ID   PA22_ASPSC              Reviewed;         119 AA.
AC   P07037;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   04-NOV-2008, entry version 64.
DE   RecName: Full=Phospholipase A2 isozyme CM-II;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
OS   Aspidelaps scutatus (Shield-nose snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea;
OC   Elapidae; Acanthophiinae; Aspidelaps.
OX   NCBI_TaxID=8607;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Venom;
RX   MEDLINE=88163080; PubMed=3442602;
RA   Joubert F.J.;
RT   "Purification, some properties of two phospholipases A2 (CM-I and CM-
RT   II) and the amino-acid sequence of CM-II from Aspidelaps scutatus
RT   (shield or shield-nose) venom.";
RL   Biol. Chem. Hoppe-Seyler 368:1597-1602(1987).
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; S00227; S00227.
DR   HSSP; P15445; 1A3D.
DR   SMR; P07037; 1-119.
DR   HOVERGEN; P07037; -.
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 CM-II.
FT                                /FTId=PRO_0000161607.
FT   ACT_SITE     47     47       By similarity.
FT   ACT_SITE     93     93       By similarity.
FT   METAL        27     27       Calcium; via carbonyl oxygen.
FT   METAL        29     29       Calcium; via carbonyl oxygen.
FT   METAL        31     31       Calcium; via carbonyl oxygen.
FT   METAL        48     48       Calcium (By similarity).
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;  13388 MW;  149F380DED335991 CRC64;
     NLYQFKNMIQ CTVPNRSWWH FADYGCFCGY GGSGTPVDEL DRCCQTHDNC YSEAEKLSGC
     KPYIKTYSYD CSQGKLTCSG NDDKCAAFVC NCDRVAAICF AGAPYIDDNY NVDLNERCQ
//