ID   PA213_AUSSU             Reviewed;         146 AA.
AC   Q9PUH1;
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 S14-72F;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   AltName: Full=ASPLA13;
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; AF184139; AAD56562.1; -; mRNA.
DR   HSSP; P00608; 1AE7.
DR   SMR; Q9PUH1; 28-146.
DR   HOVERGEN; Q9PUH1; -.
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_0000022809.
FT   CHAIN        28    146       Phospholipase A2 isozyme S14-72F.
FT                                /FTId=PRO_0000022810.
FT   ACT_SITE     75     75       By similarity.
FT   ACT_SITE    120    120       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    145       By similarity.
FT   DISULFID     56     72       By similarity.
FT   DISULFID     71    126       By similarity.
FT   DISULFID     78    119       By similarity.
FT   DISULFID     87    112       By similarity.
FT   DISULFID    105    117       By similarity.
SQ   SEQUENCE   146 AA;  16280 MW;  CABA49837A25186B CRC64;
     MYPAHLLVLL AVCVSLLGAA SIPPQPLNLV QFSYLIQCAN HGSRATWHYT DYGCYCGSGG
     SGTPVDELDR CCQTHDNCYG EAEKKGCYPK MLAYDYYCGG DGPYCRNIKK ECQRFVCDCD
     VEAAKCFARA PYNDANWNID TKKRCQ
//