ID   PA22_BUNFL              Reviewed;         147 AA.
AC   Q7T2Q4;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   16-JUN-2009, entry version 32.
DE   RecName: Full=Phospholipase A2-2;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   AltName: Full=PA2-II;
DE   Flags: Precursor;
OS   Bungarus flaviceps flaviceps (Red-headed krait).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea;
OC   Elapidae; Bungarinae; Bungarus.
OX   NCBI_TaxID=8615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=16458338; DOI=10.1016/j.toxicon.2005.12.004;
RA   Yanoshita R., Ogawa Y., Murayama N., Omori-Satoh T., Saguchi K.,
RA   Higuchi S., Khow O., Chanhome L., Samejima Y., Sitprija V.;
RT   "Molecular cloning of the major lethal toxins from two kraits
RT   (Bungarus flaviceps and Bungarus candidus).";
RL   Toxicon 47:416-424(2006).
CC   -!- FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-
CC       acyl groups in 3-sn-phosphoglycerides.
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 (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; AB112360; BAC77656.1; -; mRNA.
DR   HSSP; Q9DF33; 1M8T.
DR   HOVERGEN; Q7T2Q4; -.
DR   BRENDA; 3.1.1.4; 322414.
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   2: Evidence at transcript level;
KW   Calcium; Disulfide bond; Hydrolase; Lipid degradation; Metal-binding;
KW   Secreted; Signal.
FT   SIGNAL        1     19       Potential.
FT   PROPEP       20     27       By similarity.
FT                                /FTId=PRO_0000271458.
FT   CHAIN        28    147       Phospholipase A2-2.
FT                                /FTId=PRO_5000050836.
FT   ACT_SITE     75     75       By similarity.
FT   ACT_SITE    121    121       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     99       By similarity.
FT   DISULFID     54    146       By similarity.
FT   DISULFID     56     72       By similarity.
FT   DISULFID     71    127       By similarity.
FT   DISULFID     78    120       By similarity.
FT   DISULFID     88    113       By similarity.
FT   DISULFID    106    118       By similarity.
SQ   SEQUENCE   147 AA;  15875 MW;  2A705D44885EDDDC CRC64;
     MNPAHLLVLS AVCVSLLGAA IVPPQPLNLI QFSSLIQCAN GGSRATWHYA DYGCYCGKGG
     GGTPVDELDR CCQTHDNCYG EAEKLTKCSP YYKTYKYDCS EGKLTCNDAP GSCERSVCDC
     DRVAAICFAG APYNDKNFMI NTETNCQ
//