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Basic phospholipase A2 A (svPLA2) (EC 3.1.1.4) (Crotoxin basic chain 1) (Phosphatidylcholine 2-acylhydrolase)

 PA2BA_CRODR             Reviewed;         122 AA.
P86169;
10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
10-FEB-2009, sequence version 1.
22-NOV-2017, entry version 28.
RecName: Full=Basic phospholipase A2 A;
Short=svPLA2;
EC=3.1.1.4;
AltName: Full=Crotoxin basic chain 1 {ECO:0000303|PubMed:19013478};
AltName: Full=Phosphatidylcholine 2-acylhydrolase {ECO:0000303|PubMed:19013478};
Crotalus durissus ruruima (South American rattlesnake) (Mt. Roraima
rattlesnake).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
NCBI_TaxID=221570;
[1] {ECO:0000305}
PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND MASS SPECTROMETRY.
TISSUE=Venom {ECO:0000269|PubMed:19013478};
PubMed=19013478; DOI=10.1016/j.toxicon.2008.10.021;
Diz Filho E.B.S., Marangoni S., Toyama D.O., Fagundes F.H.R.,
Oliveira S.C.B., Fonseca F.V., Calgarotto A.K., Joazeiro P.P.,
Toyama M.H.;
"Enzymatic and structural characterization of new PLA2 isoform
isolated from white venom of Crotalus durissus ruruima.";
Toxicon 53:104-114(2009).
-!- FUNCTION: Snake venom phospholipase A that has strong
antimicrobial activity against the Gram-negative bacterium
X.axonopodis. Antimicrobial activity is not abolished by EDTA or
p-BPB and is therefore not strongly dependent on the enzymatic
activity. PLA2 catalyzes the calcium-dependent hydrolysis of the
2-acyl groups in 3-sn-phosphoglycerides.
{ECO:0000269|PubMed:19013478}.
-!- CATALYTIC ACTIVITY: Phosphatidylcholine + H(2)O = 1-
acylglycerophosphocholine + a carboxylate. {ECO:0000255|PROSITE-
ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036,
ECO:0000269|PubMed:19013478}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:19013478};
Note=Binds 1 Ca(2+) ion. {ECO:0000269|PubMed:19013478};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=2.3 mM for NOBA {ECO:0000269|PubMed:19013478};
Vmax=377 nmol/min/mg enzyme for NOBA
{ECO:0000269|PubMed:19013478};
pH dependence:
Optimum pH is 8.0. {ECO:0000269|PubMed:19013478};
Temperature dependence:
Optimum temperature is 40 degrees Celsius.
{ECO:0000269|PubMed:19013478};
-!- SUBUNIT: This toxin consists of 2 subunits: acidic and basic. The
acidic subunit is non-toxic, without enzymatic activity and
comprises 3 peptides that are cross-linked by 7 disulfide bridges.
The basic subunit is toxic, has phospholipase A2 activity and is
composed of a single chain. {ECO:0000269|PubMed:19013478}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19013478}.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
{ECO:0000269|PubMed:19013478}.
-!- MASS SPECTROMETRY: Mass=14299.34; Method=MALDI; Range=1-122;
Evidence={ECO:0000269|PubMed:19013478};
-!- SIMILARITY: Belongs to the phospholipase A2 family. Group II
subfamily. D49 sub-subfamily. {ECO:0000305}.
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SMR; P86169; -.
HOVERGEN; HBG008137; -.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0072556; C:other organism presynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0004623; F:phospholipase A2 activity; IDA:UniProtKB.
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:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
GO; GO:0009405; P:pathogenesis; IDA:UniProtKB.
GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
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;
Antibiotic; Antimicrobial; Calcium; Direct protein sequencing;
Disulfide bond; Hydrolase; Lipid degradation; Lipid metabolism;
Metal-binding; Neurotoxin; Presynaptic neurotoxin; Secreted; Toxin.
CHAIN 1 122 Basic phospholipase A2 A.
/FTId=PRO_0000363990.
ACT_SITE 47 47 {ECO:0000250|UniProtKB:P14421}.
ACT_SITE 89 89 {ECO:0000250|UniProtKB:P14421}.
METAL 27 27 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P14421}.
METAL 29 29 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P14421}.
METAL 31 31 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P14421}.
METAL 48 48 Calcium. {ECO:0000250|UniProtKB:P14421}.
DISULFID 26 115 {ECO:0000250|UniProtKB:P14421}.
DISULFID 28 44 {ECO:0000250|UniProtKB:P14421}.
DISULFID 43 95 {ECO:0000250|UniProtKB:P14421}.
DISULFID 49 122 {ECO:0000250|UniProtKB:P14421}.
DISULFID 50 88 {ECO:0000250|UniProtKB:P14421}.
DISULFID 57 81 {ECO:0000250|UniProtKB:P14421}.
DISULFID 75 86 {ECO:0000250|UniProtKB:P14421}.
SEQUENCE 122 AA; 14199 MW; CC5CFF491931C79A CRC64;
HLLQFNKMIK FETRKNAIPF YAFYGCYCGW GGRGRPKDAT DRCCFVHDCC YGKLAKCNTK
WDIYPYSLKS GYITCGKGTW CEEQICECDR VAAECLRRSL STYKYGYMFY PDSRCRGPSE
TC


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