PA2AA_PSEFE
ID PA2AA_PSEFE Reviewed; 122 AA.
AC P0DKR3;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 03-AUG-2022, entry version 25.
DE RecName: Full=Acidic phospholipase A2 CbIalpha;
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 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, 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 -!- 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 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 II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0DKR3; -.
DR SMR; P0DKR3; -.
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:InterPro.
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 Direct protein sequencing; Disulfide bond; Hydrolase; Metal-binding;
KW Neurotoxin; Presynaptic neurotoxin; Secreted; Toxin.
FT CHAIN 1..122
FT /note="Acidic phospholipase A2 CbIalpha"
FT /id="PRO_0000420357"
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; 13625 MW; 8FF0216CCD0F4E0D CRC64;
NLFQFGEMIF EKTGKEAVHS YAIYGCYCGW GGQGRAMDAT DRCCFVHDCC YGRVNGCNPK
MATYSTSFQN GDIVCGDNDL CLRAVCECDR AAAICLGQNV NTYNKNYEHY SISHCMEESE
QC
