PA2A_BOTLC
ID PA2A_BOTLC Reviewed; 60 AA.
AC P0DJ62;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Acidic phospholipase A2;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Bl-PLA2;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase 1B;
DE Flags: Fragment;
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]
RP PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Venom;
RX PubMed=21699995; DOI=10.1016/j.cbpc.2011.06.003;
RA Nunes D.C., Rodrigues R.S., Lucena M.N., Cologna C.T., Oliveira A.C.,
RA Hamaguchi A., Homsi-Brandeburgo M.I., Arantes E.C., Teixeira D.N.,
RA Ueira-Vieira C., Rodrigues V.M.;
RT "Isolation and functional characterization of proinflammatory acidic
RT phospholipase A2 from Bothrops leucurus snake venom.";
RL Comp. Biochem. Physiol. 154:226-233(2011).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that exhibits an indirect
CC hemolytic activity, a low myotoxicity, and induces edema. In addition,
CC this enzyme has been shown to induce the release of some pro- and anti-
CC inflammatory cytokines from human PBMC (IL12B, TNF-alpha, IL1B and IL6
CC but not variation has been observed for IL-8 and IL-10). PLA2 catalyzes
CC the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-
CC phosphoglycerides. {ECO:0000269|PubMed:21699995}.
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:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-
CC ProRule:PRU10036, ECO:0000269|PubMed:21699995};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:21699995}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21699995}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:21699995}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0DJ62; -.
DR SMR; P0DJ62; -.
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:0044179; P:hemolysis in another organism; 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 CDD; cd00125; PLA2c; 1.
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.
DR PROSITE; PS00118; PA2_HIS; 1.
PE 1: Evidence at protein level;
KW Calcium; Cytolysis; Direct protein sequencing; Disulfide bond; Hemolysis;
KW Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding; Myotoxin;
KW Secreted; Toxin.
FT CHAIN 1..>60
FT /note="Acidic phospholipase A2"
FT /id="PRO_0000413803"
FT ACT_SITE 47
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10035,
FT ECO:0000255|PROSITE-ProRule:PRU10036"
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 DISULFID 57..?
FT /evidence="ECO:0000250"
FT NON_TER 60
SQ SEQUENCE 60 AA; 6555 MW; EF0C5F60B1765429 CRC64;
SLWQFGKMIN YVMGESGVLQ YLSYGCYCGL GGQGQPTDAT DRCCFVHDCC YGKVTGCDPK
