ID   PA22_ERIMA              Reviewed;         121 AA.
AC   P24294;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   25-NOV-2008, entry version 57.
DE   RecName: Full=Phospholipase A2 isozyme PLA-2;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
OS   Eristocophis macmahoni (Leaf-nosed viper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea;
OC   Viperidae; Viperinae; Eristocophis.
OX   NCBI_TaxID=8702;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Venom;
RX   MEDLINE=92037623; PubMed=1935962;
RA   Siddiqi A.R., Zaidi Z.H., Joernvall H.;
RT   "Purification and characterization of two highly different group II
RT   phospholipase A2 isozymes from a single viperid (Eristocophis
RT   macmahoni) venom.";
RL   Eur. J. Biochem. 201:675-679(1991).
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   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II
CC       subfamily.
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DR   PIR; S17861; S17861.
DR   HSSP; P81458; 1VIP.
DR   HOVERGEN; P24294; -.
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    121       Phospholipase A2 isozyme PLA-2.
FT                                /FTId=PRO_0000161646.
FT   ACT_SITE     47     47       By similarity.
FT   ACT_SITE     89     89       By similarity.
FT   METAL        27     27       Calcium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        29     29       Calcium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        31     31       Calcium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        48     48       Calcium (By similarity).
FT   DISULFID     26    115       By similarity.
FT   DISULFID     28     44       By similarity.
FT   DISULFID     43     95       By similarity.
FT   DISULFID     49    121       By similarity.
FT   DISULFID     50     88       By similarity.
FT   DISULFID     57     81       By similarity.
FT   DISULFID     75     86       By similarity.
SQ   SEQUENCE   121 AA;  13675 MW;  E4B753CE0D16E845 CRC64;
     NLYQFGEMIS KKTGTFGLFS YVYYGCYCGL GGKGKPLDAT DRCCFVHDCC YGRVNGCNPK
     LSIYSYSFQN GDIVCGDEED CLRDVCECDR VAAICFGENM NTYNKKYVLY SFKECNESDQ
     C
//