ID   PA21B_LATSE             Reviewed;         145 AA.
AC   P00611; Q9I848;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-2002, sequence version 3.
DT   04-NOV-2008, entry version 72.
DE   RecName: Full=Phospholipase A2 isozyme 1;
DE            EC=3.1.1.4;
DE   AltName: Full=Phospholipase A2 isozyme I;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   AltName: Full=GL5-1;
DE   Flags: Precursor;
OS   Laticauda semifasciata (Broad-banded blue sea snake) (Erabu sea
OS   snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea;
OC   Elapidae; Laticaudinae; Laticauda.
OX   NCBI_TaxID=8631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RX   MEDLINE=22072837; PubMed=12076640; DOI=10.1016/S0041-0101(01)00272-0;
RA   Fujimi T.J., Tsuchiya T., Tamiya T.;
RT   "A comparative analysis of invaded sequences from group IA
RT   phospholipase A(2) genes provides evidence about the divergence period
RT   of genes groups and snake families.";
RL   Toxicon 40:873-884(2002).
RN   [2]
RP   PROTEIN SEQUENCE OF 28-145.
RC   TISSUE=Venom;
RX   MEDLINE=83153048; PubMed=7165712;
RA   Nishida S., Kim H.S., Tamiya N.;
RT   "Amino acid sequences of three phospholipases A I, III and IV from the
RT   venom of the sea snake Laticauda semifasciata.";
RL   Biochem. J. 207:589-594(1982).
RN   [3]
RP   SEQUENCE REVISION TO 97-107.
RX   MEDLINE=89044898; PubMed=3188064; DOI=10.1016/0041-0101(88)90281-4;
RA   Takasaki C., Kuramochi H., Shimazu T., Tamiya N.;
RT   "Correction of amino acid sequence of phospholipase A2 I from the
RT   venom of Laticauda semifasciata (Erabu sea snake).";
RL   Toxicon 26:747-749(1988).
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.
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DR   EMBL; AB062440; BAB72247.1; -; Genomic_DNA.
DR   PIR; A94325; PSLT1E.
DR   HSSP; P00608; 1AE7.
DR   HOVERGEN; P00611; -.
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     21       Potential.
FT   PROPEP       22     27
FT                                /FTId=PRO_0000022896.
FT   CHAIN        28    145       Phospholipase A2 isozyme 1.
FT                                /FTId=PRO_0000022897.
FT   ACT_SITE     75     75       By similarity.
FT   ACT_SITE    119    119       By 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        59     59       Calcium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        76     76       Calcium (By similarity).
FT   SITE         91     91       Specific activity reduced 20-fold by
FT                                modification.
FT   DISULFID     38     98       By similarity.
FT   DISULFID     54    144       By similarity.
FT   DISULFID     56     72       By similarity.
FT   DISULFID     71    125       By similarity.
FT   DISULFID     78    118       By similarity.
FT   DISULFID     87    111       By similarity.
FT   DISULFID    105    116       By similarity.
FT   CONFLICT     39     40       VN -> NV (in Ref. 2; AA sequence).
FT   CONFLICT     77     77       D -> N (in Ref. 2; AA sequence).
SQ   SEQUENCE   145 AA;  15900 MW;  1F84DF6F7BC5348F CRC64;
     MYPAHLLVLL AVCVSLLGAT AIPPLPLNLV QFSNLIQCVN KGSRASYHYA DYGCYCGAGG
     SGTPVDELDR CCKIHDDCYG EAEKMGCYPK WTLYTYDCST EEPNCSTKTG CQGFVCACDL
     EAAKCFARSP YNNKNYNIDT SKRCK
//