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Phospholipase D LiSicTox-alphaIA1bii (PLD) (EC 3.1.4.4) (Dermonecrotic toxin) (Loxtox i4) (Sphingomyelin phosphodiesterase D 1) (SMD 1) (SMase D 1) (Sphingomyelinase D 1) (Fragment)

 A1HB2_LOXIN             Reviewed;         302 AA.
P0CE82; B2KKV9; P83045; Q3HL91; Q6W8Q5; Q7YW73;
23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
23-MAR-2010, sequence version 1.
22-NOV-2017, entry version 27.
RecName: Full=Phospholipase D LiSicTox-alphaIA1bii;
Short=PLD;
EC=3.1.4.4;
AltName: Full=Dermonecrotic toxin;
AltName: Full=Loxtox i4;
AltName: Full=Sphingomyelin phosphodiesterase D 1;
Short=SMD 1;
Short=SMase D 1;
Short=Sphingomyelinase D 1;
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).
[2]
PROTEIN SEQUENCE OF 23-60, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Venom;
PubMed=9790962; DOI=10.1006/bbrc.1998.9474;
Tambourgi D.V., Magnoli F.C., van den Berg C.W., Morgan B.P.,
de Araujo P.S., Alves E.W., Da Silva W.D.;
"Sphingomyelinases in the venom of the spider Loxosceles intermedia
are responsible for both dermonecrosis and complement-dependent
hemolysis.";
Biochem. Biophys. Res. Commun. 251:366-373(1998).
-!- FUNCTION: Catalyzes the hydrolysis of sphingomyelin. May also act
on other phosphatidyl esters. Induces complement-dependent
hemolysis, dermonecrosis, blood vessel permeability and platelet
aggregation. {ECO:0000269|PubMed:9790962}.
-!- CATALYTIC ACTIVITY: A phosphatidylcholine + H(2)O = choline + a
phosphatidate. {ECO:0000269|PubMed:9790962}.
-!- 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:0000269|PubMed:9790962}.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
{ECO:0000269|PubMed:9790962}.
-!- 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; EF535253; ABU43332.1; -; mRNA.
PDB; 4RW3; X-ray; 1.72 A; A=24-302.
PDB; 4RW5; X-ray; 1.64 A; A=24-302.
PDBsum; 4RW3; -.
PDBsum; 4RW5; -.
ProteinModelPortal; P0CE82; -.
SMR; P0CE82; -.
PRIDE; P0CE82; -.
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:0090729; F:toxin activity; IEA:UniProtKB-KW.
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;
3D-structure; Complement system impairing toxin; Cytolysis;
Dermonecrotic toxin; Direct protein sequencing; Disulfide bond;
Hemolysis; Hydrolase; Magnesium; Metal-binding; Secreted; Signal;
Toxin; Zymogen.
SIGNAL <1 14 {ECO:0000255}.
PROPEP 15 22 {ECO:0000250}.
/FTId=PRO_0000392741.
CHAIN 23 302 Phospholipase D LiSicTox-alphaIA1bii.
/FTId=PRO_0000392742.
DOMAIN 243 273 GDPD.
ACT_SITE 34 34 {ECO:0000250|UniProtKB:Q8I914}.
ACT_SITE 70 70 Nucleophile.
{ECO:0000250|UniProtKB:Q8I914}.
METAL 54 54 Magnesium.
{ECO:0000250|UniProtKB:Q8I914}.
METAL 56 56 Magnesium.
{ECO:0000250|UniProtKB:Q8I914}.
METAL 114 114 Magnesium.
{ECO:0000250|UniProtKB:Q8I914}.
SITE 250 250 Important for catalytic activity.
{ECO:0000250|UniProtKB:Q8I914}.
SITE 269 269 Important for catalytic activity.
{ECO:0000250|UniProtKB:Q8I914}.
DISULFID 74 80 {ECO:0000250|UniProtKB:Q8I914}.
DISULFID 76 219 {ECO:0000250}.
CONFLICT 54 54 E -> EI (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 58 58 S -> F (in Ref. 2; AA sequence).
{ECO:0000305}.
NON_TER 1 1
STRAND 27 34 {ECO:0000244|PDB:4RW5}.
HELIX 39 47 {ECO:0000244|PDB:4RW5}.
STRAND 51 59 {ECO:0000244|PDB:4RW5}.
STRAND 65 68 {ECO:0000244|PDB:4RW5}.
HELIX 86 96 {ECO:0000244|PDB:4RW5}.
STRAND 110 115 {ECO:0000244|PDB:4RW5}.
HELIX 117 119 {ECO:0000244|PDB:4RW5}.
HELIX 122 124 {ECO:0000244|PDB:4RW5}.
HELIX 125 139 {ECO:0000244|PDB:4RW5}.
HELIX 142 144 {ECO:0000244|PDB:4RW5}.
STRAND 151 157 {ECO:0000244|PDB:4RW5}.
HELIX 159 162 {ECO:0000244|PDB:4RW5}.
HELIX 163 174 {ECO:0000244|PDB:4RW5}.
HELIX 178 183 {ECO:0000244|PDB:4RW5}.
STRAND 184 188 {ECO:0000244|PDB:4RW5}.
HELIX 194 204 {ECO:0000244|PDB:4RW5}.
STRAND 208 215 {ECO:0000244|PDB:4RW5}.
HELIX 225 234 {ECO:0000244|PDB:4RW5}.
STRAND 243 247 {ECO:0000244|PDB:4RW5}.
HELIX 252 260 {ECO:0000244|PDB:4RW5}.
STRAND 264 269 {ECO:0000244|PDB:4RW5}.
HELIX 271 278 {ECO:0000244|PDB:4RW5}.
HELIX 281 284 {ECO:0000244|PDB:4RW5}.
STRAND 287 289 {ECO:0000244|PDB:4RW5}.
SEQUENCE 302 AA; 33641 MW; 0E97975AA4424F72 CRC64;
ARVVLGCWSV LSQAAQTDDE ERAGNRRPIW IMGHMVNAIG QIDEFVNLGA NSIETDVSFD
DNANPEYTYH GIPCDCGRNC KKYENFNDFL KGLRSATTPG NSKYQEKLVL VVFDLKTGSL
YDNQANDAGK KLAKNLLQHY WNNGNNGGRA YIVLSIPDLN HYPLIKGFKD QLTKDGHPEL
MDKVGHDFSG NDDIGDVGKA YKKAGITGHI WQSDGITNCL PRGLSRVNAA VANRDSANGF
INKVYYWTVD KRSTTRDALD AGVDGIMTNY PDVITDVLNE AAYKKKFRVA TYDDNPWVTF
KK


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