PA2B1_BOTPA
ID PA2B1_BOTPA Reviewed; 50 AA.
AC P0DM51;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2013, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Basic phospholipase A2 BnpTX-1;
DE Short=BnPTx-I;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
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]
RP PROTEIN SEQUENCE, FUNCTION, BIOASSAY, CATALYTIC ACTIVITY, SUBUNIT, ACTIVITY
RP REGULATION, DISULFIDE BONDS, AND TOXIC DOSE.
RC TISSUE=Venom;
RX PubMed=15302537; DOI=10.1016/j.toxicon.2004.06.008;
RA Rodrigues V.M., Marcussi S., Cambraia R.S., de Araujo A.L.,
RA Malta-Neto N.R., Hamaguchi A., Ferro E.A., Homsi-Brandeburgo M.I.,
RA Giglio J.R., Soares A.M.;
RT "Bactericidal and neurotoxic activities of two myotoxic phospholipases A2
RT from Bothrops neuwiedi pauloensis snake venom.";
RL Toxicon 44:305-314(2004).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2). In vitro, shows
CC anticoagulant activity and induces cytotoxicity when tested on C2C12
CC myoblasts/myotubes. In vivo, when tested on mice, induces myotoxicity
CC (intramuscular injection), edema (injection in the subplantar region)
CC and lethality. Also induces neurotoxic effect on mouse neuromuscular
CC preparations and has bactericidal activity on the Gram-negative
CC bacteria E.coli (ATCC29648) and the Gram-positive S.aureus (ATCC
CC 25923). The catalytic and anticoagulant activities of BnpTX-I are
CC higher than those of BnpTX-II. PLA2 catalyzes the calcium-dependent
CC hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
CC {ECO:0000269|PubMed:15302537}.
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:15302537};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC -!- ACTIVITY REGULATION: P-bromophenacyl bromide (BPB) completely inhibit
CC the catalytic activity whereas it only partially reduces the toxic
CC activities. EDTA and magnesium ions partially inhibit the catalytic
CC activity and partially reduce the toxic activities.
CC {ECO:0000269|PubMed:15302537}.
CC -!- SUBUNIT: Dimer. {ECO:0000269|PubMed:15302537}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: Contains 7 disulfide bonds.
CC -!- TOXIC DOSE: LD(50) is 5.1 +/- 1.3 mg/kg by intraperitoneal injection
CC into mice. {ECO:0000269|PubMed:15302537}.
CC -!- TOXIC DOSE: LD(50) is 2.3 +/- 0.8 mg/kg by intravenous injection into
CC mice. {ECO:0000269|PubMed:15302537}.
CC -!- MISCELLANEOUS: Has a pI of approximately 7.8 and about 121 amino acids.
CC {ECO:0000305|PubMed:15302537}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0DM51; -.
DR SMR; P0DM51; -.
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:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
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 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 Antibiotic; Antimicrobial; Blood coagulation cascade inhibiting toxin;
KW Calcium; Direct protein sequencing; Disulfide bond;
KW Hemostasis impairing toxin; Hydrolase; Lipid degradation; Lipid metabolism;
KW Metal-binding; Myotoxin; Neurotoxin; Secreted; Toxin.
FT CHAIN 1..>50
FT /note="Basic phospholipase A2 BnpTX-1"
FT /id="PRO_0000423032"
FT ACT_SITE 47
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..?
FT /evidence="ECO:0000250"
FT DISULFID 28..44
FT /evidence="ECO:0000250"
FT DISULFID 43..?
FT /evidence="ECO:0000250"
FT DISULFID 49..?
FT /evidence="ECO:0000250"
FT DISULFID 50..?
FT /evidence="ECO:0000250"
FT NON_TER 50
SQ SEQUENCE 50 AA; 5653 MW; 220BFE9682613497 CRC64;
DLWQFGKMIL KVAGKLPFPY YGAYGCYCGW GGRGKPKDPT DRCCFVHDCC
