ID   PA21B_VIPAP             Reviewed;         138 AA.
AC   Q8JFG0;
DT   28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-NOV-2008, entry version 44.
DE   RecName: Full=Phospholipase A2, B chain;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   AltName: Full=Vaspin chain B;
DE   Flags: Precursor;
OS   Vipera aspis aspis (Aspic viper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea;
OC   Viperidae; Viperinae; Vipera.
OX   NCBI_TaxID=194601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   MEDLINE=22209323; PubMed=12220671; DOI=10.1016/S0014-5793(02)03205-2;
RA   Jan V., Maroun R.C., Robbe-Vincent A., De Haro L., Choumet V.;
RT   "Toxicity evolution of Vipera aspis aspis venom: identification and
RT   molecular modeling of a novel phospholipase A(2) heterodimer
RT   neurotoxin.";
RL   FEBS Lett. 527:263-263(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RX   MEDLINE=22707820; PubMed=12823540;
RX   DOI=10.1046/j.1432-1033.2003.03629.x;
RA   Guillemin I., Bouchier C., Garrigues T., Wisner A., Choumet V.;
RT   "Sequences and structural organization of phospholipase A2 genes from
RT   Vipera aspis aspis, V. aspis zinnikeri and Vipera berus berus venom.
RT   Identification of the origin of a new viper population based on
RT   ammodytin I1 heterogeneity.";
RL   Eur. J. Biochem. 270:2697-2706(2003).
CC   -!- FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-
CC       acyl groups in 3-sn-phosphoglycerides.
CC   -!- FUNCTION: The vaspin complex shows postsynaptic neurotoxicity,
CC       while the isolated vaspin B chain is a presynaptic neurotoxin (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Phosphatidylcholine + H(2)O = 1-
CC       acylglycerophosphocholine + a carboxylate.
CC   -!- COFACTOR: Binds 1 calcium ion per subunit (By similarity).
CC   -!- SUBUNIT: Heterodimer of a weakly toxic basic protein having
CC       phospholipase A2 activity (B chain) and a nontoxic acidic protein
CC       functioning as its inhibitor (A chain).
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; AJ459807; CAD30850.1; -; mRNA.
DR   EMBL; AY243576; AAO86504.1; -; Genomic_DNA.
DR   HSSP; P14420; 1JLT.
DR   HOVERGEN; Q8JFG0; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030550; F:acetylcholine receptor inhibitor activity; 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:0006644; P:phospholipid metabolic process; IEA:InterPro.
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   SMART; SM00085; PA2c; 1.
DR   PROSITE; PS00119; PA2_ASP; 1.
DR   PROSITE; PS00118; PA2_HIS; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Hydrolase; Lipid degradation; Metal-binding; Neurotoxin;
KW   Postsynaptic neurotoxin; Presynaptic neurotoxin; Secreted; Signal;
KW   Toxin.
FT   SIGNAL        1     16       By similarity.
FT   CHAIN        17    138       Phospholipase A2, B chain.
FT                                /FTId=PRO_0000022968.
FT   ACT_SITE     63     63       By similarity.
FT   ACT_SITE    105    105       By similarity.
FT   METAL        43     43       Calcium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        45     45       Calcium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        47     47       Calcium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        64     64       Calcium (By similarity).
FT   DISULFID     42    131       By similarity.
FT   DISULFID     44     60       By similarity.
FT   DISULFID     59    111       By similarity.
FT   DISULFID     65    138       By similarity.
FT   DISULFID     66    104       By similarity.
FT   DISULFID     73     97       By similarity.
FT   DISULFID     91    102       By similarity.
SQ   SEQUENCE   138 AA;  15610 MW;  28C749D504D1EA3E CRC64;
     MRILWIVAVC LIGVEGNLFQ FAKMINGKLG AFSVWNYISY GCYCGWGGQG TPKDATDRCC
     FVHDCCYGRV RGCNPKLAIY SYSFKKGNIV CGKNNGCLRD ICECDRVAAN CFHQNKNTYN
     KNYRFLSSSR CRQTSEQC
//