ID   PA2A_PORNA              Reviewed;          10 AA.
AC   B3EWG8;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2012, sequence version 1.
DT   25-MAY-2022, entry version 22.
DE   RecName: Full=Acidic phospholipase A2 PnPLA2;
DE            Short=svPLA2;
DE            EC=3.1.1.4 {ECO:0000250|UniProtKB:P86389};
DE   Flags: Fragment;
OS   Porthidium nasutum (Hognosed pitviper) (Bothrops nasutus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Porthidium.
OX   NCBI_TaxID=74558;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND MASS SPECTROMETRY.
RC   TISSUE=Venom {ECO:0000269|PubMed:22251437};
RX   PubMed=22251437; DOI=10.1016/j.cbpb.2011.12.010;
RA   Vargas L.J., Londono M., Quintana J.C., Rua C., Segura C., Lomonte B.,
RA   Nunez V.;
RT   "An acidic phospholipase A(2) with antibacterial activity from Porthidium
RT   nasutum snake venom.";
RL   Comp. Biochem. Physiol. 161B:341-347(2012).
CC   -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that has antibacterial
CC       activity against S.aureus ATCC 25923 and ATCC 29213, acts by inducing
CC       bacterial membrane breakage. Displays a potent inhibitory effect on
CC       collagen-induced human platelet aggregation and has indirect hemolytic
CC       activity. Does not show cytotoxicity to murine skeletal muscle
CC       myoblasts. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-
CC       acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:22251437}.
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:0000250|UniProtKB:P86389};
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 {ECO:0000269|PubMed:22251437}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:22251437}.
CC   -!- MASS SPECTROMETRY: Mass=15802.6; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:22251437};
CC   -!- MISCELLANEOUS: The determined pI of this protein is: 4.6.
CC       {ECO:0000269|PubMed:22251437}.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC       {ECO:0000255}.
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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:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Calcium; Cytolysis; Direct protein sequencing;
KW   Hemolysis; Hemostasis impairing toxin; Hydrolase; Metal-binding;
KW   Platelet aggregation inhibiting toxin; Secreted; Toxin.
FT   CHAIN           1..>10
FT                   /note="Acidic phospholipase A2 PnPLA2"
FT                   /id="PRO_0000416972"
FT   NON_TER         10
FT                   /evidence="ECO:0000303|PubMed:22251437"
SQ   SEQUENCE   10 AA;  1252 MW;  511EC29ABAE9D6D7 CRC64;
     DLLQFXDMMK