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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.
08-MAY-2019, entry version 38.
RecName: Full=Phospholipase D LiSicTox-alphaIA2bii;
Short=PLD;
EC=3.1.4.4;
AltName: Full=Dermonecrotic toxin;
AltName: Full=Loxtox i2;
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: Catalyzes the hydrolysis of sphingomyelin. May also act
on other phosphatidyl esters. Induces complement-dependent
hemolysis, dermonecrosis, blood vessel permeability and platelet
aggregation (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY:
Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-
diacyl-sn-glycero-3-phosphate + choline + H(+);
Xref=Rhea:RHEA:14445, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:57643, ChEBI:CHEBI:58608;
EC=3.1.4.4;
-!- 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:0000250}.
-!- 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; EF535251; ABU43330.1; -; mRNA.
SMR; B2KKV7; -.
ArachnoServer; AS000693; Sphingomyelinase D (LiSicTox-alphaIA2bii).
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; 1.
2: Evidence at transcript level;
Complement system impairing toxin; Cytolysis; Dermonecrotic toxin;
Disulfide bond; Glycoprotein; Hemolysis; Hydrolase; Magnesium;
Metal-binding; Secreted; Signal; Toxin; Zymogen.
SIGNAL <1 14 {ECO:0000255}.
PROPEP 15 22 {ECO:0000250}.
/FTId=PRO_0000380635.
CHAIN 23 302 Phospholipase D LiSicTox-alphaIA2bii.
/FTId=PRO_0000380636.
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}.
CARBOHYD 279 279 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 74 80 {ECO:0000250|UniProtKB:Q8I914}.
DISULFID 76 219 {ECO:0000250}.
NON_TER 1 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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WP1963: The effect of Glucocorticoids on target gene expression

Related Genes :
[] Phospholipase D LgSicTox-alphaI-Loxn-A (PLD) (EC 3.1.4.4) (Dermonecrotic toxin) (Loxnecrogin-A) (Sphingomyelin phosphodiesterase D) (SMD) (SMase D) (Sphingomyelinase D) (Fragments)
[plc cpa CPE0036] Phospholipase C (PLC) (EC 3.1.4.3) (Alpha-toxin) (Hemolysin) (Lecithinase) (Phosphatidylcholine cholinephosphohydrolase)
[Smpd3 Cca1] Sphingomyelin phosphodiesterase 3 (EC 3.1.4.12) (Confluent 3Y1 cell-associated protein 1) (Neutral sphingomyelinase 2) (nSMase-2) (nSMase2) (Neutral sphingomyelinase II)
[PLDALPHA1 PLD1 At3g15730 MSJ11.13] Phospholipase D alpha 1 (AtPLDalpha1) (PLD alpha 1) (EC 3.1.4.4) (Choline phosphatase 1) (PLDalpha) (Phosphatidylcholine-hydrolyzing phospholipase D 1)
[Pld2] Phospholipase D2 (PLD 2) (mPLD2) (EC 3.1.4.4) (Choline phosphatase 2) (PLD1C) (Phosphatidylcholine-hydrolyzing phospholipase D2)
[PLD2] Phospholipase D2 (PLD 2) (hPLD2) (EC 3.1.4.4) (Choline phosphatase 2) (PLD1C) (Phosphatidylcholine-hydrolyzing phospholipase D2)
[Pld2] Phospholipase D2 (PLD 2) (rPLD2) (EC 3.1.4.4) (Choline phosphatase 2) (PLD1C) (Phosphatidylcholine-hydrolyzing phospholipase D2)
[Pld1] Phospholipase D1 (PLD 1) (rPLD1) (EC 3.1.4.4) (Choline phosphatase 1) (Phosphatidylcholine-hydrolyzing phospholipase D1)
[botD] Botulinum neurotoxin type D (BoNT/D) (Bontoxilysin-D) [Cleaved into: Botulinum neurotoxin D light chain (LC) (EC 3.4.24.69); Botulinum neurotoxin D heavy chain (HC)]
[PLDGAMMA1 At4g11850 T26M18.60] Phospholipase D gamma 1 (AtPLDgamma1) (PLD gamma 1) (EC 3.1.4.4) (Choline phosphatase) (Lecithinase D) (Lipophosphodiesterase II)
[pld] Phospholipase D (PLD) (EC 3.1.4.4) [Cleaved into: Phospholipase D catalytic chain; Phospholipase D regulatory chain]
[PLDDELTA At4g35790 F4B14.60] Phospholipase D delta (AtPLDdelta) (PLD delta) (EC 3.1.4.4)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)] (Fragment)
[NAPEPLD C7orf18] N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D (N-acyl phosphatidylethanolamine phospholipase D) (NAPE-PLD) (NAPE-hydrolyzing phospholipase D) (EC 3.1.4.54)
[PLDBETA1 At2g42010 T6D20.10] Phospholipase D beta 1 (AtPLDbeta1) (PLD beta 1) (PLDbeta) (EC 3.1.4.4)
[Napepld Mbldc1] N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D (N-acyl phosphatidylethanolamine phospholipase D) (NAPE-PLD) (NAPE-hydrolyzing phospholipase D) (EC 3.1.4.54)
[Napepld] N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D (N-acyl phosphatidylethanolamine phospholipase D) (NAPE-PLD) (NAPE-hydrolyzing phospholipase D) (EC 3.1.4.54)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[Pld6] Mitochondrial cardiolipin hydrolase (EC 3.1.-.-) (Choline phosphatase 6) (Mitochondrial phospholipase) (MitoPLD) (Phosphatidylcholine-hydrolyzing phospholipase D6) (Phospholipase D6) (PLD 6) (Protein zucchini homolog) (mZuc)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[PLD6] Mitochondrial cardiolipin hydrolase (EC 3.1.-.-) (Choline phosphatase 6) (Mitochondrial phospholipase) (MitoPLD) (Phosphatidylcholine-hydrolyzing phospholipase D6) (Phospholipase D6) (PLD 6) (Protein zucchini homolog)
[POL RR33_52437gpPOL] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)] (Fragment)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)] (Fragment)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)] (Fragment)
[hchA A9819_11910 ACN81_03425 AML35_08765 AW059_23935 BANRA_00208 BANRA_00433 BANRA_02614 BHF46_18455 BMT91_24760 BvCmsC61A_00149 BvCmsH15A_00510 BvCmsKSNP120_04693 BvCmsKSP026_03873 BvCmsKSP076_04891 C4J69_22715 C7B08_25495 CR538_10415 D2F89_25795 D3Y67_22910 D9G42_11130 D9I97_22010 D9J11_25195 DP258_02540 E5M00_18610 EC3234A_36c00010 EC382_21100 ECTO6_01955 EFV06_13085 EPS71_23885 FORC82_1921 NCTC8500_02249 NCTC9037_02122 NCTC9117_02637 NCTC9969_02156 SAMEA3472108_01151 SAMEA3484427_04795 SAMEA3484429_02051 SAMEA3752557_05476 SAMEA3752559_04333] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[PLDZETA1 PLDP1 At3g16785 K20I9.1 MGL6.26] Phospholipase D zeta 1 (PLDzeta1) (EC 3.1.4.4) (Phospholipase D p1) (AtPLDp1) (Phospholipase D1 PHOX and PX-containing domain protein)
[PLPZETA2 PLDP2 At3g05630 F18C1.10] Phospholipase D zeta 2 (PLDzeta2) (EC 3.1.4.4) (Phospholipase D p2) (AtPLDp2) (Phospholipase D2 PHOX and PX-containing domain protein)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)] (Fragment)

Bibliography :
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