ID   PA2B3_BOTMA             Reviewed;          50 AA.
AC   B3A0N3;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 27.
DE   RecName: Full=Basic phospholipase A2 Bmaj-9 {ECO:0000303|Ref.1};
DE            Short=svPLA2 {ECO:0000303|Ref.1};
DE            EC=3.1.1.4 {ECO:0000269|Ref.1};
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase {ECO:0000250|UniProtKB:P86804};
DE   Flags: Fragment;
OS   Bothrops marajoensis (Marajo lancehead).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=157554;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Venom {ECO:0000303|Ref.1};
RX   DOI=10.1590/S1678-91992012000100008;
RA   Galbiatti C., Rocha T., Randazzo-Moura P., Ponce-Soto L.A., Marangoni S.,
RA   Cruz-Hoefling M.A., Rodrigues-Simioni L.;
RT   "Pharmacological and partial biochemical characterization of Bmaj-9
RT   isolated from Bothrops marajoensis snake venom.";
RL   J. Venom. Anim. Toxins Incl. Trop. Dis. 18:62-72(2012).
CC   -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that causes irreversible
CC       neuromuscular blockade in chick biventer cervicis muscle preparations.
CC       The neuromuscular blockade is mediated by inhibitory action at the
CC       presynaptic motor nerve endings. PLA2 catalyzes the calcium-dependent
CC       hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
CC       {ECO:0000269|Ref.1}.
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:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-
CC         ProRule:PRU10036, ECO:0000269|Ref.1};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:P59071};
CC       Note=Binds 1 Ca(2+) ion. {ECO:0000250|UniProtKB:P59071};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305|Ref.1}.
CC   -!- MASS SPECTROMETRY: Mass=13679.33; Method=MALDI;
CC       Evidence={ECO:0000269|Ref.1};
CC   -!- MISCELLANEOUS: Does not show myotoxicity. {ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC       D49 sub-subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; B3A0N3; -.
DR   SMR; B3A0N3; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004623; F:phospholipase A2 activity; IDA:UniProtKB.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR   GO; GO:0044487; P:envenomation resulting in modulation of transmission of nerve impulse in another organism; IDA:UniProtKB.
DR   GO; GO:0009395; P:phospholipid catabolic process; IDA:UniProtKB.
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   PANTHER; PTHR11716; PTHR11716; 1.
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; Neurotoxin;
KW   Presynaptic neurotoxin; Secreted; Toxin.
FT   CHAIN           1..>50
FT                   /note="Basic phospholipase A2 Bmaj-9"
FT                   /evidence="ECO:0000269|Ref.1"
FT                   /id="PRO_0000414628"
FT   ACT_SITE        48
FT                   /evidence="ECO:0000250|UniProtKB:P59071,
FT                   ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-
FT                   ProRule:PRU10036"
FT   BINDING         27
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P59071"
FT   BINDING         29
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P59071"
FT   BINDING         31
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P59071"
FT   BINDING         49
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P59071"
FT   DISULFID        26..?
FT                   /evidence="ECO:0000250|UniProtKB:P59071"
FT   DISULFID        28..45
FT                   /evidence="ECO:0000250|UniProtKB:P59071"
FT   DISULFID        44..?
FT                   /evidence="ECO:0000250|UniProtKB:P59071"
FT   DISULFID        50..?
FT                   /evidence="ECO:0000250|UniProtKB:P59071"
FT   NON_TER         50
FT                   /evidence="ECO:0000303|Ref.1"
SQ   SEQUENCE   50 AA;  5714 MW;  3BA5719D8E43F4B5 CRC64;
     DLWQWGQMIL KETGKLPFSY YTAYGCYCGW GGRGGKPKAD TDRCCFVHDC