ID   PA20_BUNMU              Reviewed;         145 AA.
AC   P00606;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 2.
DT   04-NOV-2008, entry version 71.
DE   RecName: Full=Phospholipase A2;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   Flags: Precursor;
OS   Bungarus multicinctus (Many-banded krait).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea;
OC   Elapidae; Bungarinae; Bungarus.
OX   NCBI_TaxID=8616;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   MEDLINE=90356415; PubMed=2388841; DOI=10.1093/nar/18.15.4608;
RA   Danse J.-M.;
RT   "Nucleotide sequence encoding for non-toxic phospholipase-A2 from
RT   Bungarus multicinctus.";
RL   Nucleic Acids Res. 18:4608-4608(1990).
RN   [2]
RP   PROTEIN SEQUENCE OF 28-145.
RC   TISSUE=Venom;
RX   MEDLINE=81168081; PubMed=7217037;
RA   Kondo K., Toda H., Narita K.;
RT   "Amino acid sequence of phospholipase A from Bungarus multicinctus
RT   venom.";
RL   J. Biochem. 89:37-47(1981).
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X53406; CAA37482.1; -; mRNA.
DR   PIR; S10981; PSKF2U.
DR   HSSP; Q9DF52; 1FE5.
DR   SMR; P00606; 28-145.
DR   HOVERGEN; P00606; -.
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; Signal.
FT   SIGNAL        1     19       Potential.
FT   PROPEP       20     27
FT                                /FTId=PRO_0000022833.
FT   CHAIN        28    145       Phospholipase A2.
FT                                /FTId=PRO_0000022834.
FT   ACT_SITE     73     73       By similarity.
FT   ACT_SITE    119    119       By similarity.
FT   METAL        53     53       Calcium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        55     55       Calcium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        57     57       Calcium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        74     74       Calcium (By similarity).
FT   DISULFID     38     97       By similarity.
FT   DISULFID     52    144       By similarity.
FT   DISULFID     54     70       By similarity.
FT   DISULFID     69    125       By similarity.
FT   DISULFID     76    118       By similarity.
FT   DISULFID     86    111       By similarity.
FT   DISULFID    104    116       By similarity.
SQ   SEQUENCE   145 AA;  15593 MW;  F7959376589967CA CRC64;
     MNPAHLLILS AVCVSLLGAA NVPPQHLNLY QFKNMIVCAG TRPWIGYVNY GCYCGAGGSG
     TPVDELDRCC YVHDNCYGEA EKIPGCNPKT KTYSYTCTKP NLTCTDAAGT CARIVCDCDR
     TAAICFAAAP YNINNFMISS STHCQ
//