ID   PA216_AUSSU             Reviewed;         152 AA.
AC   Q9PUG8;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-NOV-2008, entry version 46.
DE   RecName: Full=Phospholipase A2 isozyme S16-19;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   AltName: Full=ASPLA16;
DE   Flags: Precursor;
OS   Austrelaps superbus (Australian copperhead).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea;
OC   Elapidae; Acanthophiinae; Austrelaps.
OX   NCBI_TaxID=29156;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   MEDLINE=20166950; PubMed=10700385; DOI=10.1006/abbi.1999.1672;
RA   Singh S.B., Armugam A., Kini R.M., Jeyaseelan K.;
RT   "Phospholipase A(2) with platelet aggregation inhibitor activity from
RT   Austrelaps superbus venom: protein purification and cDNA cloning.";
RL   Arch. Biochem. Biophys. 375:289-303(2000).
CC   -!- FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-
CC       acyl groups in 3-sn-phosphoglycerides. Inhibits collagen-induced
CC       platelet aggregation (By similarity).
CC   -!- CATALYTIC ACTIVITY: Phosphatidylcholine + H(2)O = 1-
CC       acylglycerophosphocholine + a carboxylate.
CC   -!- COFACTOR: Calcium (Probable).
CC   -!- SUBCELLULAR LOCATION: Secreted (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- PTM: This enzyme lacks one of the seven disulfide bonds found in
CC       similar PA2 proteins.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I
CC       subfamily.
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DR   EMBL; AF184142; AAD56409.1; -; mRNA.
DR   HSSP; P80966; 1GP7.
DR   HOVERGEN; Q9PUG8; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004623; F:phospholipase A2 activity; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:InterPro.
DR   GO; GO:0009405; P:pathogenesis; 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; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Calcium; Hydrolase; Lipid degradation; Metal-binding; Secreted;
KW   Signal; Toxin.
FT   SIGNAL        1     19       Potential.
FT   PROPEP       20     27       Potential.
FT                                /FTId=PRO_0000022815.
FT   CHAIN        28    152       Phospholipase A2 isozyme S16-19.
FT                                /FTId=PRO_0000022816.
FT   ACT_SITE     75     75       By similarity.
FT   ACT_SITE    126    126       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    104       By similarity.
FT   DISULFID     54    151       By similarity.
FT   DISULFID     71    132       By similarity.
FT   DISULFID     78    125       By similarity.
FT   DISULFID     88    118       By similarity.
FT   DISULFID    111    123       By similarity.
SQ   SEQUENCE   152 AA;  16690 MW;  5C5E4EE5C4C33FDD CRC64;
     MYPAHLLVLL AVCVSLLGAS NIPLPSLDFE QFGKMIQCTI PCEESCLAYM DYGCYCGPGG
     SGTPLDELDR CRQTHDNCYA EAGKLPACKA MLSEPYNDTY SYGCIERQLT CNDDNDECKA
     FICNCDRAAV ICFSGAPYND SNYDIGTIEH CK
//