ID   PA21B_TRIMU             Reviewed;         122 AA.
AC   Q91506;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 54.
DE   RecName: Full=Phospholipase A2 1;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
OS   Trimeresurus mucrosquamatus (Taiwan habu) (Protobothrops
OS   mucrosquamatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea;
OC   Viperidae; Crotalinae; Protobothrops.
OX   NCBI_TaxID=103944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RA   Tsai I.-H.;
RT   "Cloning and sequencing of an phospholipase A2 from Taiwan habu.";
RL   Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-
CC       acyl groups in 3-sn-phosphoglycerides (By similarity).
CC   -!- CATALYTIC ACTIVITY: Phosphatidylcholine + H(2)O = 1-
CC       acylglycerophosphocholine + a carboxylate.
CC   -!- COFACTOR: Binds 1 calcium ion (By similarity).
CC   -!- SUBUNIT: Homodimer (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 II
CC       subfamily.
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DR   EMBL; X77088; CAA54363.1; -; mRNA.
DR   PIR; S46979; S46979.
DR   HSSP; P51972; 1VAP.
DR   SMR; Q91506; 1-122.
DR   HOVERGEN; Q91506; -.
DR   BRENDA; 3.1.1.4; 19091.
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.
FT   CHAIN         1    122       Phospholipase A2 1.
FT                                /FTId=PRO_0000161705.
FT   ACT_SITE     47     47       By similarity.
FT   ACT_SITE     88     88       By similarity.
FT   METAL        27     27       Calcium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        29     29       Calcium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        31     31       Calcium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        48     48       Calcium (By similarity).
FT   DISULFID     26    115       By similarity.
FT   DISULFID     28     44       By similarity.
FT   DISULFID     43     94       By similarity.
FT   DISULFID     49    122       By similarity.
FT   DISULFID     50     87       By similarity.
FT   DISULFID     57     81       By similarity.
FT   DISULFID     75     85       By similarity.
SQ   SEQUENCE   122 AA;  13615 MW;  CA62DAAE5D284626 CRC64;
     NLWQFENMIM KVAKKSGILS YSAYGCYCGW GGRGTPKDAT DRCCFVHDCC YGKVTGCNPK
     LGKYTYSSEN GDIICGGDGP CKEVCECDRA AAICFRDNLD TYDRKTYWKY PASNCQEDSE
     PC
//