ID   PA21_AGKPI              Reviewed;         123 AA.
AC   P51972;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   16-JUN-2009, entry version 69.
DE   RecName: Full=Phospholipase A2;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   AltName: Full=APP-D-49;
OS   Agkistrodon piscivorus piscivorus (Eastern cottonmouth).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea;
OC   Viperidae; Crotalinae; Agkistrodon.
OX   NCBI_TaxID=8716;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Venom;
RX   MEDLINE=93257049; PubMed=8489705; DOI=10.1007/BF01026040;
RA   Welches W., Reardon I.M., Heinrikson R.L.;
RT   "An examination of structural interactions presumed to be of
RT   importance in the stabilization of phospholipase A2 dimers based upon
RT   comparative protein sequence analysis of a monomeric and dimeric
RT   enzyme from the venom of Agkistrodon p. piscivorus.";
RL   J. Protein Chem. 12:187-193(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-23, AND PALMITOYLATION AT LYS-7 AND LYS-10.
RC   TISSUE=Venom;
RX   MEDLINE=88298768; PubMed=3403524;
RA   Cho W., Tomasselli A.G., Heinrikson R.L., Kezdy F.J.;
RT   "The chemical basis for interfacial activation of monomeric
RT   phospholipases A2. Autocatalytic derivatization of the enzyme by acyl
RT   transfer from substrate.";
RL   J. Biol. Chem. 263:11237-11241(1988).
RN   [3]
RP   CHARACTERIZATION.
RC   TISSUE=Venom;
RX   MEDLINE=85054816; PubMed=6438084;
RA   Maraganore J.M., Merutka G., Cho W., Welches W., Kezdy F.J.,
RA   Heinrikson R.L.;
RT   "A new class of phospholipases A2 with lysine in place of aspartate
RT   49. Functional consequences for calcium and substrate binding.";
RL   J. Biol. Chem. 259:13839-13843(1984).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RC   TISSUE=Venom;
RX   MEDLINE=97166209; PubMed=9013608; DOI=10.1074/jbc.272.26.16152;
RA   Han S.K., Yoon E.T., Scott D.L., Sigler P.B., Cho W.;
RT   "Structural aspects of interfacial adsorption. A crystallographic and
RT   site-directed mutagenesis study of the phospholipase A2 from the venom
RT   of Agkistrodon piscivorus piscivorus.";
RL   J. Biol. Chem. 272:3573-3582(1997).
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.
CC   -!- SUBUNIT: Monomer or homodimer.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- PTM: Acylation causes dimerization.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II
CC       subfamily.
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DR   PIR; B53872; B53872.
DR   PDB; 1VAP; X-ray; 1.60 A; A/B=1-123.
DR   PDBsum; 1VAP; -.
DR   HOVERGEN; P51972; -.
DR   BRENDA; 3.1.1.4; 256843.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004623; F:phospholipase A2 activity; IEA:EC.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
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   3D-structure; Calcium; Direct protein sequencing; Disulfide bond;
KW   Hydrolase; Lipid degradation; Lipoprotein; Metal-binding; Palmitate;
KW   Secreted.
FT   CHAIN         1    123       Phospholipase A2.
FT                                /FTId=PRO_0000161605.
FT   ACT_SITE     47     47       By similarity.
FT   ACT_SITE     89     89       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.
FT   LIPID         7      7       N6-palmitoyl lysine.
FT   LIPID        10     10       N6-palmitoyl lysine.
FT   DISULFID     26    116
FT   DISULFID     28     44
FT   DISULFID     43     95
FT   DISULFID     49    123
FT   DISULFID     50     88
FT   DISULFID     57     81
FT   DISULFID     75     86
FT   HELIX         2     13
FT   HELIX        17     20
FT   STRAND       21     24
FT   TURN         25     27
FT   STRAND       28     30
FT   HELIX        39     52
FT   TURN         59     61
FT   STRAND       66     69
FT   STRAND       72     75
FT   HELIX        80     98
FT   HELIX       100    102
FT   HELIX       105    108
FT   HELIX       113    115
SQ   SEQUENCE   123 AA;  13989 MW;  C39986552D990D72 CRC64;
     NLFQFEKLIK KMTGKSGMLW YSAYGCYCGW GGQGRPKDAT DRCCFVHDCC YGKVTGCNPK
     MDIYTYSVDN GNIVCGGTNP CKKQICECDR AAAICFRDNL KTYDSKTYWK YPKKNCKEES
     EPC
//