PA2A1_BOTPA
ID PA2A1_BOTPA Reviewed; 48 AA.
AC C0HJU3;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 15.
DE RecName: Full=Acidic phospholipase A2 {ECO:0000303|PubMed:17451767};
DE Short=Bp-PLA2 {ECO:0000303|PubMed:17451767};
DE EC=3.1.1.4 {ECO:0000269|PubMed:17451767};
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase {ECO:0000250|UniProtKB:P14418};
DE Flags: Fragment;
OS Bothrops pauloensis (Neuwied's lancehead) (Bothrops neuwiedi pauloensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=1042543;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, COFACTOR, ACTIVITY REGULATION, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom {ECO:0000303|PubMed:17451767};
RX PubMed=17451767; DOI=10.1016/j.toxicon.2007.03.005;
RA Rodrigues R.S., Izidoro L.F., Teixeira S.S., Silveira L.B., Hamaguchi A.,
RA Homsi-Brandeburgo M.I., Selistre-de-Araujo H.S., Giglio J.R., Fuly A.L.,
RA Soares A.M., Rodrigues V.M.;
RT "Isolation and functional characterization of a new myotoxic acidic
RT phospholipase A(2) from Bothrops pauloensis snake venom.";
RL Toxicon 50:153-165(2007).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that shows myotoxicity
CC and induces paw edema in mice (PubMed:17451767). Exhibits indirect
CC hemolytic activity (PubMed:17451767). Inhibits platelet aggregation
CC induced by ADP and collagen (PubMed:17451767). PLA2 catalyzes the
CC calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-
CC phosphoglycerides (PubMed:17451767). {ECO:0000269|PubMed:17451767}.
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:17451767};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:17451767};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250|UniProtKB:P14418};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA. Inhibited by Ba(2+), Cu(+),
CC Fe(2+) and Zn(2+) ions and, to a lesser extent, by Mn(2+) and Mg(2+)
CC ions. {ECO:0000269|PubMed:17451767}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0-8.5. Activity decreases rapidly at basic or acidic
CC pH and is virtually absent at pH 12 and pH 3.5, respectively.
CC {ECO:0000269|PubMed:17451767};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17451767}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17451767}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:17451767}.
CC -!- MISCELLANEOUS: On the 2D-gel the determined pI of this protein is: 4.3,
CC its MW is: 15.8 kDa. {ECO:0000269|PubMed:17451767}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR AlphaFoldDB; C0HJU3; -.
DR SMR; C0HJU3; -.
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 Gene3D; 1.20.90.10; -; 1.
DR InterPro; IPR001211; PLipase_A2.
DR InterPro; IPR016090; PLipase_A2_dom.
DR InterPro; IPR036444; PLipase_A2_dom_sf.
DR PANTHER; PTHR11716; PTHR11716; 1.
DR Pfam; PF00068; Phospholip_A2_1; 1.
DR SMART; SM00085; PA2c; 1.
DR SUPFAM; SSF48619; SSF48619; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond;
KW Hemostasis impairing toxin; Hydrolase; Lipid degradation; Lipid metabolism;
KW Metal-binding; Platelet aggregation inhibiting toxin; Secreted; Toxin.
FT CHAIN 1..48
FT /note="Acidic phospholipase A2"
FT /evidence="ECO:0000269|PubMed:17451767"
FT /id="PRO_0000433784"
FT ACT_SITE 47
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 26..?
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 28..44
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 44..?
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT NON_TER 48
FT /evidence="ECO:0000303|PubMed:17451767"
SQ SEQUENCE 48 AA; 5544 MW; DE3B171A87E652D7 CRC64;
NLVQFKTLIM KIAGRSVVYK YFYYGCYCGW GGIGQPRDAT DRCCFVHD
