PA23_BOTMT
ID PA23_BOTMT Reviewed; 32 AA.
AC P0DMK1;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 1.
DT 03-AUG-2022, entry version 18.
DE RecName: Full=Basic phospholipase A2 BmatTX-III {ECO:0000303|PubMed:24724078};
DE Short=svPLA2;
DE EC=3.1.1.4 {ECO:0000269|PubMed:24724078};
DE AltName: Full=Asp49 PLA2;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Flags: Fragment;
OS Bothrops matogrossensis (Pitviper) (Bothrops neuwiedi matogrossensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=1171125;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, SUBUNIT, CATALYTIC ACTIVITY, MASS SPECTROMETRY,
RP AND SUBCELLULAR LOCATION.
RX PubMed=24724078; DOI=10.1155/2014/195356;
RA de Moura A.A., Kayano A.M., Oliveira G.A., Setubal S.S., Ribeiro J.G.,
RA Barros N.B., Nicolete R., Moura L.A., Fuly A.L., Nomizo A., da Silva S.L.,
RA Fernandes C.F., Zuliani J.P., Stabeli R.G., Soares A.M., Calderon L.A.;
RT "Purification and biochemical characterization of three myotoxins from
RT Bothrops mattogrossensis snake venom with toxicity against Leishmania and
RT tumor cells.";
RL Biomed. Res. Int. 2014:1-13(2014).
CC -!- FUNCTION: Snake venom phospholipase A2 that shows high myotoxic
CC activity, slight neutrophil activation (demonstrated by activation
CC induction of IL-1beta production), slight cytotoxicity against tumor
CC cell lines (T leukemia and breast adenocarcinoma), and slight
CC antiparasitic activity against promastigote forms of Leishmania
CC amazonensis. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-
CC acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:24724078}.
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:24724078};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:24724078}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24724078}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:24724078}.
CC -!- MASS SPECTROMETRY: Mass=13681; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:24724078};
CC -!- MISCELLANEOUS: Does not induce platelet aggregation and does not
CC inhibit collagen or ADP-induced platelet aggregation.
CC {ECO:0000305|PubMed:24724078}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC K49 sub-subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0DMK1; -.
DR SMR; P0DMK1; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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 Gene3D; 1.20.90.10; -; 1.
DR InterPro; IPR001211; PLipase_A2.
DR InterPro; IPR016090; PLipase_A2_dom.
DR InterPro; IPR036444; PLipase_A2_dom_sf.
DR Pfam; PF00068; Phospholip_A2_1; 1.
DR PRINTS; PR00389; PHPHLIPASEA2.
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; Myotoxin; Secreted;
KW Toxin.
FT CHAIN 1..>32
FT /note="Basic phospholipase A2 BmatTX-III"
FT /id="PRO_0000429742"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 26..?
FT /evidence="ECO:0000250|UniProtKB:Q90249"
FT DISULFID 28..?
FT /evidence="ECO:0000250|UniProtKB:Q90249"
FT NON_TER 32
SQ SEQUENCE 32 AA; 3522 MW; 623724AAB76B9D21 CRC64;
DLWELAKMIL KETGKNPLPS YGAYGCYCGW GG
