O70572 (NSMA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sphingomyelin phosphodiesterase 2
EC=3.1.4.12

Alternative name(s):
Lyso-platelet-activating factor-phospholipase C
Short name=Lyso-PAF-PLC
Neutral sphingomyelinase
Short name=N-SMase
Short name=nSMase

Gene names

Name:

Smpd2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	419 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Converts sphingomyelin to ceramide. Hydrolyze 1-acyl-2-lyso-sn-glycero-3-phosphocholine (lyso-PC) and 1-O-alkyl-2-lyso-sn-glycero-3-phosphocholine (lyso-platelet-activating factor). The physiological substrate seems to be Lyso-PAF By similarity.
Catalytic activity	Sphingomyelin + H2O = N-acylsphingosine + choline phosphate.
Cofactor	Magnesium.
Subcellular location	Membrane; Multi-pass membrane protein.
Tissue specificity	Although widely expressed in all tissues examined, except the spleen, high enzymatic activity occurs only in the brain. Ref.1
Disruption phenotype	Mice lacking Smpd2 and Smpd3 are completely devoid of neutral SMase activity but do not developed sphingomyelin storage abnormalities. Ref.3
Sequence similarities	Belongs to the neutral sphingomyelinase family.
Biophysicochemical properties	pH dependence: Optimum pH is 6.5-7.5.

Ontologies

Keywords
Cellular component	Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW sphingomyelin phosphodiesterase activity Inferred from mutant phenotype Ref.3. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 419	419	Sphingomyelin phosphodiesterase 2		PRO_0000075687
Regions
	Transmembrane	326 – 346	21	Helical; Potential
	Transmembrane	354 – 374	21	Helical; Potential
Sites
	Active site	272	1	Proton acceptor By similarity
	Metal binding	49	1	Magnesium By similarity
	Site	180	1	Important for substrate recognition By similarity

Sequences

	Sequence		Length	Mass (Da)
	O70572 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 5812FC630A69C356	FASTA	419	47,467
	10 20 30 40 50 60 MKLNFSLRLR VFNLNCWDIP YLSKHRADRM KRLGDFLNLE NFDLALLEEV WSEQDFQYLR 70 80 90 100 110 120 QRLSLTYPDA HYFRSGMIGS GLCVFSKHPI QEIFQHVYSL NGYPYMFHHG DWFCGKSVGL 130 140 150 160 170 180 LVLRLSGLVL NAYVTHLHAE YSRQKDIYFA HRVAQAWELA QFIHHTSKNA DVVLLCGDLN 190 200 210 220 230 240 MHPKDLGCCL LKEWTGLHDA FVETEDFKGS DDGCTMVPKN CYVSQQDLGP FPSGIRIDYV 250 260 270 280 290 300 LYKAVSEFHV CCETLKTTTG CDPHSDKPFS DHEALMATLY VKHSPPQEDP CTACGPLERS 310 320 330 340 350 360 DLISVLREAR TELGLGIAKA RWWAAFSGYV IVWGLSLLVL LCVLAAGEEA REVAIILCIP 370 380 390 400 410 SVGLVLVAGA VYLFHKQEAK GLCRAQAEML HVLTRETETQ DRGSEPHLAY CLQQEGDRA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloned mammalian neutral sphingomyelinase: functions in sphingolipid signaling?" Tomiuk S., Hofmann K., Nix M., Zumbansen M., Stoffel W. Proc. Natl. Acad. Sci. U.S.A. 95:3638-3643(1998) [PubMed: 9520418] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, TISSUE SPECIFICITY.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Salivary gland.
[3]	"Neutral sphingomyelinase 2 (smpd3) in the control of postnatal growth and development." Stoffel W., Jenke B., Bloeck B., Zumbansen M., Koebke J. Proc. Natl. Acad. Sci. U.S.A. 102:4554-4559(2005) [PubMed: 15764706] [Abstract] Cited for: DISRUPTION PHENOTYPE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ222800 mRNA. Translation: CAA10994.1. BC010978 mRNA. Translation: AAH10978.1.
IPI	IPI00119432.
RefSeq	NP_033239.1. NM_009213.2.
UniGene	Mm.953.
3D structure databases
ProteinModelPortal	O70572.
ModBase	Search...
Protein-protein interaction databases
STRING	O70572.
Proteomic databases
PRIDE	O70572.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000019965; ENSMUSP00000019965; ENSMUSG00000019822.
GeneID	20598.
KEGG	mmu:20598.
UCSC	uc007exs.1. mouse.
Organism-specific databases
CTD	6610.
MGI	MGI:1278330. Smpd2.
Phylogenomic databases
eggNOG	roNOG07612.
HOGENOM	HBG447226.
HOVERGEN	HBG019089.
InParanoid	O70572.
OMA	CWGIPYL.
OrthoDB	EOG4X3H1B.
PhylomeDB	O70572.
Gene expression databases
ArrayExpress	O70572.
Bgee	O70572.
CleanEx	MM_SMPD2.
Genevestigator	O70572.
GermOnline	ENSMUSG00000019822. Mus musculus.
Family and domain databases
InterPro	IPR005135. Endo/exonuclease/phosphatase. [Graphical view]
KO	K12351.
Pfam	PF03372. Exo_endo_phos. 1 hit. [Graphical view]
SUPFAM	SSF56219. Exo_endo_phos. 1 hit.
ProtoNet	Search...
Other
NextBio	298919.
SOURCE	Search...

Entry information

Entry name

NSMA_MOUSE

Accession

Primary (citable) accession number: O70572

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 11, 2002
Last sequence update:	August 1, 1998
Last modified:	November 16, 2011
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program