ID   PA21_ECHCO              Reviewed;         138 AA.
AC   Q90ZZ9;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-NOV-2008, entry version 41.
DE   RecName: Full=Phospholipase A2 EC1;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   Flags: Precursor;
OS   Echis coloratus (Carpet viper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea;
OC   Viperidae; Viperinae; Echis.
OX   NCBI_TaxID=64175;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Kordis D., Gubensek F.;
RT   "Evolutionary relationships of Viperidae phospholipase A2 genes
RT   inferred from intron sequences.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: Phosphatidylcholine + H(2)O = 1-
CC       acylglycerophosphocholine + a carboxylate.
CC   -!- COFACTOR: Binds 1 calcium ion (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted (By similarity).
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II
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   EMBL; AF253050; AAK49823.1; -; Genomic_DNA.
DR   HSSP; P04084; 1VPI.
DR   HOVERGEN; Q90ZZ9; -.
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   3: Inferred from homology;
KW   Calcium; Hydrolase; Lipid degradation; Metal-binding; Secreted;
KW   Signal.
FT   SIGNAL        1     16       By similarity.
FT   CHAIN        17    138       Phospholipase A2 EC1.
FT                                /FTId=PRO_0000022868.
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;  15770 MW;  1A5D9F17FDAA9D56 CRC64;
     MRTLWIVAVW LMSVEGNLYQ FGKMIKNKTG KPAMFSYSAY GCYCGWGGQG KPQDASDRCC
     FVHDCCYTRV NDCSPKMTSY SYSFENRDII CGDDDSCRKA VCECDREAAI CLGENVNTYD
     EKYRFYSSSH CVEETEQC
//