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Protein

Phospholipase D LlSicTox-alphaIII1i

Gene
N/A
Organism
Loxosceles laeta (South American recluse spider) (Scytodes laeta)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

A phosphatidylcholine + H2O = choline + a phosphatidate.

Cofactori

Mg2+2 PublicationsNote: Binds 1 Mg2+ ion per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei381 Publication1
Metal bindingi58Magnesium2 Publications1
Metal bindingi60Magnesium2 Publications1
Active sitei73Nucleophile1 Publication1
Metal bindingi117Magnesium2 Publications1
Sitei259Important for catalytic activity1
Sitei278Important for catalytic activity1

GO - Molecular functioni

GO - Biological processi

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

BRENDAi3.1.4.41. 6922.
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

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
PropeptideiPRO_000003558322 – 265
ChainiPRO_000003558427 – 311Phospholipase D LlSicTox-alphaIII1iAdd BLAST285

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi77 ↔ 832 Publications

Keywords - PTMi

Disulfide bond, Zymogen

Expressioni

Tissue specificityi

Expressed by the venom gland.

Structurei

Secondary structure

1311
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi30 – 38Combined sources9
Helixi45 – 52Combined sources8
Beta strandi55 – 64Combined sources10
Beta strandi67 – 72Combined sources6
Beta strandi86 – 88Combined sources3
Helixi89 – 99Combined sources11
Beta strandi113 – 118Combined sources6
Helixi125 – 127Combined sources3
Helixi128 – 142Combined sources15
Helixi145 – 147Combined sources3
Beta strandi154 – 160Combined sources7
Helixi162 – 164Combined sources3
Helixi165 – 177Combined sources13
Helixi181 – 186Combined sources6
Beta strandi187 – 191Combined sources5
Beta strandi196 – 198Combined sources3
Helixi202 – 212Combined sources11
Beta strandi218 – 222Combined sources5
Helixi229 – 243Combined sources15
Beta strandi252 – 256Combined sources5
Helixi261 – 270Combined sources10
Beta strandi273 – 278Combined sources6
Helixi280 – 288Combined sources9
Turni290 – 295Combined sources6
Beta strandi296 – 298Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XX1X-ray1.75A/B/C/D27-311[»]
2F9RX-ray1.85A/B/C/D27-311[»]
ProteinModelPortaliQ8I914.
SMRiQ8I914.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8I914.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini252 – 282GDPDAdd BLAST31

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XX1X-ray1.75A/B/C/D27-311[»]
2F9RX-ray1.85A/B/C/D27-311[»]
ProteinModelPortaliQ8I914.
SMRiQ8I914.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

ArachnoServeriAS000132. Sphingomyelinase D (LlSicTox-alphaIII1i).

Enzyme and pathway databases

BRENDAi3.1.4.41. 6922.
SABIO-RKQ8I914.

Miscellaneous databases

EvolutionaryTraceiQ8I914.

Family and domain databases

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

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 2, 2016
This is version 72 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.