ID   PA21_TROCA              Reviewed;         151 AA.
AC   Q45Z30;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 28.
DE   RecName: Full=Phospholipase A2, acidic 1;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase 1;
DE            Short=PLA-1;
DE   Flags: Precursor;
OS   Tropidechis carinatus (Australian rough-scaled snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea;
OC   Elapidae; Notechinae; Tropidechis.
OX   NCBI_TaxID=100989;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=16261251; DOI=10.1007/s00018-005-5384-9;
RA   St Pierre L., Woods R., Earl S.T.H., Masci P.P., Lavin M.F.;
RT   "Identification and analysis of venom gland-specific genes from the
RT   coastal taipan (Oxyuranus scutellatus) and related species.";
RL   Cell. Mol. Life Sci. 62:2679-2693(2005).
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.
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; DQ085836; AAZ22654.1; -; mRNA.
DR   HOVERGEN; Q45Z30; -.
DR   BRENDA; 3.1.1.4; 295067.
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: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; Disulfide bond; Hydrolase; Lipid degradation; Metal-binding;
KW   Secreted; Signal; Toxin.
FT   SIGNAL        1     27       Potential.
FT   CHAIN        28    151       Phospholipase A2, acidic 1.
FT                                /FTId=PRO_0000043276.
FT   ACT_SITE     75     75       By similarity.
FT   ACT_SITE    126    126       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    104       By similarity.
FT   DISULFID     54    151       By similarity.
FT   DISULFID     56     72       By similarity.
FT   DISULFID     71    132       By similarity.
FT   DISULFID     78    125       By similarity.
FT   DISULFID     88    118       By similarity.
FT   DISULFID    111    123       By similarity.
SQ   SEQUENCE   151 AA;  16921 MW;  663C0EF2DEB9935A CRC64;
     MYPAHLLVLL AVCVSLLGAA SIPARPLNLY QFGNMIQCAN HGRRPTRHYM DYGCYCGKGG
     SGTPVDELDR CCQTHDDCYG EAEKLPACNY MMSGPYYNTY SYECNDGELT CKDNNDECKA
     FICNCDRTAA ICFARTPYND ANWNIDTKTR C
//