PA2B1_BOTMA
ID PA2B1_BOTMA Reviewed; 121 AA.
AC P86803;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Basic phospholipase A2 BmjeTX-I;
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 a slight
CC blockade of neuromuscular contraction in an indirectly stimulated chick
CC biventer cervicis nerve-muscle preparation. Does not inhibit
CC contraction of chick biventer cervicic nerve-muscle preparation in
CC response to treatment with acetylcholine or KCl. The neuromuscular
CC blockade is mediated by inhibitory action at the presynaptic motor
CC nerve endings. Lyses skeletal myoblasts and myotubes in vitro, and
CC intramuscular injection causes local muscle necrosis. Induces edema in
CC the mouse foot pad. Induces a transient increase of IL-6 levels. PLA2
CC catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-
CC sn-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=13825.73; 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; P86803; -.
DR SMR; P86803; -.
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:0044649; P:envenomation resulting in cytolysis in another organism; IDA:UniProtKB.
DR GO; GO:0044398; P:envenomation resulting in induction of edema 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; 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-I"
FT /id="PRO_0000401141"
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; 13810 MW; F339E72DB34500DE CRC64;
DLWQFGQMIL KETGKIPFPY YGAYGCYCGW GGRGGKPKAG TDRCCYVHDC CYGKLTSCPK
TDDRYSYSWL DGTIVCGEDD PCKELCECDK KIAVCFRENL GTYNKKYRYH LKSCKKADKP
C
