PLA23_BOTDP
ID PLA23_BOTDP Reviewed; 45 AA.
AC C0HJP9;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 04-FEB-2015, sequence version 1.
DT 03-AUG-2022, entry version 17.
DE RecName: Full=Phospholipase A2 3 {ECO:0000303|PubMed:26051123};
DE Short=BdsPLA2 III {ECO:0000303|PubMed:26051123};
DE Short=svPLA2;
DE EC=3.1.1.4 {ECO:0000269|PubMed:26051123};
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase {ECO:0000250|UniProtKB:Q8AXY1};
DE Flags: Fragments;
OS Bothrops diporus (Chaco lancehead) (Bothrops neuwiedi diporus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=1107943;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RX PubMed=26051123; DOI=10.1016/j.bbamem.2015.06.003;
RA Yunes Quartino P.J., Portela M., Lima A., Duran R., Lomonte B.,
RA Fidelio G.D.;
RT "A constant area monolayer method to assess optimal lipid packing for
RT lipolysis tested with several secreted phospholipase A2.";
RL Biochim. Biophys. Acta 1848:2216-2224(2015).
CC -!- FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:26051123}.
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:26051123};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:26051123};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26051123}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:26051123}.
CC -!- MASS SPECTROMETRY: Mass=14000; Mass_error=300; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:26051123};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR AlphaFoldDB; C0HJP9; -.
DR SMR; C0HJP9; -.
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: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 InterPro; IPR036444; PLipase_A2_dom_sf.
DR InterPro; IPR033113; PLipase_A2_His_AS.
DR SUPFAM; SSF48619; SSF48619; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Lipid degradation; Lipid metabolism; Metal-binding; Secreted; Toxin.
FT CHAIN 1..>45
FT /note="Phospholipase A2 3"
FT /evidence="ECO:0000269|PubMed:26051123"
FT /id="PRO_0000431695"
FT ACT_SITE 39
FT /evidence="ECO:0000250"
FT BINDING 20
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q8AXY1"
FT BINDING 24
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q8AXY1"
FT BINDING 25
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q8AXY1"
FT BINDING 40
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q8AXY1"
FT DISULFID 21..36
FT /evidence="ECO:0000250|UniProtKB:Q8AXY1"
FT UNSURE 2
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:26051123"
FT UNSURE 15
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:26051123"
FT UNSURE 29
FT /note="I or L"
FT /evidence="ECO:0000269|PubMed:26051123"
FT NON_CONS 7..8
FT /evidence="ECO:0000303|PubMed:26051123"
FT NON_CONS 17..18
FT /evidence="ECO:0000303|PubMed:26051123"
FT NON_CONS 26..27
FT /evidence="ECO:0000303|PubMed:26051123"
FT NON_CONS 34..35
FT /evidence="ECO:0000303|PubMed:26051123"
FT NON_TER 45
FT /evidence="ECO:0000303|PubMed:26051123"
SQ SEQUENCE 45 AA; 5314 MW; CBE6E6C093BF1B35 CRC64;
NLWQFGRVFV YPDVLCKGCY CGWGGRMDIY TYSRCCFVHD CCYGK
