PA2B3_BOTBZ
ID PA2B3_BOTBZ Reviewed; 121 AA.
AC P0DQQ0; P0DTS7;
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 BbTX-III {ECO:0000303|PubMed:19539640};
DE Short=svPLA2;
DE EC=3.1.1.4 {ECO:0000269|PubMed:19539640};
DE AltName: Full=Brazilitoxin III {ECO:0000303|PubMed:19539640};
DE Short=BbTX-III {ECO:0000303|PubMed:19539640};
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
OS Bothrops brazili (Brazil's lancehead).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=157546;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR
RP LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC TISSUE=Venom;
RX PubMed=19539640; DOI=10.1016/j.toxicon.2009.06.008;
RA Huancahuire-Vega S., Ponce-Soto L.A., Martins-de-Souza D., Marangoni S.;
RT "Structural and functional characterization of brazilitoxins II and III
RT (BbTX-II and -III), two myotoxins from the venom of Bothrops brazili
RT snake.";
RL Toxicon 54:818-827(2009).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that exhibits myotoxin
CC and anticoagulant activity (PubMed:19539640). Displays edema-inducing
CC activities in mouse paw (PubMed:19539640). Also displays cytotoxic
CC activity against some cell lines and myotubes, and antimicrobial
CC activities against E.coli, C.albicans and Leishmania (PubMed:19539640).
CC PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in
CC 3-sn-phosphoglycerides. {ECO:0000269|PubMed:19539640}.
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:19539640};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:19539640};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:19539640};
CC Temperature dependence:
CC Optimum temperature is 35-45 degrees Celsius.
CC {ECO:0000269|PubMed:19539640};
CC -!- SUBUNIT: Homodimer; non-covalently linked.
CC {ECO:0000269|PubMed:19539640}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19539640}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:19539640}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0DQQ0; -.
DR SMR; P0DQQ0; -.
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:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
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 PRINTS; PR00389; PHPHLIPASEA2.
DR SMART; SM00085; PA2c; 1.
DR SUPFAM; SSF48619; SSF48619; 1.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Blood coagulation cascade inhibiting toxin;
KW Calcium; Direct protein sequencing; Disulfide bond;
KW Hemostasis impairing toxin; Hydrolase; Lipid degradation; Lipid metabolism;
KW Metal-binding; Myotoxin; Secreted; Toxin.
FT CHAIN 1..121
FT /note="Basic phospholipase A2 BbTX-III"
FT /evidence="ECO:0000269|PubMed:19539640"
FT /id="PRO_0000453020"
FT ACT_SITE 47
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 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 28..44
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 43..95
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 49..121
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 50..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; 14144 MW; 823837FEDD15C145 CRC64;
SLWEWGQMIL KETGKNPFPY YGAYGCYCGW GGRRKPKDAT DRCCFVHDCC RYKKLTGCPK
TNDRYSYSRL DYTIVCGEDD PCKEICECDK AAAVCFRENL RTYNKKYMAH LRVLCKKDKP
C
