ID   PA22_BITNA              Reviewed;         119 AA.
AC   P00621;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   04-NOV-2008, entry version 59.
DE   RecName: Full=Phospholipase A2 isozyme CM-II;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
OS   Bitis nasicornis (Rhinoceros adder) (Rhinoceros viper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea;
OC   Viperidae; Viperinae; Bitis.
OX   NCBI_TaxID=8695;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Venom;
RX   MEDLINE=84133812; PubMed=6667925;
RA   Joubert F.J., Townshend G.S., Botes D.P.;
RT   "Snake Venoms. Purification, some properties of two phospholipases A2
RT   (CM-I and CM-II) and the amino-acid sequence of CM-II and Bitis
RT   nasicornis (horned adder) venom.";
RL   Hoppe-Seyler's Z. Physiol. Chem. 364:1717-1726(1983).
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   -!- PTM: Six disulfide bonds are present.
CC   -!- MISCELLANEOUS: Two very similar relatively nontoxic phospholipases
CC       were isolated from the venom, CM-II (shown here) and CM-I. The
CC       amino acid composition of CM-I differed from that of CM-II in
CC       having 1 more Thr and Ala and one fewer Ser and Lys.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II
CC       subfamily.
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DR   PIR; A00761; PSBG2H.
DR   HSSP; P81458; 1VIP.
DR   HOVERGEN; P00621; -.
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_0000161616.
FT   ACT_SITE     45     45       By similarity.
FT   ACT_SITE     87     87       By similarity.
FT   METAL        25     25       Calcium; via carbonyl oxygen (By
FT                                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        46     46       Calcium (By similarity).
SQ   SEQUENCE   119 AA;  13665 MW;  E625A8F304770181 CRC64;
     DLTQFGNMIN KMGQSVFDYI YYGCYCGWGG QGKPRDATDR CCFVHDCCYG KMGTYDTKWT
     SYKYEFQDGD IICGDKDPQK KELCECDRVA AICFANSRNT YNSKYFGYSS SKCTETEQC
//