ID   PA2B2_CROMT             Reviewed;          23 AA.
AC   P0DJN4;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2012, sequence version 1.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=Basic phospholipase A2 CB2;
DE            Short=svPLA2;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   Flags: Fragment;
OS   Crotalus mitchellii mitchellii (San Lucan speckled rattlesnake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX   NCBI_TaxID=384067;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=15032748; DOI=10.1042/bj20040125;
RA   Chen Y.-H., Wang Y.-M., Hseu M.-J., Tsai I.-H.;
RT   "Molecular evolution and structure-function relationships of crotoxin-like
RT   and asparagine-6-containing phospholipases A2 in pit viper venoms.";
RL   Biochem. J. 381:25-34(2004).
CC   -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that shows presynaptic
CC       neurotoxicity. PLA2 catalyzes the calcium-dependent hydrolysis of the
CC       2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:15032748}.
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   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         Vmax=430 umol/min/mg enzyme with DPPC + deoxycholate as substrate (at
CC         pH 7.4 and 37 degrees Celsius) {ECO:0000269|PubMed:15032748};
CC         Vmax=123 umol/min/mg enzyme with DPPC + Triton X-100 as substrate (at
CC         pH 7.4 and 37 degrees Celsius) {ECO:0000269|PubMed:15032748};
CC         Note=When tested as a monomer.;
CC   -!- SUBUNIT: Heterodimer of an acidic subunit and a basic chain. The acidic
CC       subunit is non-toxic, without enzymatic activity and comprises 3
CC       peptides that are cross-linked by 7 disulfide bridges. The basic
CC       subunit is toxic, has phospholipase A2 activity and is composed of a
CC       single chain. {ECO:0000269|PubMed:15032748}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- PTM: Contains 7 disulfide bonds. {ECO:0000250}.
CC   -!- MASS SPECTROMETRY: Mass=14244; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:15032748};
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P0DJN4; -.
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   Calcium; Direct protein sequencing; Disulfide bond; Hydrolase;
KW   Lipid degradation; Lipid metabolism; Metal-binding; Neurotoxin;
KW   Presynaptic neurotoxin; Secreted; Toxin.
FT   CHAIN           1..>23
FT                   /note="Basic phospholipase A2 CB2"
FT                   /id="PRO_0000418569"
FT   NON_TER         23
SQ   SEQUENCE   23 AA;  2807 MW;  9F0BAFC57F83E3E0 CRC64;
     SLLQFNKMIK FETRKNAIPF YAF