Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q8I914

- A311_LOXLA

UniProt

Q8I914 - A311_LOXLA

Protein

Phospholipase D LlSicTox-alphaIII1i

Gene
N/A
Organism
Loxosceles laeta (South American recluse spider) (Scytodes laeta)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 62 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

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

    Catalytic activityi

    A phosphatidylcholine + H2O = choline + a phosphatidate.

    Cofactori

    Binds 1 magnesium ion per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei38 – 381
    Metal bindingi58 – 581Magnesium
    Metal bindingi60 – 601Magnesium
    Active sitei73 – 731Nucleophile
    Metal bindingi117 – 1171Magnesium
    Sitei259 – 2591Important for catalytic activity
    Sitei278 – 2781Important for catalytic activity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. N-acylphosphatidylethanolamine-specific phospholipase D activity Source: UniProtKB-EC
    3. phospholipase D activity Source: UniProtKB-EC

    GO - Biological processi

    1. hemolysis in other organism Source: UniProtKB-KW
    2. lipid metabolic process Source: InterPro

    Keywords - Molecular functioni

    Complement system impairing toxin, Hydrolase, Toxin

    Keywords - Biological processi

    Cytolysis, Hemolysis

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    SABIO-RKQ8I914.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phospholipase D LlSicTox-alphaIII1i (EC:3.1.4.4)
    Short name:
    PLD
    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
    OrganismiLoxosceles laeta (South American recluse spider) (Scytodes laeta)
    Taxonomic identifieri58217 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaAraneaeAraneomorphaeHaplogynaeSicariidaeLoxosceles

    Organism-specific databases

    ArachnoServeriAS000132. Sphingomyelinase D (LlSicTox-alphaIII1i).

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Propeptidei22 – 265PRO_0000035583
    Chaini27 – 311285Phospholipase D LlSicTox-alphaIII1iPRO_0000035584Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi77 ↔ 832 Publications

    Keywords - PTMi

    Disulfide bond, Zymogen

    Expressioni

    Tissue specificityi

    Expressed by the venom gland.

    Structurei

    Secondary structure

    1
    311
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi30 – 389
    Helixi45 – 528
    Beta strandi55 – 6410
    Beta strandi67 – 726
    Beta strandi86 – 883
    Helixi89 – 9911
    Beta strandi113 – 1186
    Helixi125 – 1273
    Helixi128 – 14215
    Helixi145 – 1473
    Beta strandi154 – 1607
    Helixi162 – 1643
    Helixi165 – 17713
    Helixi181 – 1866
    Beta strandi187 – 1915
    Beta strandi196 – 1983
    Helixi202 – 21211
    Beta strandi218 – 2225
    Helixi229 – 24315
    Beta strandi252 – 2565
    Helixi261 – 27010
    Beta strandi273 – 2786
    Helixi280 – 2889
    Turni290 – 2956
    Beta strandi296 – 2983

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1XX1X-ray1.75A/B/C/D27-311[»]
    2F9RX-ray1.85A/B/C/D27-311[»]
    ProteinModelPortaliQ8I914.
    SMRiQ8I914. Positions 27-311.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8I914.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini252 – 28231GDPDAdd
    BLAST

    Sequence similaritiesi

    Contains 1 GDPD domain.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.20.20.190. 1 hit.
    InterProiIPR017946. PLC-like_Pdiesterase_TIM-brl.
    [Graphical view]
    SUPFAMiSSF51695. SSF51695. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q8I914-1 [UniParc]FASTAAdd to Basket

    « Hide

    MYAHLALILG CWTVVLQGAE TDVGERADNR RPIWNLAHMV NAVAQIPDFL    50
    DLGANALEAD VTFKGSVPTY TYHGTPCDFG RDCIRWEYFN VFLKTLREYT 100
    TPGNAKYRDG FILFVLDLKT GSLSNDQVRP AGENVAKELL QNYWNNGNNG 150
    GRAYVVLSLP DIGHYEFVRG FKEVLKKEGH EDLLEKVGYD FSGPYLPSLP 200
    TLDATHEAYK KAGVDGHIWL SDGLTNFSPL GDMARLKEAI KSRDSANGFI 250
    NKIYYWSVDK VSTTKAALDV GVDGIMTNYP NVLIGVLKES GYNDKYRLAT 300
    YDDNPWETFK N 311
    Length:311
    Mass (Da):34,874
    Last modified:March 1, 2003 - v1
    Checksum:i23024A2C4E7F4CC0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY093599 mRNA. Translation: AAM21154.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY093599 mRNA. Translation: AAM21154.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1XX1 X-ray 1.75 A/B/C/D 27-311 [» ]
    2F9R X-ray 1.85 A/B/C/D 27-311 [» ]
    ProteinModelPortali Q8I914.
    SMRi Q8I914. Positions 27-311.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    ArachnoServeri AS000132. Sphingomyelinase D (LlSicTox-alphaIII1i).

    Enzyme and pathway databases

    SABIO-RK Q8I914.

    Miscellaneous databases

    EvolutionaryTracei Q8I914.

    Family and domain databases

    Gene3Di 3.20.20.190. 1 hit.
    InterProi IPR017946. PLC-like_Pdiesterase_TIM-brl.
    [Graphical view ]
    SUPFAMi SSF51695. SSF51695. 2 hits.
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiA311_LOXLA
    AccessioniPrimary (citable) accession number: Q8I914
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 16, 2004
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 62 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programAnimal Toxin Annotation Program

    Miscellaneousi

    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.Curated

    Keywords - Technical termi

    3D-structure

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3