR   InterPro; IPR016090; PLA2-like_dom.
DR   InterPro; IPR033112; PLA2_Asp_AS.
DR   InterPro; IPR033113; PLA2_histidine.
DR   InterPro; IPR036444; PLipase_A2_dom_sf.
DR   PANTHER; PTHR11716:SF51; PHOSPHOLIPASE A2; 1.
DR   PANTHER; PTHR11716; PHOSPHOLIPASE A2 FAMILY MEMBER; 1.
DR   Pfam; PF00068; Phospholip_A2_1; 1.
DR   PRINTS; PR00389; PHPHLIPASEA2.
DR   SMART; SM00085; PA2c; 1.
DR   SUPFAM; SSF48619; Phospholipase A2, PLA2; 1.
DR   PROSITE; PS00119; PA2_ASP; 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..118
FT                   /note="Basic phospholipase A2 PA-15"
FT                   /id="PRO_0000161690"
FT   ACT_SITE        48
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        92
FT                   /evidence="ECO:0000250"
FT   BINDING         28
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         30
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         32
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         49
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   DISULFID        11..71
FT                   /evidence="ECO:0000250"
FT   DISULFID        27..117
FT                   /evidence="ECO:0000250"
FT   DISULFID        29..45
FT                   /evidence="ECO:0000250"
FT   DISULFID        44..98
FT                   /evidence="ECO:0000250"
FT   DISULFID        51..91
FT                   /evidence="ECO:0000250"
FT   DISULFID        60..84
FT                   /evidence="ECO:0000250"
FT   DISULFID        78..89
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   118 AA;  13200 MW;  EA0FDFC13D91AC9A CRC64;
     NILQFRKMIQ CANKGSRAAW HYLDYGCYCG PGGRGTPVDE LDRCCKIHDD CYIEAGKDGC
     YPKLTWYSWQ CTGDAPTCNP KSKCKDFVCA CDAAAAKCFA KAAYNKANWN IDTKTRCK
//