PA2B2_BOTMA
ID PA2B2_BOTMA Reviewed; 121 AA.
AC P86804;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Basic phospholipase A2 BmjeTX-II;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase {ECO:0000250|UniProtKB:P84397};
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] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RC TISSUE=Venom {ECO:0000269|PubMed:20195718};
RX PubMed=20195718; DOI=10.1007/s10930-010-9229-5;
RA Ponce-Soto L.A., Martins-de-Souza D., Marangoni S.;
RT "Neurotoxic, myotoxic and cytolytic activities of the new basic PLA(2)
RT isoforms BmjeTX-I and BmjeTX-II isolated from the Bothrops marajoensis
RT (Marajo Lancehead) snake venom.";
RL Protein J. 29:103-113(2010).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that induces blockade of
CC neuromuscular contraction in an indirectly stimulated chick biventer
CC cervicis nerve-muscle preparation. Does not inhibit contraction of
CC chick biventer cervicic nerve-muscle preparation in response to
CC treatment with acetylcholine or KCl. The neuromuscular blockade is
CC mediated by inhibitory action at the presynaptic motor nerve endings.
CC Lyses skeletal myoblasts and myotubes in vitro, and intramuscular
CC injection causes local muscle necrosis. Induces edema in the mouse foot
CC pad. Induces a transient increase of IL-6 levels. PLA2 catalyzes the
CC calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-
CC phosphoglycerides. {ECO:0000269|PubMed:20195718}.
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|PubMed:20195718};
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|PubMed:20195718}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:20195718}.
CC -!- MASS SPECTROMETRY: Mass=13881.48; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:20195718};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P86804; -.
DR SMR; P86804; -.
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; IDA:UniProtKB.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0044649; P:envenomation resulting in cytolysis in another organism; IDA:UniProtKB.
DR GO; GO:0044521; P:envenomation resulting in muscle damage in another organism; IDA:UniProtKB.
DR GO; GO:0009395; P:phospholipid catabolic process; IDA:UniProtKB.
DR CDD; cd00125; PLA2c; 1.
DR Gene3D; 1.20.90.10; -; 1.
DR InterPro; IPR001211; PLipase_A2.
DR InterPro; IPR033112; PLipase_A2_Asp_AS.
DR InterPro; IPR016090; PLipase_A2_dom.
DR InterPro; IPR036444; PLipase_A2_dom_sf.
DR InterPro; IPR033113; PLipase_A2_His_AS.
DR PANTHER; PTHR11716; PTHR11716; 1.
DR Pfam; PF00068; Phospholip_A2_1; 1.
DR PRINTS; PR00389; PHPHLIPASEA2.
DR SMART; SM00085; PA2c; 1.
DR SUPFAM; SSF48619; SSF48619; 1.
DR PROSITE; PS00119; PA2_ASP; 1.
DR PROSITE; PS00118; PA2_HIS; 1.
PE 1: Evidence at protein level;
KW Calcium; Cytolysis; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Lipid degradation; Lipid metabolism; Metal-binding; Myotoxin; Neurotoxin;
KW Presynaptic neurotoxin; Secreted; Toxin.
FT CHAIN 1..121
FT /note="Basic phospholipase A2 BmjeTX-II"
FT /id="PRO_0000401142"
FT ACT_SITE 48
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT ACT_SITE 89
FT /evidence="ECO:0000250|UniProtKB:P59071"
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..114
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 28..45
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 44..95
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 50..121
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 51..88
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 58..82
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 76..86
FT /evidence="ECO:0000250|UniProtKB:P59071"
SQ SEQUENCE 121 AA; 13865 MW; FAC644A79E017227 CRC64;
DLWQWGQMIL KETGKIPFSY YGAYGCYCGW GGRGGKPKAG TDRCCYVHDC CYGKLTSCPK
TDDRYSYSRL DLTIVCGEDD PCKELCECDK KIAVCFRENL GTYNKKYRYH LKSCKKADKP
C
