PA2BD_BOTLC
ID PA2BD_BOTLC Reviewed; 122 AA.
AC P86974;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=Basic phospholipase A2;
DE Short=blD-PLA2 {ECO:0000303|PubMed:17110015};
DE Short=svPLA2;
DE EC=3.1.1.4 {ECO:0000250|UniProtKB:P86389};
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
OS Bothrops leucurus (Whitetail lancehead).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=157295;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE.
RC TISSUE=Venom;
RA Sanchez E.F.;
RL Submitted (JUN-2011) to UniProtKB.
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 1-48, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Venom {ECO:0000269|PubMed:17110015};
RX PubMed=17110015; DOI=10.1016/j.biochi.2006.10.010;
RA Higuchi D.A., Barbosa C.M., Bincoletto C., Chagas J.R., Magalhaes A.,
RA Richardson M., Sanchez E.F., Pesquero J.B., Araujo R.C., Pesquero J.L.;
RT "Purification and partial characterization of two phospholipases A2 from
RT Bothrops leucurus (white-tailed-jararaca) snake venom.";
RL Biochimie 89:319-328(2007).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that does not inhibit
CC platelet aggregation. Exhibits cytotoxic and anticoagulant activity.
CC Induces Ehrlich tumor growth but not angiogenesis. PLA2 catalyzes the
CC calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-
CC phosphoglycerides. {ECO:0000269|PubMed:17110015}.
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:0000250|UniProtKB:P86389, ECO:0000255|PROSITE-
CC ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17110015}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:17110015}.
CC -!- MISCELLANEOUS: Displays 20 times higher phospholipase activity than
CC blK-PLA2. {ECO:0000269|PubMed:17110015}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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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.
DR PROSITE; PS00119; PA2_ASP; 1.
DR PROSITE; PS00118; PA2_HIS; 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; Secreted;
KW Toxin.
FT CHAIN 1..122
FT /note="Basic phospholipase A2"
FT /id="PRO_0000413006"
FT ACT_SITE 47
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT ACT_SITE 89
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..115
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 28..44
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 43..95
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 49..122
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 50..88
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 57..81
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 75..86
FT /evidence="ECO:0000250|UniProtKB:P14418"
SQ SEQUENCE 122 AA; 13933 MW; EC07FE16FF94AC6F CRC64;
DLWQFGQMIL KETGKLPFPY YTTYGCYCGW GGQGQPKDAT DRCCFVHDCC YGKLTNCKPK
TDRYSYSREN GVIICGEGTP CEKQICECDK AAAVCFRENL RTYKXXYMAY PDVLCKKPAE
KC
