PA2B1_BOTMO
ID PA2B1_BOTMO Reviewed; 121 AA.
AC P0C8M1;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Basic phospholipase A2 BmTX-I;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
OS Bothrops moojeni (Lance-headed viper) (Caissaca).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=98334;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=18501940; DOI=10.1016/j.toxicon.2008.03.030;
RA Calgarotto A.K., Damico D.C.S., Ponce-Soto L.A., Baldasso P.A.,
RA Da Silva S.L., Souza G.H.M.F., Eberlin M.N., Marangoni S.;
RT "Biological and biochemical characterization of new basic phospholipase
RT A(2) BmTX-I isolated from Bothrops moojeni snake venom.";
RL Toxicon 51:1509-1519(2008).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that shows enzymatic
CC activity in the presence of a synthetic substrate. In vitro, blocks the
CC neuromuscular transmission in young chick biventer cervicis
CC preparations. In mice, induces myonecrosis and a systemic interleukin-6
CC response upon intramuscular injection. Also induces edema and exerts a
CC strong pro-inflammatory effect. PLA2 catalyzes the calcium-dependent
CC hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
CC {ECO:0000269|PubMed:18501940}.
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};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:18501940};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000269|PubMed:18501940};
CC -!- ACTIVITY REGULATION: Inhibited by magnesium, cadmium and manganese
CC ions. Also inhibited by crotapotin. {ECO:0000269|PubMed:18501940}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:18501940};
CC Temperature dependence:
CC Optimum temperature is 35-45 degrees Celsius.
CC {ECO:0000269|PubMed:18501940};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18501940}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=14238.71; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18501940};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; P0C8M1; -.
DR SMR; P0C8M1; -.
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 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 Secreted; Toxin.
FT CHAIN 1..121
FT /note="Basic phospholipase A2 BmTX-I"
FT /id="PRO_0000359436"
FT ACT_SITE 48
FT /evidence="ECO:0000250"
FT ACT_SITE 89
FT /evidence="ECO:0000250"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 26..114
FT /evidence="ECO:0000250"
FT DISULFID 28..45
FT /evidence="ECO:0000250"
FT DISULFID 44..95
FT /evidence="ECO:0000250"
FT DISULFID 50..121
FT /evidence="ECO:0000250"
FT DISULFID 51..88
FT /evidence="ECO:0000250"
FT DISULFID 58..82
FT /evidence="ECO:0000250"
FT DISULFID 76..86
FT /evidence="ECO:0000250"
SQ SEQUENCE 121 AA; 14081 MW; 4441455A8D14F766 CRC64;
DLWQFNKMIK KEVGKLPFPF YGAYGCYCGW GGRGEKPKDG TDRCCFVHDC CYKKLTGCPK
WDDRYSYSWK DITIVCGEDL PCEEICECDR AAAVCFYENL GTYNKKYMKH LKPCKKADYP
C
