ID   PA2AA_CROHD             Reviewed;          23 AA.
AC   P0DJR1;
DT   03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 1.
DT   25-MAY-2022, entry version 15.
DE   RecName: Full=Acidic phospholipase CHA-E6a;
DE            Short=svPLA2;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   Flags: Fragment;
OS   Crotalus horridus (Timber rattlesnake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX   NCBI_TaxID=35024;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, AND MASS SPECTROMETRY.
RC   STRAIN=South Carolina; TISSUE=Venom;
RX   PubMed=20347857; DOI=10.1016/j.toxicon.2010.03.015;
RA   Wang Y.-M., Parmelee J., Guo Y.-W., Tsai I.-H.;
RT   "Absence of phospholipase A(2) in most Crotalus horridus venom due to
RT   translation blockage: comparison with Crotalus horridus atricaudatus
RT   venom.";
RL   Toxicon 56:93-100(2010).
CC   -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that shows high lipolytic
CC       (1048 umol/mg/min) and weak ADP-induced platelet aggregation
CC       activities. Also shows weak anticoagulant activity (IC(50) is less than
CC       1.0 uM). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC       groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:20347857}.
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:20347857};
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   -!- PTM: Contains 7 disulfide bonds. {ECO:0000250}.
CC   -!- MASS SPECTROMETRY: Mass=13770; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:20347857};
CC   -!- MISCELLANEOUS: The subspecies C.h.atricaudatus mentioned in
CC       PubMed:20347857 is currently considered invalid. However, since
CC       different origins of specimens explain sequence variations, the
CC       specimen origins are indicated under strain in the reference section
CC       (in PubMed:20347857, South Carolina to C.h.atricaudatus).
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC       D49 sub-subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0DJR1; -.
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; Disulfide bond; Hemostasis impairing toxin;
KW   Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding;
KW   Platelet aggregation inhibiting toxin; Secreted; Toxin.
FT   CHAIN           1..>23
FT                   /note="Acidic phospholipase CHA-E6a"
FT                   /id="PRO_0000419285"
FT   NON_TER         23
SQ   SEQUENCE   23 AA;  2690 MW;  19F674D953D66851 CRC64;
     SLVQFEMMIM EVAKRSGLLW YSA