PA2A1_BOTPI
ID PA2A1_BOTPI Reviewed; 122 AA.
AC C9DPL5;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Acidic phospholipase A2 BpirPLA2-I;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase 1B;
OS Bothrops pirajai (Piraja'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=113192;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-61, SYNTHESIS OF 1-14;
RP 61-71 AND 105-117, MOTIF, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY
RP REGULATION, AND 3D-STRUCTURE MODELING.
RC TISSUE=Venom, and Venom gland;
RX PubMed=21331602; DOI=10.1007/s00204-011-0665-6;
RA Teixeira S.S., Silveira L.B., da Silva F.M., Marchi-Salvador D.P.,
RA Silva F.P. Jr., Izidoro L.F., Fuly A.L., Juliano M.A., Dos Santos C.R.,
RA Murakami M.T., Sampaio S.V., da Silva S.L., Soares A.M.;
RT "Molecular characterization of an acidic phospholipase A(2) from Bothrops
RT pirajai snake venom: synthetic C-terminal peptide identifies its
RT antiplatelet region.";
RL Arch. Toxicol. 85:1219-1233(2011).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits
CC collagen/ADP-induced platelet aggregation, and induces hypotension in
CC rats (activity abolished in the presence of p-bromophenacyl bromide).
CC PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in
CC 3-sn-phosphoglycerides. {ECO:0000269|PubMed:21331602}.
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, ECO:0000269|PubMed:21331602};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA and p-bromophenacyl bromide
CC (BPB). {ECO:0000269|PubMed:21331602}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MISCELLANEOUS: This enzyme does not show myotoxic activity.
CC {ECO:0000305|PubMed:21331602}.
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 EMBL; GQ406049; ACV87234.1; -; mRNA.
DR AlphaFoldDB; C9DPL5; -.
DR SMR; C9DPL5; -.
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 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 Calcium; Direct protein sequencing; Disulfide bond;
KW Hemostasis impairing toxin; Hydrolase; Hypotensive agent;
KW Lipid degradation; Lipid metabolism; Metal-binding;
KW Platelet aggregation inhibiting toxin; Secreted; Toxin.
FT CHAIN 1..122
FT /note="Acidic phospholipase A2 BpirPLA2-I"
FT /id="PRO_0000413802"
FT MOTIF 105..117
FT /note="Antiplatelet activity"
FT ACT_SITE 47
FT /evidence="ECO:0000250|UniProtKB:P06859"
FT ACT_SITE 89
FT /evidence="ECO:0000250|UniProtKB:P06859"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 26..115
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 28..44
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 43..95
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 49..122
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 50..88
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 57..81
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 75..86
FT /evidence="ECO:0000250|UniProtKB:O42191"
SQ SEQUENCE 122 AA; 13636 MW; 7C06ADFD15DAE8BA CRC64;
NLWQFGKLIM KIAGESGVFK YLSYGCYCGL GGQGQPTDAT DRCCFVHDCC YGKVTGCDPK
IDSYTYSKEN GDVVCGGDDP CKKQICECDR VAATCFRDNK DTYDIKYWFY GAKNCQEESE
PC
