ID   PA217_AUSSU             Reviewed;         152 AA.
AC   Q9PUG7;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-NOV-2008, entry version 45.
DE   RecName: Full=Phospholipase A2 isozyme S17-58;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   AltName: Full=ASPLA17;
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   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I
CC       subfamily.
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DR   EMBL; AF184143; AAD56410.1; -; mRNA.
DR   HSSP; P00593; 4BP2.
DR   HOVERGEN; Q9PUG7; -.
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; 1.
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_0000022817.
FT   CHAIN        28    152       Phospholipase A2 isozyme S17-58.
FT                                /FTId=PRO_0000022818.
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     56     72       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;  16641 MW;  0F2BD5BDDCF04FCB CRC64;
     MYPAHLLVLL AVCVSLLGAS NIPLPSLDFE QFGKMIQCTI PCEESCLAYM DYGCYCGPGG
     SGTPSDELDR CCQTHDNCYA EAGKLPACKA MLSEPYNDTY SYSCIERQLT CNDDNDECKA
     FICNCDRAAV ICFSGAPYND SNYDIGTIEH CK
//