PA2B2_PSEFE
ID PA2B2_PSEFE Reviewed; 122 AA.
AC P0DKR5;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=Basic phospholipase A2 CbII;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
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 CATALYTIC ACTIVITY.
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, AND 3D-STRUCTURE MODELING.
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 {ECO:0000269|PubMed:18062812}.
CC -!- FUNCTION: Monomer: Snake venom phospholipase A2 (PLA2) that exhibits
CC strong anticoagulant effects by binding to factor Xa (F10) and
CC inhibiting the prothrombinase activity (IC(50) is 20 nM). PLA2
CC catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-
CC sn-phosphoglycerides. {ECO:0000269|PubMed:18062812}.
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 Evidence={ECO:0000269|PubMed:8588211};
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 is non-toxic, and increases
CC the toxicity of the basic subunit. {ECO:0000269|PubMed:4084321}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0DKR5; -.
DR SMR; P0DKR5; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR CDD; cd00125; PLA2c; 1.
DR Gene3D; 1.20.90.10; -; 1.
DR InterPro; IPR001211; PLipase_A2.
DR InterPro; IPR033112; PLipase_A2_Asp_AS.
DR InterPro; IPR016090; PLipase_A2_dom.
DR InterPro; IPR036444; PLipase_A2_dom_sf.
DR InterPro; IPR033113; PLipase_A2_His_AS.
DR PANTHER; PTHR11716; PTHR11716; 1.
DR Pfam; PF00068; Phospholip_A2_1; 1.
DR PRINTS; PR00389; PHPHLIPASEA2.
DR SMART; SM00085; PA2c; 1.
DR SUPFAM; SSF48619; SSF48619; 1.
PE 1: Evidence at protein level;
KW Blood coagulation cascade inhibiting toxin; Calcium;
KW Direct protein sequencing; Disulfide bond; Hemostasis impairing toxin;
KW Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding; Neurotoxin;
KW Presynaptic neurotoxin; Secreted; Toxin.
FT CHAIN 1..122
FT /note="Basic phospholipase A2 CbII"
FT /id="PRO_0000420359"
FT ACT_SITE 47
FT /evidence="ECO:0000250"
FT ACT_SITE 89
FT /evidence="ECO:0000250"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 26..115
FT /evidence="ECO:0000250"
FT DISULFID 28..44
FT /evidence="ECO:0000250"
FT DISULFID 43..95
FT /evidence="ECO:0000250"
FT DISULFID 49..122
FT /evidence="ECO:0000250"
FT DISULFID 50..88
FT /evidence="ECO:0000250"
FT DISULFID 57..81
FT /evidence="ECO:0000250"
FT DISULFID 75..86
FT /evidence="ECO:0000250"
SQ SEQUENCE 122 AA; 13735 MW; CD8EEBF6ADFB9DF2 CRC64;
NLFQFTKMIN GKLGAFAVLN YISTGCYCGW GGQGTPKDAT DRCCFVHDCC YGRVKGCNPK
LAIYSYSFQK GNIVCGKNNG CLRDICECDR VAANCFHQNK NTYNRNYRFL SSSRCRQTSE
QC
