PA2_BOTBS
ID PA2_BOTBS Reviewed; 98 AA.
AC P0DUN5;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 02-JUN-2021, sequence version 1.
DT 03-AUG-2022, entry version 5.
DE RecName: Full=Basic phospholipase A2 Bbil-TX {ECO:0000303|PubMed:23509754};
DE Short=svPLA2;
DE EC=3.1.1.4 {ECO:0000269|PubMed:23509754};
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Flags: Fragments;
OS Bothrops bilineatus smaragdinus (Two-striped forest-pitviper).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=2815652;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, MASS SPECTROMETRY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Venom;
RX PubMed=23509754; DOI=10.1155/2013/612649;
RA Corasolla Carregari V.C., Stuani Floriano R., Rodrigues-Simioni L.,
RA Winck F.V., Baldasso P.A., Ponce-Soto L.A., Marangoni S.;
RT "Biochemical, pharmacological, and structural characterization of new basic
RT PLA2 Bbil-TX from Bothriopsis bilineata snake venom.";
RL Biomed. Res. Int. 612649:612649-612649(2013).
RN [2]
RP FUNCTION.
RC TISSUE=Venom;
RX PubMed=23541434; DOI=10.1016/j.toxicon.2013.03.006;
RA Floriano R.S., Carregari V.C., de Abreu V.A., Kenzo-Kagawa B.,
RA Ponce-Soto L.A., da Cruz-Hoefling M.A., Hyslop S., Marangoni S.,
RA Rodrigues-Simioni L.;
RT "Pharmacological study of a new Asp49 phospholipase A(2) (Bbil-TX) isolated
RT from Bothriopsis bilineata smargadina (forest viper) venom in vertebrate
RT neuromuscular preparations.";
RL Toxicon 69:191-199(2013).
RN [3]
RP FUNCTION.
RX PubMed=25572337; DOI=10.1016/j.toxicon.2015.01.001;
RA Floriano R.S., Rocha T., Carregari V.C., Marangoni S.,
RA da Cruz-Hoefling M.A., Hyslop S., Rodrigues-Simioni L., Rowan E.G.;
RT "The neuromuscular activity of Bothriopsis bilineata smaragdina (forest
RT viper) venom and its toxin Bbil-TX (Asp49 phospholipase A2) on isolated
RT mouse nerve-muscle preparations.";
RL Toxicon 96:24-37(2015).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that induces myonecrosis,
CC when intramuscularly injected into mice (PubMed:23509754). Does not
CC show systemic myotoxic effect (after intravenous injection)
CC (PubMed:23509754). Does not show cytotoxic activities in myotubes and
CC myoblasts (PubMed:23509754). Induces marked paw edema after subplantar
CC injections (PubMed:23509754). Also induces an increase in vascular
CC permeability and in the levels of TNF-alpha, IL-6, and IL-1 cytokines
CC (PubMed:23509754). causes enzymatic-dependent neuromuscular blockade in
CC avian and mammalian neuromuscular preparations in vitro essentially by
CC a presynaptic mechanism with no significant direct action on skeletal
CC muscle function (PubMed:23541434, PubMed:25572337). PLA2 catalyzes the
CC calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-
CC phosphoglycerides (PubMed:23509754). {ECO:0000269|PubMed:23509754,
CC ECO:0000269|PubMed:23541434, ECO:0000269|PubMed:25572337}.
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:23509754};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:23509754};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by divalent cations different from
CC calcium ions (cadmium, magnesium, manganese, zinc), since they act as
CC competitive antagonists of this cofactor (PubMed:23509754). Crotapotin
CC F3 from C.durissus cascavella rattlesnake venom and antihemorrhagic
CC factor DA2-II from D.albiventris opossum sera inhibit its enzymatic
CC activity (PubMed:23509754). {ECO:0000269|PubMed:23509754}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=24.75 nmol/min/mg enzyme {ECO:0000269|PubMed:23509754};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:23509754};
CC Temperature dependence:
CC Optimum temperature is 25-37 degrees Celsius.
CC {ECO:0000269|PubMed:23509754};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23509754}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:23509754}.
CC -!- MASS SPECTROMETRY: Mass=14243.8; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:23509754};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0DUN5; -.
DR SMR; P0DUN5; -.
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 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 SMART; SM00085; PA2c; 1.
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; Neurotoxin;
KW Presynaptic neurotoxin; Secreted; Toxin.
FT CHAIN 1..98
FT /note="Basic phospholipase A2 Bbil-TX"
FT /evidence="ECO:0000269|PubMed:23509754"
FT /id="PRO_0000452896"
FT ACT_SITE 30
FT /evidence="ECO:0000250|UniProtKB:P62022"
FT ACT_SITE 65
FT /evidence="ECO:0000250|UniProtKB:P62022"
FT BINDING 19
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P62022"
FT BINDING 21
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P62022"
FT BINDING 23
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P62022"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P62022"
FT DISULFID 18..91
FT /evidence="ECO:0000250|UniProtKB:P62022"
FT DISULFID 20..27
FT /evidence="ECO:0000250|UniProtKB:P62022"
FT DISULFID 26..71
FT /evidence="ECO:0000250|UniProtKB:P62022"
FT DISULFID 32..98
FT /evidence="ECO:0000250|UniProtKB:P62022"
FT DISULFID 33..64
FT /evidence="ECO:0000250|UniProtKB:P62022"
FT DISULFID 51..62
FT /evidence="ECO:0000250|UniProtKB:P62022"
FT DISULFID 57..?
FT /evidence="ECO:0000250|UniProtKB:P62022"
FT NON_CONS 7..8
FT /evidence="ECO:0000305|PubMed:23509754"
FT NON_CONS 25..26
FT /evidence="ECO:0000305|PubMed:23509754"
FT NON_CONS 36..37
FT /evidence="ECO:0000305|PubMed:23509754"
SQ SEQUENCE 98 AA; 11409 MW; F8CB5F4093BD33AA CRC64;
HLLQFNKNAI PFYAFYGCYC GWGGRCCFVH DCCYGKWDIY PYSLKSGYIT CGKGTWCEEQ
ICECDRVAAE CLRRSLSTYK YGYMFYPDSR CRGPSETC
