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Reviewed, UniProtKB/Swiss-Prot Q9ET64 (NSMA_RAT)

Last modified January 19, 2010. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Sphingomyelin phosphodiesterase 2
    EC=3.1.4.12
Alternative name(s):
    Neutral sphingomyelinase
      Short name=nSMase
      Short name=N-SMase
    Lyso-platelet-activating factor-phospholipase C
      Short name=Lyso-PAF-PLC
Gene names
Name: Smpd2
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length422 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Catalytic activity

Sphingomyelin + H2O = N-acylsphingosine + choline phosphate.

Cofactor

Magnesium.

Subcellular location

Membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the neutral sphingomyelinase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 422422Sphingomyelin phosphodiesterase 2
PRO_0000075688

Regions

Transmembrane325 – 34521 Potential
Transmembrane354 – 37421 Potential

Sites

Active site2721Proton acceptor Probable
Metal binding491Magnesium By similarity
Site1801Important for substrate recognition By similarity

Experimental info

Mutagenesis1361H → A: Complete loss of activity.
Mutagenesis1511H → A: Reduced activity.
Mutagenesis1511H → Y: Complete loss of activity.
Mutagenesis2721H → A: Complete loss of activity.

Sequences

Sequence LengthMass (Da)Tools
Q9ET64-1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 109A5133A056AAF1

FASTA42247,645
        10         20         30         40         50         60 
MKHNFSLRLR VFNLNCWDIP YLSKHRADRM KRLGDFLNLE SFDLALLEEV WSEQDFQYLK 

        70         80         90        100        110        120 
QKLSLTYPDA HYFRSGIIGS GLCVFSRHPI QEIVQHVYTL NGYPYKFYHG DWFCGKAVGL 

       130        140        150        160        170        180 
LVLHLSGLVL NAYVTHLHAE YSRQKDIYFA HRVAQAWELA QFIHHTSKKA NVVLLCGDLN 

       190        200        210        220        230        240 
MHPKDLGCCL LKEWTGLRDA FVETEDFKGS EDGCTMVPKN CYVSQQDLGP FPFGVRIDYV 

       250        260        270        280        290        300 
LYKAVSGFHI CCKTLKTTTG CDPHNGTPFS DHEALMATLC VKHSPPQEDP CSAHGSAERS 

       310        320        330        340        350        360 
ALISALREAR TELGRGIAQA RWWAALFGYV MILGLSLLVL LCVLAAGEEA REVAIMLWTP 

       370        380        390        400        410        420 
SVGLVLGAGA VYLFHKQEAK SLCRAQAEIQ HVLTRTTETQ DLGSEPHPTH CRQQEADRAE 


EK 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression of rat neutral sphingomyelinase: enzymological characterization and identification of essential histidine residues."
Mizutani Y., Tamiya-Koizumi K., Irie F., Hirabayashi Y., Miwa M., Yoshida S.
Biochim. Biophys. Acta 1485:236-246(2000) [PubMed: 10832103] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, MUTAGENESIS.
Strain: Sprague-Dawley.
Tissue: Liver.
[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: Spleen.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB047002 mRNA. Translation: BAB08219.1.
BC091139 mRNA. Translation: AAH91139.1.
IPIIPI00192440.
RefSeqNP_112650.1.
UniGeneRn.18572

3D structure databases

SMRQ9ET64. Positions 9-279.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9ET64.

Genome annotation databases

EnsemblENSRNOT00000000336; ENSRNOP00000000336; ENSRNOG00000000306; Rattus norvegicus. [Genome view]
GeneID83537.
KEGGrno:83537.
UCSCNM_031360. rat.

Organism-specific databases

CTD83537.
RGD619753. Smpd2.

Phylogenomic databases

eggNOGroNOG07612.
HOVERGENQ9ET64.
InParanoidQ9ET64.
OMADFQYLRQ.
OrthoDBEOG9GJ28P.
PhylomeDBQ9ET64.

Enzyme and pathway databases

BRENDA3.1.4.12. 248.

Gene expression databases

ArrayExpressQ9ET64.
GenevestigatorQ9ET64.
GermOnlineENSRNOG00000000306. Rattus norvegicus.

Family and domain databases

InterProIPR005135. Endo/exonuclease/phosphatase.
[Graphical view]
PfamPF03372. Exo_endo_phos. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio616049.

Entry information

Entry nameNSMA_RAT
AccessionPrimary (citable) accession number: Q9ET64
Secondary accession number(s): Q5BKB2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 11, 2002
Last sequence update: March 1, 2001
Last modified: January 19, 2010
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents