ID   PA21B_MICNI             Reviewed;          27 AA.
AC   P21790;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   25-NOV-2008, entry version 51.
DE   RecName: Full=Phospholipase A2 isozyme 1;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   Flags: Fragment;
OS   Micrurus nigrocinctus (Central American coral snake) (Gargantilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea;
OC   Elapidae; Elapinae; Micrurus.
OX   NCBI_TaxID=8635;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Venom;
RA   Mochca-Morales J., Martin B.M., Zamudio F.Z., Possani L.D.;
RT   "Isolation and characterization of three toxic phospholipases from the
RT   venom of the coral snake Micrurus nigrocinctus.";
RL   Toxicon 28:616-617(1990).
CC   -!- FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-
CC       acyl groups in 3-sn-phosphoglycerides. Inhibits neuromuscular
CC       transmission by blocking acetylcholine release from the nerve
CC       termini. Acts presynaptically.
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   PIR; A35948; A35948.
DR   HSSP; P00598; 1POA.
DR   HOVERGEN; P21790; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0042734; C:presynaptic membrane; 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:0009405; P:pathogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0007268; P:synaptic transmission; 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   PROSITE; PS00119; PA2_ASP; PARTIAL.
DR   PROSITE; PS00118; PA2_HIS; PARTIAL.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Hydrolase; Lipid degradation;
KW   Neurotoxin; Presynaptic neurotoxin; Secreted; Toxin.
FT   CHAIN         1    >27       Phospholipase A2 isozyme 1.
FT                                /FTId=PRO_0000161658.
FT   NON_TER      27     27
SQ   SEQUENCE   27 AA;  3314 MW;  38637ECA600F49A0 CRC64;
     NLYQFKNMIQ CTTKRSVLEF MEYGCYC
//