ID   PA21B_NAJME             Reviewed;         118 AA.
AC   P00599;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   04-NOV-2008, entry version 71.
DE   RecName: Full=Phospholipase A2 isozyme DE-I;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
OS   Naja melanoleuca (Forest cobra) (Black-lipped cobra).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea;
OC   Elapidae; Elapinae; Naja.
OX   NCBI_TaxID=8643;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Venom;
RX   MEDLINE=75128076; PubMed=1122292;
RA   Joubert F.J.;
RT   "The amino acid sequence of phospholipase A, fractions DE-I and DE-
RT   II.";
RL   Biochim. Biophys. Acta 379:345-359(1975).
RN   [2]
RP   DISULFIDE BONDS.
RX   MEDLINE=75128074; PubMed=1122290;
RA   Joubert F.J., van der Walt S.J.;
RT   "Naja melanoleuca (forest cobra) venom. Purification and some
RT   properties of phospholipases A.";
RL   Biochim. Biophys. Acta 379:317-328(1975).
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 I
CC       subfamily.
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DR   PIR; A00741; PSNJ1W.
DR   PDB; 1OO1; Model; -; A=1-118.
DR   PDBsum; 1OO1; -.
DR   SMR; P00599; 1-118.
DR   HOVERGEN; P00599; -.
DR   GO; GO:0005576; C:extracellular region; 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   1: Evidence at protein level;
KW   3D-structure; Calcium; Direct protein sequencing; Hydrolase;
KW   Lipid degradation; Metal-binding; Secreted.
FT   CHAIN         1    118       Phospholipase A2 isozyme DE-I.
FT                                /FTId=PRO_0000161663.
FT   ACT_SITE     47     47       By similarity.
FT   ACT_SITE     92     92       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     11     72       By similarity.
FT   DISULFID     26    117       By similarity.
FT   DISULFID     28     44       By similarity.
FT   DISULFID     43     98       By similarity.
FT   DISULFID     50     91       By similarity.
FT   DISULFID     60     84       By similarity.
FT   DISULFID     78     89       By similarity.
FT   HELIX         2     12
FT   HELIX        18     22
FT   TURN         25     27
FT   STRAND       28     30
FT   HELIX        39     55
FT   TURN         62     64
FT   STRAND       69     71
FT   STRAND       76     78
FT   HELIX        83    101
FT   HELIX       106    108
FT   HELIX       113    116
SQ   SEQUENCE   118 AA;  13473 MW;  0B2792570FF5D94D CRC64;
     NLYQFKNMIH CTVPNRPWWH FANYGCYCGR GGKGTPVDDL DRCCQIHDKC YDEAEKISGC
     WPYIKTYTYE SCQGTLTCKD GGKCAASVCD CDRVAANCFA RATYNDKNYN IDFNARCQ
//