ID   PA2_BOTIN               Reviewed;          45 AA.
AC   P0DV82;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   25-MAY-2022, sequence version 1.
DT   03-AUG-2022, entry version 2.
DE   RecName: Full=Acidic phospholipase A2 Bi PLA2 {ECO:0000303|PubMed:17953979};
DE            Short=svPLA2;
DE            EC=3.1.1.4 {ECO:0000269|PubMed:17953979};
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   Flags: Fragment;
OS   Bothrops insularis (Golden lancehead) (Lachesis insularis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=8723;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=17953979; DOI=10.1016/j.toxicon.2007.08.017;
RA   Machado Braga M.D., Costa Martins A.M., Alves C.D., de Menezes D.B.,
RA   Martins R.D., Ferreira Barbosa P.S., de Sousa Oliveira I.M., Toyama M.H.,
RA   Toyama D.O., Dos Santos Diz Filho E.B., Ramos Fagundes F.H., Fonteles M.C.,
RA   Azul Monteiro H.S.;
RT   "Purification and renal effects of phospholipase A(2) isolated from
RT   Bothrops insularis venom.";
RL   Toxicon 51:181-190(2008).
CC   -!- FUNCTION: Snake venom phospholipase A2 (PLA2) induces increase of
CC       creatine kinase levels, which is an indicator or myonecrosis
CC       (PubMed:17953979). It also promotes renal alterations in the isolated
CC       perfused rat kidney (PubMed:17953979). It increases perfusion pressure
CC       (PP), renal vascular resistance (RVR), urinary flow (UF) and glomerular
CC       filtration rate (GFR). Sodium and chloride tubular reabsorption
CC       decreased at 120 minutes, without alteration in potassium transport
CC       (PubMed:17953979). PLA2 catalyzes the calcium-dependent hydrolysis of
CC       the 2-acyl groups in 3-sn-phosphoglycerides (PubMed:17953979).
CC       {ECO:0000269|PubMed:17953979}.
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:17953979};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:P59071};
CC       Note=Binds 1 Ca(2+) ion. {ECO:0000250|UniProtKB:P59071};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17953979}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:17953979}.
CC   -!- MASS SPECTROMETRY: Mass=13984.20; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:17953979};
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
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   PRINTS; PR00389; PHPHLIPASEA2.
DR   SMART; SM00085; PA2c; 1.
DR   SUPFAM; SSF48619; SSF48619; 1.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Disulfide bond; Hydrolase;
KW   Metal-binding; Myotoxin; Secreted; Toxin.
FT   CHAIN           1..>45
FT                   /note="Acidic phospholipase A2 Bi PLA2"
FT                   /evidence="ECO:0000305|PubMed:17953979"
FT                   /id="PRO_0000455657"
FT   BINDING         27
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P59071"
FT   BINDING         29
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P59071"
FT   BINDING         31
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P59071"
FT   DISULFID        26..?
FT                   /evidence="ECO:0000305"
FT   DISULFID        28..44
FT                   /evidence="ECO:0000250|UniProtKB:P59071"
FT   DISULFID        43..?
FT                   /evidence="ECO:0000305"
FT   NON_TER         45
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   45 AA;  4997 MW;  5B80EE5AB5DA6BC4 CRC64;
     SLFEFGKMIL KETGKNPFTS YGFYGCYCGW GGRGGPKDAT DRCCF