ID   PA21B_PSEAU             Reviewed;         118 AA.
AC   P04056;
DT   01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1986, sequence version 1.
DT   04-NOV-2008, entry version 64.
DE   RecName: Full=Phospholipase A2 isozyme PA-11;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
OS   Pseudechis australis (Mulga snake) (King brown snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea;
OC   Elapidae; Acanthophiinae; Pseudechis.
OX   NCBI_TaxID=8670;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Venom;
RX   MEDLINE=85193286; PubMed=3887651; DOI=10.1016/0041-0101(85)90112-6;
RA   Nishida S., Terashima M., Tamiya N.;
RT   "Amino acid sequences of phospholipases A2 from the venom of an
RT   Australian elapid snake (king brown snake, Pseudechis australis).";
RL   Toxicon 23:87-104(1985).
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   -!- TOXIC DOSE: LD(50) is 0.24 mg/kg by intravenous injection.
CC   -!- MISCELLANEOUS: There are many protein components with
CC       phospholipase A2 activity in the Mulga snake venom and some of
CC       them are myotoxic.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I
CC       subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   PIR; A00747; PSSNK1.
DR   HSSP; P00608; 1AE7.
DR   HOVERGEN; P04056; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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.
FT   CHAIN         1    118       Phospholipase A2 isozyme PA-11.
FT                                /FTId=PRO_0000161686.
FT   ACT_SITE     48     48       By similarity.
FT   ACT_SITE     92     92       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    117       By similarity.
FT   DISULFID     29     45       By similarity.
FT   DISULFID     44     98       By similarity.
FT   DISULFID     51     91       By similarity.
FT   DISULFID     60     84       By similarity.
FT   DISULFID     78     89       By similarity.
SQ   SEQUENCE   118 AA;  12966 MW;  F7C90529BB12D5A1 CRC64;
     NLIQFGNMIQ CANKGSRPSL DYADYGCYCG WGGSGTPVDE LDRCCQVHDN CYEQAGKKGC
     FPKLTLYSWK CTGNVPTCNS KPGCKSFVCA CDAAAAKCFA KAPYKKENYN IDTKKRCK
//