Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8I914

- A311_LOXLA

UniProt

Q8I914 - A311_LOXLA

(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)

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

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

Mg2+Note: Binds 1 Mg(2+) 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
Complete GO annotation...

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-KW
Complete GO annotation...

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 – 389Combined sources
Helixi45 – 528Combined sources
Beta strandi55 – 6410Combined sources
Beta strandi67 – 726Combined sources
Beta strandi86 – 883Combined sources
Helixi89 – 9911Combined sources
Beta strandi113 – 1186Combined sources
Helixi125 – 1273Combined sources
Helixi128 – 14215Combined sources
Helixi145 – 1473Combined sources
Beta strandi154 – 1607Combined sources
Helixi162 – 1643Combined sources
Helixi165 – 17713Combined sources
Helixi181 – 1866Combined sources
Beta strandi187 – 1915Combined sources
Beta strandi196 – 1983Combined sources
Helixi202 – 21211Combined sources
Beta strandi218 – 2225Combined sources
Helixi229 – 24315Combined sources
Beta strandi252 – 2565Combined sources
Helixi261 – 27010Combined sources
Beta strandi273 – 2786Combined sources
Helixi280 – 2889Combined sources
Turni290 – 2956Combined sources
Beta strandi296 – 2983Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MYAHLALILG CWTVVLQGAE TDVGERADNR RPIWNLAHMV NAVAQIPDFL
60 70 80 90 100
DLGANALEAD VTFKGSVPTY TYHGTPCDFG RDCIRWEYFN VFLKTLREYT
110 120 130 140 150
TPGNAKYRDG FILFVLDLKT GSLSNDQVRP AGENVAKELL QNYWNNGNNG
160 170 180 190 200
GRAYVVLSLP DIGHYEFVRG FKEVLKKEGH EDLLEKVGYD FSGPYLPSLP
210 220 230 240 250
TLDATHEAYK KAGVDGHIWL SDGLTNFSPL GDMARLKEAI KSRDSANGFI
260 270 280 290 300
NKIYYWSVDK VSTTKAALDV GVDGIMTNYP NVLIGVLKES GYNDKYRLAT
310
YDDNPWETFK N
Length:311
Mass (Da):34,874
Last modified:March 1, 2003 - v1
Checksum:i23024A2C4E7F4CC0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY093599 mRNA. Translation: AAM21154.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY093599 mRNA. Translation: AAM21154.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 64 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