ID   PA2AE_NOTSC             Reviewed;         125 AA.
AC   Q9PSN5;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Acidic phospholipase A2 HTe;
DE            Short=svPLA2;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
OS   Notechis scutatus scutatus (Mainland tiger snake) (Common tiger snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Acanthophiinae; Notechis.
OX   NCBI_TaxID=70142;
RN   [1]
RP   PROTEIN SEQUENCE, AND FUNCTION.
RC   TISSUE=Venom;
RX   PubMed=7733680; DOI=10.1006/abbi.1995.1257;
RA   Francis B., Coffield J.A., Simpson L.L., Kaiser I.I.;
RT   "Amino acid sequence of a new type of toxic phospholipase A2 from the venom
RT   of the Australian tiger snake (Notechis scutatus scutatus).";
RL   Arch. Biochem. Biophys. 318:481-488(1995).
CC   -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that blocks neuromuscular
CC       transmission, but that does not produce blockade by virtue of a
CC       selective action on nerve endings. Instead, the toxin acts both on
CC       nerve and on muscle. PLA2 catalyzes the calcium-dependent hydrolysis of
CC       the 2-acyl groups in 3-sn-phosphoglycerides.
CC       {ECO:0000269|PubMed:7733680}.
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   -!- PTM: No glycosylation was detected on this protein.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC       D49 sub-subfamily. {ECO:0000305}.
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DR   PIR; S65624; S65624.
DR   AlphaFoldDB; Q9PSN5; -.
DR   SMR; Q9PSN5; -.
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:UniProtKB-EC.
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:UniProtKB-KW.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR   CDD; cd00125; PLA2c; 1.
DR   Gene3D; 1.20.90.10; -; 1.
DR   InterPro; IPR001211; PLipase_A2.
DR   InterPro; IPR033112; PLipase_A2_Asp_AS.
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.
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; Myotoxin; Neurotoxin;
KW   Secreted; Toxin.
FT   CHAIN           1..125
FT                   /note="Acidic phospholipase A2 HTe"
FT                   /id="PRO_0000161677"
FT   ACT_SITE        48
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        99
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..77
FT                   /evidence="ECO:0000250"
FT   DISULFID        27..124
FT                   /evidence="ECO:0000250"
FT   DISULFID        29..45
FT                   /evidence="ECO:0000250"
FT   DISULFID        44..105
FT                   /evidence="ECO:0000250"
FT   DISULFID        51..98
FT                   /evidence="ECO:0000250"
FT   DISULFID        61..91
FT                   /evidence="ECO:0000250"
FT   DISULFID        84..96
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   125 AA;  14262 MW;  714C56FD730216C4 CRC64;
     NLYQFGNMIQ CANHGRRPTR HYMDYGCYCG KGGSGTPVDE LDRCCQTHDD CYGEAEKLPA
     CNYMMSGPYY NTYSYECNEG ELTCKDNNDE CKAFICNCDR TAAICFARAP YNDANWNIDT
     KTRCQ