ID   PA2AB_PSEFE             Reviewed;          20 AA.
AC   P0DKR4;
DT   28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2012, sequence version 1.
DT   25-MAY-2022, entry version 18.
DE   RecName: Full=Acidic phospholipase A2 CbIbeta;
DE            Short=svPLA2;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   Flags: Fragments;
OS   Pseudocerastes fieldi (Field's horned viper) (Pseudocerastes persicus
OS   fieldi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Pseudocerastes.
OX   NCBI_TaxID=1355908;
RN   [1]
RP   PROTEIN SEQUENCE, AND FUNCTION.
RC   TISSUE=Venom;
RX   PubMed=8588211; DOI=10.1016/0041-0101(95)00034-j;
RA   Francis B., Bdolah A., Kaiser I.I.;
RT   "Amino acid sequences of a heterodimeric neurotoxin from the venom of the
RT   false horned viper (Pseudocerastes fieldi).";
RL   Toxicon 33:863-874(1995).
RN   [2]
RP   SUBUNIT.
RX   PubMed=4084321;
RA   Bdolah A., Kinamon S., Batzri-Izraeli R.;
RT   "The neurotoxic complex from the venom of Pseudocerastes fieldi.
RT   Contribution of the nontoxic subunit.";
RL   Biochem. Int. 11:627-636(1985).
RN   [3]
RP   FUNCTION AS AN ANTICOAGULANT.
RX   PubMed=18062812; DOI=10.1186/1472-6807-7-82;
RA   Faure G., Gowda V.T., Maroun R.C.;
RT   "Characterization of a human coagulation factor Xa-binding site on
RT   Viperidae snake venom phospholipases A2 by affinity binding studies and
RT   molecular bioinformatics.";
RL   BMC Struct. Biol. 7:82-82(2007).
CC   -!- FUNCTION: Heterodimer: presynaptic neurotoxin.
CC   -!- FUNCTION: Monomer: Snake venom phospholipase A2 (PLA2) is inactive
CC       towards micellar phosphatidylcholine but is weakly active towards non-
CC       micellar dithiolecithin. PLA2 catalyzes the calcium-dependent
CC       hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC         glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC         ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC   -!- SUBUNIT: Heterodimer of an acidic subunit (CbIalpha or CbIbeta) and a
CC       basic subunit (CbII). The acidic subunit (CbI) is non-toxic, and
CC       increases the toxicity of the basic subunit (CbII).
CC       {ECO:0000269|PubMed:4084321}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- PTM: Contains 7 disulfide bonds. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC       D49 sub-subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0DKR4; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hydrolase; Neurotoxin;
KW   Presynaptic neurotoxin; Secreted; Toxin.
FT   CHAIN           <1..>20
FT                   /note="Acidic phospholipase A2 CbIbeta"
FT                   /id="PRO_0000420358"
FT   NON_CONS        15..16
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         20
SQ   SEQUENCE   20 AA;  2281 MW;  F108C5CBDCD91F5E CRC64;
     DCCYGRVNGC NPKMADKNYE