PA2A_BOTMO
ID PA2A_BOTMO Reviewed; 138 AA.
AC G3DT18;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Acidic phospholipase A2 BmooPLA2;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Flags: Precursor;
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 NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MASS SPECTROMETRY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=22571953; DOI=10.1016/j.jpba.2012.04.008;
RA Silveira L.B., Marchi-Salvador D.P., Santos-Filho N.A., Silva F.P. Jr.,
RA Marcussi S., Fuly A.L., Nomizo A., da Silva S.L., Stabeli R.G.,
RA Arantes E.C., Soares A.M.;
RT "Isolation and expression of a hypotensive and anti-platelet acidic
RT phospholipase A(2) from Bothrops moojeni snake venom.";
RL J. Pharm. Biomed. Anal. 73:35-43(2013).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits ADP- and
CC collagen-induced platelet aggregation, has edema-inducing, anti-
CC coagulant activity, antibacterial activity, and cytotoxic activity. In
CC vivo, has a hypotensive effect. PLA2 catalyzes the calcium-dependent
CC hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
CC {ECO:0000269|PubMed:22571953}.
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; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=13601; Method=MALDI; Note=Average mass.;
CC Evidence={ECO:0000269|PubMed:22571953};
CC -!- MISCELLANEOUS: Does not show myotoxic activity.
CC {ECO:0000305|PubMed:22571953}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR EMBL; HQ327311; ADQ08654.1; -; mRNA.
DR AlphaFoldDB; G3DT18; -.
DR SMR; G3DT18; -.
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 GO; GO:0008217; P:regulation of blood pressure; IEA:UniProtKB-KW.
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 Antibiotic; Antimicrobial; Blood coagulation cascade inhibiting toxin;
KW Calcium; Disulfide bond; Hemostasis impairing toxin; Hydrolase;
KW Hypotensive agent; Lipid degradation; Lipid metabolism; Metal-binding;
KW Platelet aggregation inhibiting toxin; Secreted; Signal; Toxin.
FT SIGNAL 1..16
FT /evidence="ECO:0000250"
FT CHAIN 17..138
FT /note="Acidic phospholipase A2 BmooPLA2"
FT /id="PRO_5000793120"
FT ACT_SITE 63
FT /evidence="ECO:0000250|UniProtKB:P06859"
FT ACT_SITE 105
FT /evidence="ECO:0000250|UniProtKB:P06859"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 42..131
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 44..60
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 59..111
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 65..138
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 66..104
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 73..97
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 91..102
FT /evidence="ECO:0000250|UniProtKB:O42191"
SQ SEQUENCE 138 AA; 15680 MW; 6C3070733C7B576D CRC64;
MRTLWIVAVL LLGVEGNLWQ FEMLIMKIAK TSGFLFYSSY GCYCGWGGHG RPQDATDRCC
FVHDCCYGKV TGCNPKTDSY TYSEENGDVV CGGDDPCKKQ ICECDRVAAT CFRDNKDTYD
NKYWFYPAKN CQEESEPC
