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Phospholipase D LbSicTox-alphaIB1a (PLD) (EC 3.1.4.4) (Dermonecrotic toxin) (Lb1) (Sphingomyelin phosphodiesterase D 1) (SMD 1) (SMase D 1) (Sphingomyelinase D 1)

 A1KA_LOXBO              Reviewed;         279 AA.
Q5YD77;
06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
23-NOV-2004, sequence version 1.
15-FEB-2017, entry version 50.
RecName: Full=Phospholipase D LbSicTox-alphaIB1a;
Short=PLD;
EC=3.1.4.4;
AltName: Full=Dermonecrotic toxin;
AltName: Full=Lb1;
AltName: Full=Sphingomyelin phosphodiesterase D 1;
Short=SMD 1;
Short=SMase D 1;
Short=Sphingomyelinase D 1;
Loxosceles boneti (North American fiddleback spider).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
Araneae; Araneomorphae; Haplogynae; Sicariidae; Loxosceles.
NCBI_TaxID=283164;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-35, AND FUNCTION.
TISSUE=Venom, and Venom gland;
PubMed=15450925; DOI=10.1016/j.toxicon.2004.06.013;
Ramos-Cerrillo B., Olvera A., Odell G.V., Zamudio F.,
Paniagua-Solis J., Alagon A., Stock R.P.;
"Genetic and enzymatic characterization of sphingomyelinase D isoforms
from the North American fiddleback spiders Loxosceles boneti and
Loxosceles reclusa.";
Toxicon 44:507-514(2004).
[2]
FUNCTION, AND TOXIC DOSE.
PubMed=16759681; DOI=10.1016/j.toxicon.2006.04.010;
Olvera A., Ramos-Cerrillo B., Estevez J., Clement H., de Roodt A.,
Paniagua-Solis J., Vazquez H., Zavaleta A., Arruz M.S., Stock R.P.,
Alagon A.;
"North and south american Loxosceles spiders: development of a
polyvalent antivenom with recombinant sphingomyelinases D as
antigens.";
Toxicon 48:64-74(2006).
-!- FUNCTION: Catalyzes the hydrolysis of sphingomyelin (about 31.5
U/mg). May also act on other phosphatidyl esters. May induce
complement-dependent hemolysis, dermonecrosis, blood vessel
permeability and platelet aggregation.
{ECO:0000269|PubMed:15450925, ECO:0000269|PubMed:16759681}.
-!- CATALYTIC ACTIVITY: A phosphatidylcholine + H(2)O = choline + a
phosphatidate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
-!- TOXIC DOSE: LD(50) is 200-250 ug/kg by intraperitoneal injection
into mice. {ECO:0000269|PubMed:16759681}.
-!- SIMILARITY: Belongs to the arthropod phospholipase D family. Class
II subfamily. {ECO:0000305}.
-!- CAUTION: Dermonecrotic toxins were previously known as
sphingomyelin phosphodiesterase D based on their ability to
hydrolyze sphingomyelin into choline and acylsphingosine
phosphate. Based on additional biochemical analysis, the enzymes
have been renamed phospholipase D to represent a more accurate and
broader denomination. {ECO:0000305}.
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EMBL; AY559844; AAT66073.1; -; mRNA.
ProteinModelPortal; Q5YD77; -.
SMR; Q5YD77; -.
ArachnoServer; AS000519; Sphingomyelinase D (LbSicTox-alphaIB1a).
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-EC.
GO; GO:0044179; P:hemolysis in other organism; IEA:UniProtKB-KW.
GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
Gene3D; 3.20.20.190; -; 1.
InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
SUPFAM; SSF51695; SSF51695; 2.
1: Evidence at protein level;
Complement system impairing toxin; Cytolysis; Dermonecrotic toxin;
Direct protein sequencing; Disulfide bond; Hemolysis; Hydrolase;
Magnesium; Metal-binding; Secreted; Toxin.
CHAIN 1 279 Phospholipase D LbSicTox-alphaIB1a.
/FTId=PRO_0000279554.
DOMAIN 220 250 GDPD.
ACT_SITE 11 11 {ECO:0000250}.
ACT_SITE 47 47 Nucleophile. {ECO:0000250}.
METAL 31 31 Magnesium. {ECO:0000250}.
METAL 33 33 Magnesium. {ECO:0000250}.
METAL 91 91 Magnesium. {ECO:0000250}.
SITE 227 227 Important for catalytic activity.
{ECO:0000250}.
SITE 246 246 Important for catalytic activity.
{ECO:0000250}.
DISULFID 51 57 {ECO:0000250}.
DISULFID 53 196 {ECO:0000250}.
CONFLICT 6 6 A -> V (in Ref. 1; AA sequence).
{ECO:0000305}.
SEQUENCE 279 AA; 30997 MW; DB34384AB755A847 CRC64;
ANKRPAWIMG HMVNAIAQID EFVNLGANSI ETDVSFDSSA NPEYTYHGIP CDCGRTCTKW
ENFNDFLVGL RKATTPDDSN YHEKLILVVF DLKTGSLYDN QAYDAGKKLA KSILQHYWNN
GNNGGRAYIV LSIPNLAHYK LITGFKETLT SDGHPELMDK IGYDFSGNDA IGDVASAYQK
AGVTGHVWQS DGITNCLLRG LSRVREAVAN RDSSNGYINK VYYWTVDKRA STRDALDAGV
DGIMTNYPDV IADVLSESAY SAKFRIATYD DNPWETFKN


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