ID   PA2B6_CRODM             Reviewed;          21 AA.
AC   P0CAS1;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   25-MAY-2022, entry version 27.
DE   RecName: Full=Phospholipase A2 crotoxin basic chain;
DE            Short=CB;
DE            Short=svPLA2;
DE            EC=3.1.1.4;
DE   AltName: Full=Cdcum6;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   Flags: Fragment;
OS   Crotalus durissus cumanensis (South American rattlesnake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX   NCBI_TaxID=184542;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, COFACTOR, MASS SPECTROMETRY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   TISSUE=Venom;
RX   PubMed=19673100; DOI=10.1016/j.toxicon.2009.01.021;
RA   Pereanez J.A., Nunez V., Huancahuire-Vega S., Marangoni S.,
RA   Ponce-Soto L.A.;
RT   "Biochemical and biological characterization of a PLA2 from crotoxin
RT   complex of Crotalus durissus cumanensis.";
RL   Toxicon 53:534-542(2009).
CC   -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that induces a
CC       conspicuous local myotoxic effect and moderate footpad edema. In vitro,
CC       it shows anticoagulant effects and is not cytotoxic on myoblast but is
CC       able to lyse myotubes. PLA2 catalyzes the calcium-dependent hydrolysis
CC       of the 2-acyl groups in 3-sn-phosphoglycerides.
CC       {ECO:0000269|PubMed:19673100}.
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;
CC         Evidence={ECO:0000269|PubMed:19673100};
CC       Note=Binds 1 Ca(2+) ion. {ECO:0000269|PubMed:19673100};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=6.0 mM for 4-nitro-3-(octanoyloxy)benzoic acid
CC         {ECO:0000269|PubMed:19673100};
CC         Vmax=3.44 nmol/min/mg enzyme {ECO:0000269|PubMed:19673100};
CC       pH dependence:
CC         Optimum pH is 8.0. {ECO:0000269|PubMed:19673100};
CC       Temperature dependence:
CC         Optimum temperature is 30-45 degrees Celsius.
CC         {ECO:0000269|PubMed:19673100};
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MASS SPECTROMETRY: Mass=14321.98; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:19673100};
CC   -!- TOXIC DOSE: LD(50) is > 0.245 mg/kg by intraperitoneal injection into
CC       mice.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P0CAS1; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Blood coagulation cascade inhibiting toxin; Calcium;
KW   Direct protein sequencing; Hemostasis impairing toxin; Hydrolase;
KW   Lipid degradation; Lipid metabolism; Metal-binding; Neurotoxin;
KW   Presynaptic neurotoxin; Secreted; Toxin.
FT   CHAIN           1..>21
FT                   /note="Phospholipase A2 crotoxin basic chain"
FT                   /id="PRO_0000376918"
FT   NON_TER         21
SQ   SEQUENCE   21 AA;  2424 MW;  58D943841640B2CA CRC64;
     SLVQFEKMIK EVAGKNGVPW Y