ID   PA20_NOTSC              Reviewed;         145 AA.
AC   P08873;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   16-JUN-2009, entry version 72.
DE   RecName: Full=Phospholipase A2;
DE            EC=3.1.1.4;
DE   AltName: Full=Notechis 11'2;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   Flags: Precursor;
OS   Notechis scutatus scutatus (Mainland tiger snake) (Common tiger
OS   snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea;
OC   Elapidae; Acanthophiinae; Notechis.
OX   NCBI_TaxID=70142;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   MEDLINE=89016586; 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   MEDLINE=92104171; PubMed=1761049;
RX   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
RT   Notechis scutatus scutatus.";
RL   Eur. J. Biochem. 202:493-500(1991).
CC   -!- FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-
CC       acyl groups in 3-sn-phosphoglycerides.
CC   -!- CATALYTIC ACTIVITY: Phosphatidylcholine + H(2)O = 1-
CC       acylglycerophosphocholine + a carboxylate.
CC   -!- COFACTOR: Binds 1 calcium ion per subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I
CC       subfamily.
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DR   EMBL; X12605; CAA31125.1; -; mRNA.
DR   PIR; S01390; S01390.
DR   HSSP; P00608; 1AE7.
DR   SMR; P08873; 28-145.
DR   HOVERGEN; P08873; -.
DR   BRENDA; 3.1.1.4; 292759.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004623; F:phospholipase A2 activity; IEA:EC.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR   InterPro; IPR016090; Phospholipase_A2.
DR   InterPro; IPR013090; Phospholipase_A2_AS.
DR   InterPro; IPR001211; Phospholipase_A2_euk.
DR   Gene3D; G3DSA:1.20.90.10; Phospholipase_A2; 1.
DR   PANTHER; PTHR11716; Phospholipase_A2; 1.
DR   Pfam; PF00068; Phospholip_A2_1; 1.
DR   PRINTS; PR00389; PHPHLIPASEA2.
DR   ProDom; PD000303; PhospholipaseA2; 1.
DR   SMART; SM00085; PA2c; 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; Metal-binding; Secreted; Signal.
FT   SIGNAL        1     19       Potential.
FT   PROPEP       20     27
FT                                /FTId=PRO_0000022938.
FT   CHAIN        28    145       Phospholipase A2.
FT                                /FTId=PRO_0000022939.
FT   ACT_SITE     75     75       By similarity.
FT   ACT_SITE    119    119       By similarity.
FT   METAL        55     55       Calcium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        57     57       Calcium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        59     59       Calcium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        76     76       Calcium (By similarity).
FT   DISULFID     38     98       By similarity.
FT   DISULFID     54    144       By similarity.
FT   DISULFID     56     72       By similarity.
FT   DISULFID     71    125       By similarity.
FT   DISULFID     78    118       By similarity.
FT   DISULFID     87    111       By similarity.
FT   DISULFID    105    116       By similarity.
SQ   SEQUENCE   145 AA;  15903 MW;  3F508029C6E0F001 CRC64;
     MYPAHLLVLL TVCVSLLEAS SIPARPLNLY QFGNMIQCAN HGRRPTLAYA DYGCYCGAGG
     SGTPVDELDR CCKAHDDCYG EAGKKGCYPT LTLYSWQCIE KTPTCNSKTG CERSVCDCDA
     TAAKCFAKAP YNKKNYNIDT EKRCQ
//