ID   PA21B_ACAAN             Reviewed;         119 AA.
AC   P81236;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   16-JUN-2009, entry version 54.
DE   RecName: Full=Phospholipase A2;
DE            EC=3.1.1.4;
DE   AltName: Full=Acanthin I;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
OS   Acanthophis antarcticus (Common death adder).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea;
OC   Elapidae; Acanthophiinae; Acanthophis.
OX   NCBI_TaxID=8605;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Venom;
RX   MEDLINE=98303724; PubMed=9637731; DOI=10.1006/abbi.1998.0685;
RA   Chow G., Subburaju S., Kini R.M.;
RT   "Purification, characterization, and amino acid sequence determination
RT   of acanthins, potent inhibitors of platelet aggregation from
RT   Acanthophis antarcticus (common death adder) venom.";
RL   Arch. Biochem. Biophys. 354:232-238(1998).
CC   -!- FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-
CC       acyl groups in 3-sn-phosphoglycerides. Exhibits antiplatelet
CC       activity.
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   HSSP; P00609; 2NOT.
DR   HOVERGEN; P81236; -.
DR   BRENDA; 3.1.1.4; 291618.
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.
FT   CHAIN         1    119       Phospholipase A2.
FT                                /FTId=PRO_0000161591.
FT   ACT_SITE     48     48       By similarity.
FT   ACT_SITE     93     93       By similarity.
FT   METAL        28     28       Calcium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        30     30       Calcium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        32     32       Calcium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        49     49       Calcium (By similarity).
FT   DISULFID     11     71       By similarity.
FT   DISULFID     27    118       By similarity.
FT   DISULFID     29     45       By similarity.
FT   DISULFID     44     99       By similarity.
FT   DISULFID     51     92       By similarity.
FT   DISULFID     60     85       By similarity.
FT   DISULFID     78     90       By similarity.
SQ   SEQUENCE   119 AA;  12857 MW;  229241793FA826F7 CRC64;
     DLFQFGGMIG CANKGARSWL SYVNYGCYCG WGGSGTPVDE LDRCCQIHDN CYGEAEKKQC
     GPKMTSYSWK CANDVPVCND SKSACKGFVC DCDAAAAKCF AKAPYNKNNI GIGSKTRCQ
//