ID   PA21B_AGKHA             Reviewed;         122 AA.
AC   P04417;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   04-NOV-2008, entry version 73.
DE   RecName: Full=Phospholipase A2, basic;
DE            Short=PA2-I;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
OS   Agkistrodon halys blomhoffi (Mamushi) (Gloydius blomhoffii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea;
OC   Viperidae; Crotalinae; Gloydius.
OX   NCBI_TaxID=242054;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Venom;
RX   MEDLINE=87000546; PubMed=3530322; DOI=10.1021/bi00363a020;
RA   Forst S., Weiss J., Blackburn P., Frangione B., Goni F., Elsbach P.;
RT   "Amino acid sequence of a basic Agkistrodon halys blomhoffii
RT   phospholipase A2. Possible role of NH2-terminal lysines in action on
RT   phospholipids of Escherichia coli.";
RL   Biochemistry 25:4309-4314(1986).
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   -!- SUBUNIT: In contrast to the pancreatic enzymes, the molecules of
CC       venom phospholipases A2 are dimers of identical chains; the
CC       monomers appear to be inactive.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II
CC       subfamily.
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DR   PIR; A00766; PSABA.
DR   HOVERGEN; P04417; -.
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    122       Phospholipase A2, basic.
FT                                /FTId=PRO_0000161595.
FT   ACT_SITE     47     47       By similarity.
FT   ACT_SITE     89     89       By 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        31     31       Calcium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        48     48       Calcium (By similarity).
FT   DISULFID     26    115       By similarity.
FT   DISULFID     28     44       By similarity.
FT   DISULFID     43     95       By similarity.
FT   DISULFID     49    122       By similarity.
FT   DISULFID     50     88       By similarity.
FT   DISULFID     57     81       By similarity.
FT   DISULFID     75     86       By similarity.
FT   UNSURE       74     74
SQ   SEQUENCE   122 AA;  13982 MW;  EA2C5EE5EEF44488 CRC64;
     HLLQFRKMIK KMTGKEPVIS YAFYGCYCGS GGRGKPKDAT DRCCFVHDCC YEKVTGCKPK
     WDDYTYSWKN GDIVCGGDDP CKKEICECDR AAAICFRDNL KTYKKRYMAY PDILCSSKSE
     KC
//