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Q8I914 (A311_LOXLA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phospholipase D LlSicTox-alphaIII1i

Short name=PLD
EC=3.1.4.4
Alternative name(s):
Dermonecrotic toxin
LlH17
Sphingomyelin phosphodiesterase D 1
Short name=SMD 1
Short name=SMase D 1
Short name=Sphingomyelinase D 1
Sphingomyelinase I
Short name=SMase I
OrganismLoxosceles laeta (South American recluse spider) (Scytodes laeta)
Taxonomic identifier58217 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaAraneaeAraneomorphaeHaplogynaeSicariidaeLoxosceles

Protein attributes

Sequence length311 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the hydrolysis of sphingomyelin. May also acts on other phosphatidyl esters. Induces complement-dependent hemolysis and dermonecrosis. Ref.1

Catalytic activity

A phosphatidylcholine + H2O = choline + a phosphatidate.

Cofactor

Binds 1 magnesium ion per subunit.

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Sequence similarities

Belongs to the SicTox family. Class I subfamily.

Contains 1 GDPD domain.

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.

Ontologies

Keywords
   Biological processCytolysis
Hemolysis
   Cellular componentSecreted
   DomainSignal
   LigandMagnesium
Metal-binding
   Molecular functionComplement system impairing toxin
Hydrolase
Toxin
   PTMDisulfide bond
Zymogen
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processhemolysis in other organism

Inferred from electronic annotation. Source: UniProtKB-KW

lipid metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionNAPE-specific phospholipase D activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phospholipase D activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Propeptide22 – 265
PRO_0000035583
Chain27 – 311285Phospholipase D LlSicTox-alphaIII1i
PRO_0000035584

Regions

Domain252 – 28231GDPD

Sites

Active site381 Ref.2 Ref.3
Active site731Nucleophile Ref.2 Ref.3
Metal binding581Magnesium
Metal binding601Magnesium
Metal binding1171Magnesium
Site2591Important for catalytic activity
Site2781Important for catalytic activity

Amino acid modifications

Disulfide bond77 ↔ 83 Ref.2 Ref.3

Secondary structure

.............................................. 311
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8I914 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 23024A2C4E7F4CC0

FASTA31134,874
        10         20         30         40         50         60 
MYAHLALILG CWTVVLQGAE TDVGERADNR RPIWNLAHMV NAVAQIPDFL DLGANALEAD 

        70         80         90        100        110        120 
VTFKGSVPTY TYHGTPCDFG RDCIRWEYFN VFLKTLREYT TPGNAKYRDG FILFVLDLKT 

       130        140        150        160        170        180 
GSLSNDQVRP AGENVAKELL QNYWNNGNNG GRAYVVLSLP DIGHYEFVRG FKEVLKKEGH 

       190        200        210        220        230        240 
EDLLEKVGYD FSGPYLPSLP TLDATHEAYK KAGVDGHIWL SDGLTNFSPL GDMARLKEAI 

       250        260        270        280        290        300 
KSRDSANGFI NKIYYWSVDK VSTTKAALDV GVDGIMTNYP NVLIGVLKES GYNDKYRLAT 

       310 
YDDNPWETFK N 

« Hide

References

[1]"Molecular cloning and expression of a functional dermonecrotic and haemolytic factor from Loxosceles laeta venom."
Fernandes-Pedrosa M.F., Junqueira de Azevedo I.L.M., Goncalves-de-Andrade R.M., van den Berg C.W., Ramos C.R.R., Ho P.L., Tambourgi D.V.
Biochem. Biophys. Res. Commun. 298:638-645(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
Tissue: Venom gland.
[2]"Structural basis for metal ion coordination and the catalytic mechanism of sphingomyelinases D."
Murakami M.T., Fernandes-Pedrosa M.F., Tambourgi D.V., Arni R.K.
J. Biol. Chem. 280:13658-13664(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 27-311, DISULFIDE BONDS, METAL-BINDING SITES, ACTIVE SITES.
[3]"Structural insights into the catalytic mechanism of sphingomyelinases D and evolutionary relationship to glycerophosphodiester phosphodiesterases."
Murakami M.T., Fernandes-Pedrosa M.F., de Andrade S.A., Gabdoulkhakov A., Betzel C., Tambourgi D.V., Arni R.K.
Biochem. Biophys. Res. Commun. 342:323-329(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 27-311, DISULFIDE BONDS, METAL-BINDING SITES, ACTIVE SITES, NOMENCLATURE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY093599 mRNA. Translation: AAM21154.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1XX1X-ray1.75A/B/C/D27-311[»]
2F9RX-ray1.85A/B/C/D27-311[»]
ProteinModelPortalQ8I914.
SMRQ8I914. Positions 27-311.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

ArachnoServerAS000132. Sphingomyelinase D (LlSicTox-alphaIII1i).

Enzyme and pathway databases

SABIO-RKQ8I914.

Family and domain databases

Gene3D3.20.20.190. 1 hit.
InterProIPR017946. PLC-like_Pdiesterase_TIM-brl.
[Graphical view]
SUPFAMSSF51695. SSF51695. 2 hits.
ProtoNetSearch...

Other

EvolutionaryTraceQ8I914.

Entry information

Entry nameA311_LOXLA
AccessionPrimary (citable) accession number: Q8I914
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: March 1, 2003
Last modified: February 19, 2014
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references