ID   PA21_HEMHA              Reviewed;         119 AA.
AC   P00595;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   04-NOV-2008, entry version 66.
DE   RecName: Full=Phospholipase A2 isozyme DE-1;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
OS   Hemachatus haemachatus (Ringhals) (Sepedon haemachatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea;
OC   Elapidae; Elapinae; Hemachatus.
OX   NCBI_TaxID=8626;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Venom;
RX   MEDLINE=77245910; PubMed=1236145;
RA   Joubert F.J.;
RT   "Hemachatus haemachatus (Ringhals) venom. Purification, some
RT   properties and amino-acid sequence of phospholipase A (fraction DE-
RT   I).";
RL   Eur. J. Biochem. 52:539-544(1975).
RN   [2]
RP   ACTIVE SITE.
RX   MEDLINE=81177921; PubMed=7222060; DOI=10.1016/0041-0101(80)90081-1;
RA   Yang C.C., King K.;
RT   "Chemical modification of the histidine residue in phospholipase A2
RT   from the Hemachatus haemachatus snake venom.";
RL   Toxicon 18:529-547(1980).
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   -!- TOXIC DOSE: LD(50) is 8.6 mg/kg by intravenous injection.
CC   -!- MISCELLANEOUS: Two forms of phospholipase A2 are found in Ringhals
CC       venom.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family.
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DR   PIR; A00738; PSRIA.
DR   HSSP; P15445; 1A3D.
DR   SMR; P00595; 1-119.
DR   HOVERGEN; P00595; -.
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   Calcium; Direct protein sequencing; Hydrolase; Lipid degradation;
KW   Metal-binding; Secreted.
FT   CHAIN         1    119       Phospholipase A2 isozyme DE-1.
FT                                /FTId=PRO_0000161649.
FT   ACT_SITE     93     93       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   SITE         47     47       Activity and toxicity lost upon
FT                                alkylation, Ca(2+) markedly slows
FT                                inactivation.
FT   DISULFID     11     71       By similarity.
FT   DISULFID     26    118       By similarity.
FT   DISULFID     28     44       By similarity.
FT   DISULFID     43     99       By similarity.
FT   DISULFID     50     92       By similarity.
FT   DISULFID     60     85       By similarity.
FT   DISULFID     78     90       By similarity.
SQ   SEQUENCE   119 AA;  13519 MW;  4DEDD044EFA97035 CRC64;
     NLYQFKNMIK CTVPSRSWWH FANYGCYCGR GGSGTPVDDL DRCCQTHDNC YSDAEKISGC
     RPYFKTYSYD CTKGKLTCKE GNNECAAFVC KCDRLAAICF AGAHYNDNNN YIDLARHCQ
//