ID   PA20_PSEAU              Reviewed;         118 AA.
AC   P20254;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   25-NOV-2008, entry version 62.
DE   RecName: Full=Phospholipase A2 isozyme PA-10A;
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=90260881; PubMed=2343466; DOI=10.1016/0041-0101(90)90068-I;
RA   Takasaki C., Yutani F., Kajiyashiki T.;
RT   "Amino acid sequences of eight phospholipases A2 from the venom of
RT   Australian king brown snake, Pseudechis australis.";
RL   Toxicon 28:329-339(1990).
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   -!- 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.
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DR   PIR; E34860; E34860.
DR   HSSP; P00608; 1AE7.
DR   SMR; P20254; 1-118.
DR   HOVERGEN; P20254; -.
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: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.
FT   CHAIN         1    118       Phospholipase A2 isozyme PA-10A.
FT                                /FTId=PRO_0000161685.
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;  13027 MW;  884D1D3A6E2B5FCB CRC64;
     NLIQFSNMIQ CANKGSRPSL HYADYGCYCG WGGSGTPVDE LDRCCKVHDD CYDQAGKKGC
     FPKLTLYSWD CTGNVPICNP KSKCKDFVCA CDAAAAKCFA KAPYNKANWN IDTKTRCK
//