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Phospholipase D LiSicTox-alphaIA2bii (PLD) (EC 3.1.4.4) (Dermonecrotic toxin) (Loxtox i2) (Sphingomyelin phosphodiesterase D) (SMD) (SMase D) (Sphingomyelinase D) (Fragment)

 A1IB2_LOXIN             Reviewed;         302 AA.
B2KKV7;
28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 1.
11-DEC-2019, entry version 41.
RecName: Full=Dermonecrotic toxin LiSicTox-alphaIA2bii;
EC=4.6.1.- {ECO:0000250|UniProtKB:Q4ZFU2};
AltName: Full=Loxtox i2;
AltName: Full=Phospholipase D;
Short=PLD;
AltName: Full=Sphingomyelin phosphodiesterase D;
Short=SMD;
Short=SMase D;
Short=Sphingomyelinase D;
Flags: Precursor; Fragment;
Loxosceles intermedia (Brown spider).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
Araneomorphae; Haplogynae; Sicariidae; Loxosceles.
NCBI_TaxID=58218;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Venom gland;
PubMed=17825864; DOI=10.1016/j.toxicon.2007.07.001;
Kalapothakis E., Chatzaki M., Goncalves-Dornelas H., de Castro C.S.,
Silvestre F.G., Laborne F.V., de Moura J.F., Veiga S.S.,
Chavez-Olortegui C., Granier C., Barbaro K.C.;
"The Loxtox protein family in Loxosceles intermedia (Mello-Leitao) venom.";
Toxicon 50:938-946(2007).
-!- FUNCTION: Dermonecrotic toxins cleave the phosphodiester linkage
between the phosphate and headgroup of certain phospholipids
(sphingolipid and lysolipid substrates), forming an alcohol (often
choline) and a cyclic phosphate (By similarity). This toxin acts on
sphingomyelin (SM) (By similarity). It may also act on ceramide
phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and
lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine
(LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by
transphosphatidylation, releasing exclusively cyclic phosphate products
as second products (By similarity). Induces dermonecrosis, hemolysis,
increased vascular permeability, edema, inflammatory response, and
platelet aggregation (By similarity).
{ECO:0000250|UniProtKB:A0A0D4WTV1, ECO:0000250|UniProtKB:P0CE80}.
-!- CATALYTIC ACTIVITY:
Reaction=an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-
1,3-cyclic phosphate + choline; Xref=Rhea:RHEA:60652,
ChEBI:CHEBI:15354, ChEBI:CHEBI:64583, ChEBI:CHEBI:143892;
Evidence={ECO:0000250|UniProtKB:A0A0D4WTV1};
-!- CATALYTIC ACTIVITY:
Reaction=an N-(acyl)-sphingosylphosphoethanolamine = an N-(acyl)-
sphingosyl-1,3-cyclic phosphate + ethanolamine; Xref=Rhea:RHEA:60648,
ChEBI:CHEBI:57603, ChEBI:CHEBI:143891, ChEBI:CHEBI:143892;
Evidence={ECO:0000250|UniProtKB:A0A0D4WTV1};
-!- CATALYTIC ACTIVITY:
Reaction=a 1-acyl-sn-glycero-3-phosphocholine = a 1-acyl-sn-glycero-
2,3-cyclic phosphate + choline; Xref=Rhea:RHEA:60700,
ChEBI:CHEBI:15354, ChEBI:CHEBI:58168, ChEBI:CHEBI:143947;
Evidence={ECO:0000250|UniProtKB:A0A0D4WTV1};
-!- CATALYTIC ACTIVITY:
Reaction=a 1-acyl-sn-glycero-3-phosphoethanolamine = a 1-acyl-sn-
glycero-2,3-cyclic phosphate + ethanolamine; Xref=Rhea:RHEA:60704,
ChEBI:CHEBI:57603, ChEBI:CHEBI:64381, ChEBI:CHEBI:143947;
Evidence={ECO:0000250|UniProtKB:A0A0D4WTV1};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:Q8I914};
Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8I914};
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:17825864}.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
{ECO:0000305|PubMed:17825864}.
-!- SIMILARITY: Belongs to the arthropod phospholipase D family. Class II
subfamily. {ECO:0000305}.
-!- CAUTION: The most common activity assay for dermonecrotic toxins
detects enzymatic activity by monitoring choline release from
substrate. Liberation of choline from sphingomyelin (SM) or
lysophosphatidylcholine (LPC) is commonly assumed to result from
substrate hydrolysis, giving either ceramide-1-phosphate (C1P) or
lysophosphatidic acid (LPA), respectively, as a second product.
However, two studies from Lajoie and colleagues (2013 and 2015) report
the observation of exclusive formation of cyclic phosphate products as
second products, resulting from intramolecular transphosphatidylation.
Cyclic phosphates have vastly different biological properties from
their monoester counterparts, and they may be relevant to the pathology
of brown spider envenomation. {ECO:0000250|UniProtKB:A0A0D4WTV1,
ECO:0000250|UniProtKB:A0A0D4WV12, ECO:0000250|UniProtKB:Q4ZFU2}.
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EMBL; EF535251; ABU43330.1; -; mRNA.
SMR; B2KKV7; -.
ArachnoServer; AS000693; Sphingomyelinase D (LiSicTox-alphaIA2bii).
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0044179; P:hemolysis in other organism; IEA:UniProtKB-KW.
GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
GO; GO:0009405; P:pathogenesis; IEA:GOC.
Gene3D; 3.20.20.190; -; 1.
InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
SUPFAM; SSF51695; SSF51695; 1.
2: Evidence at transcript level;
Cytolysis; Dermonecrotic toxin; Disulfide bond; Glycoprotein; Hemolysis;
Lipid degradation; Lipid metabolism; Lyase; Magnesium; Metal-binding;
Secreted; Signal; Toxin; Zymogen.
SIGNAL <1..14
/evidence="ECO:0000255"
PROPEP 15..22
/evidence="ECO:0000250"
/id="PRO_0000380635"
CHAIN 23..302
/note="Dermonecrotic toxin LiSicTox-alphaIA2bii"
/id="PRO_0000380636"
ACT_SITE 34
/evidence="ECO:0000250|UniProtKB:Q8I914"
ACT_SITE 70
/note="Nucleophile"
/evidence="ECO:0000250|UniProtKB:Q8I914"
METAL 54
/note="Magnesium"
/evidence="ECO:0000250|UniProtKB:Q8I914"
METAL 56
/note="Magnesium"
/evidence="ECO:0000250|UniProtKB:Q8I914"
METAL 114
/note="Magnesium"
/evidence="ECO:0000250|UniProtKB:Q8I914"
CARBOHYD 279
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 74..80
/evidence="ECO:0000250|UniProtKB:P0CE80"
DISULFID 76..219
/evidence="ECO:0000250|UniProtKB:P0CE80"
NON_TER 1
SEQUENCE 302 AA; 33627 MW; 871758A6434036F4 CRC64;
IALILVCWSV LSQAAQTDVE GRADKRRPIW IMGHMVNAIA QIDEFVNLGA NSIETDVSFD
DNANPEYTYH GVPCDCGRSC LKWENFNDFL KGLRSATTPG NAKYQAKLIL VVFDLKTGSL
YDNQANEAGK KLAKNLLKHY WNNGNNGGRA YIVLSIPDLN HYPLIKGFKD QLTHDGHPEL
MDKVGHDFSG NDAIGDVGNA YKKAGISGHV WQSDGITNCL LRGLDRVKQA IANRDSGNGF
INKVYYWTVD KRATTRDALD AGVDGVMTNY PDVITDVLNE SAYKNKFRVA SYEDNPWETF
KK


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Related Genes :
[] Dermonecrotic toxin LiSicTox-alphaIA2bii (EC 4.6.1.-) (Loxtox i2) (Phospholipase D) (PLD) (Sphingomyelin phosphodiesterase D) (SMD) (SMase D) (Sphingomyelinase D) (Fragment)
[] Dermonecrotic toxin LiSicTox-alphaIA1bii (EC 4.6.1.-) (LiRecDT1) (Loxtox i4) (Phospholipase D) (PLD) (Sphingomyelin phosphodiesterase D 1) (SMD 1) (SMase D 1) (Sphingomyelinase D 1) (Fragment)
[] Dermonecrotic toxin LiSicTox-betaIA1i (EC 4.6.1.-) (Dermonecrotic toxin 3) (DT3) (Dermonecrotic toxin-like I) (LiRecDT3) (Loxtox i6) (P3) (Phospholipase D) (PLD) (Sphingomyelin phosphodiesterase D 3) (SMD 3) (Smase D 3) (Sphingomyelinase D 3)
[] Dermonecrotic toxin LiSicTox-alphaIA1a (EC 4.6.1.-) (Dermonecrotic toxin 1) (DT1) (LiRecDT1) (P1) (Phospholipase D) (PLD) (Sphingomyelin phosphodiesterase D 1) (SMD 1) (SMase D 1) (Sphingomyelinase D 1)
[] Dermonecrotic toxin LiSicTox-betaID1 (EC 4.6.1.-) (Dermonecrotic toxin 5) (DT5) (LiRecDT5) (Phospholipase D) (PLD) (Sphingomyelin phosphodiesterase D 5) (SMD 5) (SMase D 5) (Sphingomyelinase D 5)
[] Dermonecrotic toxin LiSicTox-alphaII1 (EC 4.6.1.-) (Dermonecrotic toxin 4) (DT4) (LiRecDT4) (Phospholipase D) (Sphingomyelin phosphodiesterase D 4) (SMD 4) (SMase D 4) (Sphingomyelinase D 4)
[] Dermonecrotic toxin LiSicTox-betaIA1ii (EC 4.6.1.-) (Dermonecrotic toxin-like II) (Loxtox i7) (Phospholipase D) (PLD) (Sphingomyelin phosphodiesterase D 7) (SMD 7) (Smase D 7) (Sphingomyelinase D 7)
[] Dermonecrotic toxin LarSicTox-alphaIB2bi (EC 4.6.1.-) (Laz-SMase D) (Phospholipase D) (PLD) (Sphingomyelin phosphodiesterase D 2) (SMD 2) (SMase D 2) (Sphingomyelinase D 2) (Fragment)
[] Dermonecrotic toxin LlSicTox-alphaIII1i (EC 4.6.1.-) (LlH17) (Phospholipase D) (PLD) (Sphingomyelin phosphodiesterase D 1) (Lox-SMaseD) (SMD 1) (SMase D 1) (Sphingomyelinase D 1) (Sphingomyelinase I) (SMase I)
[] Dermonecrotic toxin LiSicTox-alphaIA2ai (EC 4.6.1.-) (LiP2) (P2) (Phospholipase D) (PLD) (Sphingomyelin phosphodiesterase D 2) (SMD 2) (SMase D 2) (Sphingomyelinase D 2)
[] Dermonecrotic toxin LiSicTox-alphaIA1bi (EC 4.6.1.-) (LiD1) (LiP1) (P1) (Phospholipase D) (PLD) (Sphingomyelin phosphodiesterase D 1) (SMD 1) (SMase D 1) (Sphingomyelinase D 1) (recLiD1)
[] Dermonecrotic toxin LiSicTox-alphaIA2aiii (EC 4.6.1.-) (Loxtox i3) (Phospholipase D) (PLD) (Sphingomyelin phosphodiesterase D) (SMD) (SMase D) (Sphingomyelinase D) (Fragment)
[] Dermonecrotic toxin (EC 4.6.1.-) (Phospholipase D isoform 1) (LlPLD1) (PLD1) (Sphingomyelin phosphodiesterase D) (SMD) (SMase D) (Sphingomyelinase D)
[] Dermonecrotic toxin LiSicTox-alphaIA2bi (EC 4.6.1.-) (Loxtox i1) (Phospholipase D) (PLD) (Sphingomyelin phosphodiesterase D) (SMD) (SMase D) (Sphingomyelinase D)
[] Dermonecrotic toxin LrSicTox-alphaIA1ii (EC 4.6.1.-) (Dermonecrotic toxin) (Phospholipase D) (PLD) (SMaseD/LysoPLD) (Sphingomyelin phosphodiesterase D) (SMD) (SMase D) (Sphingomyelinase D)
[] Dermonecrotic toxin LiSicTox-alphaII2 (EC 4.6.1.-) (Loxtox i5) (Phospholipase D) (PLD) (Sphingomyelin phosphodiesterase D) (SMD) (SMase D) (Sphingomyelinase D)
[] Dermonecrotic toxin LiSicTox-alphaV1 (EC 4.6.1.-) (Dermonecrotic toxin 6) (DT6) (LiRecDT6) (Phospholipase D) (PLD) (Sphingomyelin phosphodiesterase D 6) (SMD 6) (SMase D 6) (Sphingomyelinase D 6)
[] Dermonecrotic toxin LgSicTox-alphaIC1 (EC 4.6.1.-) (Phospholipase D) (PLD) (Phospholipase D LgRec1) (Sphingomyelin phosphodiesterase D) (SMD) (SMase D) (Sphingomyelinase D) [Cleaved into: U1-sicaritoxin-Lg1a (U1-SCRTX-Lg1a) (Anionic antimicrobial peptide) (AAMP) (Lg-AMP1)]
[] Dermonecrotic toxin StSicTox-betaIB1i (EC 4.6.1.-) (Phospholipase D) (PLD) (Sphingomyelin phosphodiesterase D) (SMD) (SMase D) (Sphingomyelinase D)
[] Dermonecrotic toxin LiSicTox-alphaIA2aii (EC 4.6.1.-) (Dermonecrotic toxin 2) (DT2) (LiRecDT2) (LiP2) (P2) (Phospholipase D) (PLD) (Sphingomyelin phosphodiesterase D 2) (SMD 2) (SMase D 2) (Sphingomyelinase D 2) (Fragment)
[] Dermonecrotic toxin LarSicTox-betaID1 (EC 4.6.1.-) (Phospholipase D) (PLD) (Sphingomyelin phosphodiesterase D) (SMD) (SMase D) (Sphingomyelinase D) (Fragment)
[] Dermonecrotic toxin LiSicTox-alphaIVA1 (EC 4.6.1.-) (Dermonecrotic toxin 7) (DT7) (LiRecDT7) (Phospholipase D) (PLD) (Sphingomyelin phosphodiesterase D 7) (SMD 7) (SMase D 7) (Sphingomyelinase D 7)
[] Dermonecrotic toxin LgSicTox-alphaI-Loxn-A (EC 4.6.1.-) (Loxnecrogin-A) (Phospholipase D) (PLD) (Sphingomyelin phosphodiesterase D) (SMD) (SMase D) (Sphingomyelinase D) (Fragments)
[] Dermonecrotic toxin LlSicTox-betaIA1 (EC 4.6.1.-) (LlH10) (H10) (Phospholipase D) (PLD) (SMase II) (Sphingomyelin phosphodiesterase D) (SMD) (SMase D) (Sphingomyelinase D)
[] Dermonecrotic toxin LbSicTox-alphaIB1a (EC 4.6.1.-) (Lb1) (Phospholipase D) (PLD) (Sphingomyelin phosphodiesterase D 1) (SMD 1) (SMase D 1) (Sphingomyelinase D 1)
[] Dermonecrotic toxin LrSicTox-alphaIB1 (EC 4.6.1.-) (Lr1) (Phospholipase D) (PLD) (Sphingomyelin phosphodiesterase D 1) (SMD 1) (SMase D 1) (Sphingomyelinase D 1)
[] Dermonecrotic toxin LhSicTox-alphaIA2bii (EC 4.6.1.-) (Phospholipase D) (PLD) (Sphingomyelin phosphodiesterase D) (SMD) (SMase D) (Sphingomyelinase D) (Fragment)
[] Dermonecrotic toxin LiSicTox-alphaI-1 (EC 4.6.1.-) (Phospholipase D) (PLD) (Sphingomyelin phosphodiesterase D) (SMD) (SMase D) (Sphingomyelinase D) (Fragment)
[] Dermonecrotic toxin Hl-PLD1 (EC 4.6.1.-) (Phospholipase D) (PLD) (Sphingomyelin phosphodiesterase D) (SMD) (SMase D) (Sphingomyelinase D)
[] Dermonecrotic toxin LlSicTox-alphaIII1ii (EC 4.6.1.-) (Ll1) (Phospholipase D) (PLD) (Sphingomyelin phosphodiesterase D 1) (SMD 1) (SMase D 1) (Sphingomyelinase D 1)

Bibliography :