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Acidic phospholipase A2 BpirPLA2-I (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase 1B)

 PA2A1_BOTPI             Reviewed;         122 AA.
C9DPL5;
16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
03-NOV-2009, sequence version 1.
23-MAY-2018, entry version 33.
RecName: Full=Acidic phospholipase A2 BpirPLA2-I;
Short=svPLA2;
EC=3.1.1.4;
AltName: Full=Phosphatidylcholine 2-acylhydrolase 1B;
Bothrops pirajai (Piraja's lance0 head).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
NCBI_TaxID=113192;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-61, SYNTHESIS OF
1-14; 61-71 AND 105-117, MOTIF, FUNCTION, CATALYTIC ACTIVITY,
COFACTOR, ENZYME REGULATION, AND 3D-STRUCTURE MODELING.
TISSUE=Venom, and Venom gland;
PubMed=21331602; DOI=10.1007/s00204-011-0665-6;
Teixeira S.S., Silveira L.B., da Silva F.M., Marchi-Salvador D.P.,
Silva F.P. Jr., Izidoro L.F., Fuly A.L., Juliano M.A.,
Dos Santos C.R., Murakami M.T., Sampaio S.V., da Silva S.L.,
Soares A.M.;
"Molecular characterization of an acidic phospholipase A(2) from
Bothrops pirajai snake venom: synthetic C-terminal peptide identifies
its antiplatelet region.";
Arch. Toxicol. 85:1219-1233(2011).
-!- FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits
collagen/ADP-induced platelet aggregation, and induces hypotension
in rats (activity abolished in the presence of p-bromophenacyl
bromide). PLA2 catalyzes the calcium-dependent hydrolysis of the
2-acyl groups in 3-sn-phosphoglycerides.
{ECO:0000269|PubMed:21331602}.
-!- CATALYTIC ACTIVITY: Phosphatidylcholine + H(2)O = 1-
acylglycerophosphocholine + a carboxylate. {ECO:0000255|PROSITE-
ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036,
ECO:0000269|PubMed:21331602}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
Note=Binds 1 Ca(2+) ion. {ECO:0000250};
-!- ENZYME REGULATION: Inhibited by EDTA and p-bromophenacyl bromide
(BPB). {ECO:0000269|PubMed:21331602}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
-!- MISCELLANEOUS: This enzyme does not show myotoxic activity.
{ECO:0000305|PubMed:21331602}.
-!- SIMILARITY: Belongs to the phospholipase A2 family. Group II
subfamily. D49 sub-subfamily. {ECO:0000305}.
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EMBL; GQ406049; ACV87234.1; -; mRNA.
SMR; C9DPL5; -.
PRIDE; C9DPL5; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
GO; GO:0102567; F:phospholipase A2 activity (consuming 1,2-dipalmitoylphosphatidylcholine); IEA:UniProtKB-EC.
GO; GO:0102568; F:phospholipase A2 activity consuming 1,2-dioleoylphosphatidylethanolamine); IEA:UniProtKB-EC.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
GO; GO:0008217; P:regulation of blood pressure; IEA:UniProtKB-KW.
CDD; cd00125; PLA2c; 1.
Gene3D; 1.20.90.10; -; 1.
InterPro; IPR001211; PLipase_A2.
InterPro; IPR033112; PLipase_A2_Asp_AS.
InterPro; IPR016090; PLipase_A2_dom.
InterPro; IPR036444; PLipase_A2_dom_sf.
InterPro; IPR033113; PLipase_A2_His_AS.
PANTHER; PTHR11716; PTHR11716; 1.
Pfam; PF00068; Phospholip_A2_1; 1.
PRINTS; PR00389; PHPHLIPASEA2.
SMART; SM00085; PA2c; 1.
SUPFAM; SSF48619; SSF48619; 1.
PROSITE; PS00119; PA2_ASP; 1.
PROSITE; PS00118; PA2_HIS; 1.
1: Evidence at protein level;
Calcium; Direct protein sequencing; Disulfide bond;
Hemostasis impairing toxin; Hydrolase; Hypotensive agent;
Lipid degradation; Lipid metabolism; Metal-binding;
Platelet aggregation inhibiting toxin; Secreted; Toxin.
CHAIN 1 122 Acidic phospholipase A2 BpirPLA2-I.
/FTId=PRO_0000413802.
MOTIF 105 117 Antiplatelet activity.
ACT_SITE 47 47 {ECO:0000250}.
ACT_SITE 89 89 {ECO:0000250}.
METAL 27 27 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 29 29 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 31 31 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 48 48 Calcium. {ECO:0000250}.
DISULFID 26 115 {ECO:0000250}.
DISULFID 28 44 {ECO:0000250}.
DISULFID 43 95 {ECO:0000250}.
DISULFID 49 122 {ECO:0000250}.
DISULFID 50 88 {ECO:0000250}.
DISULFID 57 81 {ECO:0000250}.
DISULFID 75 86 {ECO:0000250}.
SEQUENCE 122 AA; 13636 MW; 7C06ADFD15DAE8BA CRC64;
NLWQFGKLIM KIAGESGVFK YLSYGCYCGL GGQGQPTDAT DRCCFVHDCC YGKVTGCDPK
IDSYTYSKEN GDVVCGGDDP CKKQICECDR VAATCFRDNK DTYDIKYWFY GAKNCQEESE
PC


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