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Phospholipase D LbSicTox-betaIA1a (PLD) (EC 3.1.-.-) (Dermonecrotic toxin) (Lb3) (Sphingomyelin phosphodiesterase D-like protein 3) (Sphingomyelinase D)

 B1HA_LOXBO              Reviewed;         278 AA.
Q5YD76;
06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
06-MAR-2007, sequence version 2.
10-MAY-2017, entry version 40.
RecName: Full=Phospholipase D LbSicTox-betaIA1a;
Short=PLD;
EC=3.1.-.-;
AltName: Full=Dermonecrotic toxin;
AltName: Full=Lb3;
AltName: Full=Sphingomyelin phosphodiesterase D-like protein 3;
AltName: Full=Sphingomyelinase D;
Loxosceles boneti (North American fiddleback spider).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
Araneae; Araneomorphae; Haplogynae; Sicariidae; Loxosceles.
NCBI_TaxID=283164;
[1]
NUCLEOTIDE SEQUENCE [MRNA] OF 3-278, AND PROTEIN SEQUENCE OF 1-24.
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).
-!- FUNCTION: Does not have sphingomyelinase and dermonecrotic
activities.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000305};
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
-!- 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; AY559845; AAT66074.1; -; mRNA.
ProteinModelPortal; Q5YD76; -.
ArachnoServer; AS000151; Sphingomyelinase D (LbSicTox-betaIA1a).
BRENDA; 3.1.4.41; 8288.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
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;
Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
Magnesium; Metal-binding; Secreted.
CHAIN 1 278 Phospholipase D LbSicTox-betaIA1a.
/FTId=PRO_0000279556.
DOMAIN 222 252 GDPD.
ACT_SITE 12 12 {ECO:0000250}.
ACT_SITE 48 48 Nucleophile. {ECO:0000250}.
METAL 32 32 Magnesium. {ECO:0000250}.
METAL 34 34 Magnesium. {ECO:0000250}.
METAL 92 92 Magnesium. {ECO:0000250}.
SITE 229 229 Important for catalytic activity.
{ECO:0000250}.
SITE 248 248 Important for catalytic activity.
{ECO:0000250}.
CARBOHYD 258 258 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 52 58 {ECO:0000250}.
DISULFID 54 197 {ECO:0000250}.
SEQUENCE 278 AA; 31713 MW; 8EDC1E71A0DF35B4 CRC64;
AXRPKPIWDV AHMVNDLELV DEYLGDGANG LELDVAFSDD GTAEKMYHGV PCDCFRSCKR
TETFTKYMDY IRELTTPGNS KFNNNLILLI MDLKLNGIEP NVAYAAGKSV AEKLLSSYWQ
NGESGARAYI VLSLETITRP EFINGFRDAI KASGHEELFE KIGWDFSGNE DLGDIRRVYQ
KYGIDEHIWQ GDGITNCLPR GDYRLTEAMK KKNDPDYKYT EKVYTWSIDK EASIRNALRL
GVDAVMTNYP ARVKSILNES EFSSTHRMAT YEDNPWQK


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