ID   PA21_BOTIN              Reviewed;         138 AA.
AC   Q8QG87;
DT   28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-NOV-2008, entry version 44.
DE   RecName: Full=Phospholipase A2 BITP01A;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   AltName: Full=BinTX-I;
DE   Flags: Precursor;
OS   Bothrops insularis (Island jararaca) (Queimada jararaca).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea;
OC   Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=8723;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   MEDLINE=22347338; PubMed=12459276; DOI=10.1016/S0378-1119(02)01080-6;
RA   Junqueira-de-Azevedo I.L.M., Ho P.L.;
RT   "A survey of gene expression and diversity in the venom glands of the
RT   pitviper snake Bothrops insularis through the generation of expressed
RT   sequence tags (ESTs).";
RL   Gene 299:279-291(2002).
RN   [2]
RP   PROTEIN SEQUENCE OF 17-138, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=17140721; DOI=10.1016/j.biochi.2006.10.006;
RA   Cogo J.C., Lilla S., Souza G.H.M.F., Hyslop S., de Nucci G.;
RT   "Purification, sequencing and structural analysis of two acidic
RT   phospholipases A2 from the venom of Bothrops insularis (jararaca
RT   ilhoa).";
RL   Biochimie 88:1947-1959(2006).
CC   -!- FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-
CC       acyl groups in 3-sn-phosphoglycerides. Induces edema in mice,
CC       produces neuromuscular blockade in chick biventer cervicis,
CC       increases CK release and produces myonecrosis.
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   -!- MASS SPECTROMETRY: Mass=13975; Method=Electrospray; Range=17-138;
CC       Source=PubMed:17140721;
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II
CC       subfamily.
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DR   EMBL; AF490535; AAM09694.1; -; mRNA.
DR   HSSP; P14418; 1M8R.
DR   HOVERGEN; Q8QG87; -.
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   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Hydrolase; Lipid degradation;
KW   Metal-binding; Secreted; Signal; Toxin.
FT   SIGNAL        1     16
FT   CHAIN        17    138       Phospholipase A2 BITP01A.
FT                                /FTId=PRO_0000022820.
FT   ACT_SITE     63     63       By similarity.
FT   ACT_SITE    105    105       By similarity.
FT   METAL        43     43       Calcium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        45     45       Calcium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        47     47       Calcium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        64     64       Calcium (By similarity).
FT   DISULFID     42    131       By similarity.
FT   DISULFID     44     60       By similarity.
FT   DISULFID     59    111       By similarity.
FT   DISULFID     65    138       By similarity.
FT   DISULFID     66    104       By similarity.
FT   DISULFID     73     97       By similarity.
FT   DISULFID     91    102       By similarity.
SQ   SEQUENCE   138 AA;  15759 MW;  DFB41FD618A1CE54 CRC64;
     MRTLWIMAVL LVGVEGNLWQ FGKMMNYVMG QSVVYKYFYY GCYCGWGGIG QPRDATDRCC
     FVHDCCYGKV TGCDPKTDSY TYSKENGDVV CGGDDPCKKQ ICECDRVAAT CFRDNKDTYD
     MKYWLYGAKN CQEESEPC
//