ID   PA2B2_NOTSC             Reviewed;         145 AA.
AC   P08873;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   02-SEP-2026, entry version 119.
DE   RecName: Full=Basic phospholipase A2 notechis 11'2;
DE            Short=svPLA2;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   Flags: Precursor;
OS   Notechis scutatus scutatus (Eastern tiger snake) (Naja scutata scutata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Hydrophiinae; Notechis.
OX   NCBI_TaxID=70142;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=3174443; DOI=10.1093/nar/16.18.9049;
RA   Ducancel F., Guignery Frelat G., Menez A., Boulain J.-C., Bouchier C.;
RT   "Complete amino acid sequence of a PLA2 from the tiger snake Notechis
RT   scutatus scutatus as deduced from a complementary DNA.";
RL   Nucleic Acids Res. 16:9049-9049(1988).
RN   [2]
RP   PROTEIN SEQUENCE OF 28-145.
RC   TISSUE=Venom;
RX   PubMed=1761049; DOI=10.1111/j.1432-1033.1991.tb16399.x;
RA   Bouchier C., Boyot P., Tesson F., Tremeau O., Bouet F., Hodgson D.,
RA   Boulain J.-C., Menez A.;
RT   "Notechis 11'2, a non-toxic phospholipase A2 from the venom of Notechis
RT   scutatus scutatus.";
RL   Eur. J. Biochem. 202:493-500(1991).
CC   -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that has no lethal
CC       activity. 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   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC       D49 sub-subfamily. {ECO:0000305}.
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DR   EMBL; X12605; CAA31125.1; -; mRNA.
DR   PIR; S01390; S01390.
DR   AlphaFoldDB; P08873; -.
DR   SMR; P08873; -.
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; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..27
FT                   /evidence="ECO:0000269|PubMed:1761049"
FT                   /id="PRO_0000022938"
FT   CHAIN           28..145
FT                   /note="Basic phospholipase A2 notechis 11'2"
FT                   /id="PRO_0000022939"
FT   ACT_SITE        75
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        119
FT                   /evidence="ECO:0000250"
FT   BINDING         55
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         57
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         59
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         76
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   DISULFID        38..98
FT                   /evidence="ECO:0000250"
FT   DISULFID        54..144
FT                   /evidence="ECO:0000250"
FT   DISULFID        56..72
FT                   /evidence="ECO:0000250"
FT   DISULFID        71..125
FT                   /evidence="ECO:0000250"
FT   DISULFID        78..118
FT                   /evidence="ECO:0000250"
FT   DISULFID        87..111
FT                   /evidence="ECO:0000250"
FT   DISULFID        105..116
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   145 AA;  15903 MW;  3F508029C6E0F001 CRC64;
     MYPAHLLVLL TVCVSLLEAS SIPARPLNLY QFGNMIQCAN HGRRPTLAYA DYGCYCGAGG
     SGTPVDELDR CCKAHDDCYG EAGKKGCYPT LTLYSWQCIE KTPTCNSKTG CERSVCDCDA
     TAAKCFAKAP YNKKNYNIDT EKRCQ
//