Q8I914 (A311_LOXLA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Sphingomyelin phosphodiesterase D LlSicTox-alphaIII1i Alternative name(s): LlH17 Sphingomyelin phosphodiesterase D 1 Short name=SMD 1 Short name=SMase D 1 Short name=Sphingomyelinase D 1 EC=3.1.4.41 Sphingomyelinase I Short name=SMase I
Organism	Loxosceles laeta (South American recluse spider) (Scytodes laeta)
Taxonomic identifier	58217 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Chelicerata › Arachnida › Araneae › Araneomorphae › Haplogynae › Sicariidae › Loxosceles

Protein attributes

Sequence length	311 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the hydrolysis of sphingomyelin. Induces complement-dependent hemolysis and dermonecrosis. Ref.1
Catalytic activity	Sphingomyelin + H2O = ceramide phosphate + choline.
Cofactor	Binds 1 magnesium ion per subunit.
Subcellular location	Secreted.
Tissue specificity	Expressed by the venom gland.
Sequence similarities	Belongs to the SicTox family. Alpha subfamily. Contains 1 GDPD domain.

Ontologies

Keywords
Biological process	Cytolysis Hemolysis
Cellular component	Secreted
Domain	Signal
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase Toxin
PTM	Disulfide bond Zymogen
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	cytolysis Inferred from electronic annotation. Source: UniProtKB-KW hemolysis in other organism Inferred from electronic annotation. Source: UniProtKB-KW lipid metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW sphingomyelin phosphodiesterase D activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Potential

Propeptide

22 – 26

5

By similarity

PRO_0000035583

Chain

27 – 311

285

Sphingomyelin phosphodiesterase D LlSicTox-alphaIII1i

PRO_0000035584

Regions

Domain

252 – 282

31

GDPD

Sites

Active site

38

1

Nucleophile Ref.2

Active site

73

1

Ref.2

Metal binding

58

1

Magnesium

Metal binding

60

1

Magnesium

Metal binding

117

1

Magnesium

Amino acid modifications

Disulfide bond

77 ↔ 83

Ref.2

Secondary structure

1

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311

Helix Strand Turn

Details...

Beta strand

30 – 38

9

Helix

45 – 52

8

Beta strand

55 – 64

10

Beta strand

67 – 72

6

Beta strand

86 – 88

3

Helix

89 – 99

11

Beta strand

113 – 118

6

Helix

125 – 127

3

Helix

128 – 142

15

Helix

145 – 147

3

Beta strand

154 – 160

7

Helix

162 – 164

3

Helix

165 – 177

13

Helix

181 – 186

6

Beta strand

187 – 191

5

Beta strand

196 – 198

3

Helix

202 – 212

11

Beta strand

218 – 222

5

Helix

229 – 243

15

Beta strand

252 – 256

5

Helix

261 – 270

10

Beta strand

273 – 278

6

Helix

280 – 288

9

Turn

290 – 295

6

Beta strand

296 – 298

3

Sequences

	Sequence		Length	Mass (Da)
	Q8I914 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 23024A2C4E7F4CC0	FASTA	311	34,874
	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

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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY093599 mRNA. Translation: AAM21154.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q8I914.

SMR

Q8I914. Positions 27-311.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Organism-specific databases

ArachnoServer

AS000132. Sphingomyelinase D (LlSicTox-alphaIII1i).

Family and domain databases

Gene3D

3.20.20.190. 1 hit.

InterPro

IPR017946. PLC-like_Pdiesterase_TIM-brl.
[Graphical view]

SUPFAM

SSF51695. PLC-like_Pdiesterase_TIM-brl. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q8I914.

Entry information

Entry name

A311_LOXLA

Accession

Primary (citable) accession number: Q8I914

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	March 1, 2003
Last modified:	April 3, 2013
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Animal Toxin Annotation Program