ID   PA2BD_CRODR             Reviewed;         122 AA.
AC   P0CAS4;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Basic phospholipase A2 Cdr-13;
DE            Short=svPLA2;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
OS   Crotalus durissus ruruima (South American rattlesnake) (Mt. Roraima
OS   rattlesnake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX   NCBI_TaxID=221570;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=17203396; DOI=10.1007/s10930-006-9042-3;
RA   Ponce-Soto L.A., Baldasso P.A., Romero-Vargas F.F., Winck F.V.,
RA   Novello J.C., Marangoni S.;
RT   "Biochemical, pharmacological and structural characterization of two PLA2
RT   isoforms Cdr-12 and Cdr-13 from Crotalus durissus ruruima snake venom.";
RL   Protein J. 26:39-49(2007).
CC   -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that induces myonecrosis
CC       and edema upon subcutaneous injections in mice. In vitro, causes a
CC       potent blockade of neuromuscular transmission in young chicken biventer
CC       cervicis preparation and produces cytotoxicity in murine C2C12 skeletal
CC       muscle myotubes and lack cytolytic activity upon myoblasts in vitro.
CC       PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in
CC       3-sn-phosphoglycerides. {ECO:0000269|PubMed:17203396}.
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};
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.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MASS SPECTROMETRY: Mass=14296.42; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:17203396};
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC       D49 sub-subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0CAS4; -.
DR   SMR; P0CAS4; -.
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   Calcium; Direct protein sequencing; Disulfide bond; Hydrolase;
KW   Lipid degradation; Lipid metabolism; Metal-binding; Myotoxin; Neurotoxin;
KW   Secreted; Toxin.
FT   CHAIN           1..122
FT                   /note="Basic phospholipase A2 Cdr-13"
FT                   /id="PRO_0000377504"
FT   ACT_SITE        47
FT                   /evidence="ECO:0000250|UniProtKB:P62022"
FT   ACT_SITE        89
FT                   /evidence="ECO:0000250|UniProtKB:P62022"
FT   BINDING         27
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P62022"
FT   BINDING         29
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P62022"
FT   BINDING         31
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P62022"
FT   BINDING         48
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P62022"
FT   DISULFID        26..115
FT                   /evidence="ECO:0000250|UniProtKB:P62022"
FT   DISULFID        28..44
FT                   /evidence="ECO:0000250|UniProtKB:P62022"
FT   DISULFID        43..95
FT                   /evidence="ECO:0000250|UniProtKB:P62022"
FT   DISULFID        49..122
FT                   /evidence="ECO:0000250|UniProtKB:P62022"
FT   DISULFID        50..88
FT                   /evidence="ECO:0000250|UniProtKB:P62022"
FT   DISULFID        57..81
FT                   /evidence="ECO:0000250|UniProtKB:P62022"
FT   DISULFID        75..86
FT                   /evidence="ECO:0000250|UniProtKB:P62022"
SQ   SEQUENCE   122 AA;  14297 MW;  49E4A8468FCAFBCB CRC64;
     SLVQFEKMIK EETGKNAVPF YAFYGCYCGW GGRGRPKDAT DRCCIVHDCC YEKLVKCNTK
     WDFYRYSLRS GYFQCGKGTW CEQQICECDR VAAECLRRSL STYRYGKMIY PDSRCREPSE
     TC