PA2B1_BOTBZ
ID PA2B1_BOTBZ Reviewed; 78 AA.
AC P0DQP9; 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 myotoxin-I {ECO:0000303|PubMed:18602430};
DE Short=MTX-I {ECO:0000303|PubMed:18602430};
DE Short=svPLA2;
DE EC=3.1.1.4 {ECO:0000269|PubMed:18602430};
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Flags: Fragments;
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, SUBCELLULAR LOCATION, MASS SPECTROMETRY,
RP CATALYTIC ACTIVITY, AND COFACTOR.
RC TISSUE=Venom;
RX PubMed=18602430; DOI=10.1016/j.peptides.2008.05.021;
RA Costa T.R., Menaldo D.L., Oliveira C.Z., Santos-Filho N.A., Teixeira S.S.,
RA Nomizo A., Fuly A.L., Monteiro M.C., de Souza B.M., Palma M.S.,
RA Stabeli R.G., Sampaio S.V., Soares A.M.;
RT "Myotoxic phospholipases A(2) isolated from Bothrops brazili snake venom
RT and synthetic peptides derived from their C-terminal region: cytotoxic
RT effect on microorganism and tumor cells.";
RL Peptides 29:1645-1656(2008).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that exhibits myotoxin
CC and anticoagulant activity (PubMed:18602430). Displays edema-inducing
CC activities in mouse paw (PubMed:18602430). Also displays cytotoxic
CC activity against some cell lines and myotubes, and antimicrobial
CC activities against E.coli, C.albicans and Leishmania (PubMed:18602430).
CC PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in
CC 3-sn-phosphoglycerides. {ECO:0000269|PubMed:18602430}.
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:18602430};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:18602430};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC -!- SUBUNIT: Homodimer; non-covalently linked.
CC {ECO:0000305|PubMed:18602430}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18602430}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:18602430}.
CC -!- MASS SPECTROMETRY: Mass=13870; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:18602430};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0DQP9; -.
DR SMR; P0DQP9; -.
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 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 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..78
FT /note="Basic phospholipase A2 myotoxin-I"
FT /evidence="ECO:0000269|PubMed:18602430"
FT /id="PRO_0000449044"
FT ACT_SITE 47
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT ACT_SITE 56
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 26..?
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 28..44
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 43..62
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 49..?
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 53..?
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 55..?
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 76..?
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT NON_CONS 49..50
FT /evidence="ECO:0000305|PubMed:18602430"
FT NON_CONS 65..66
FT /evidence="ECO:0000305|PubMed:18602430"
FT NON_TER 78
FT /evidence="ECO:0000305|PubMed:18602430"
SQ SEQUENCE 78 AA; 9051 MW; 920893BB17AEDA7B CRC64;
SLWEFGQMIL KETGKLPFPY YGAYGCYCGW GGRRGPKDAT DRCCYVHDCK QICECDKAAA
VCFRERKYMA YLRVLCKK
