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Reviewed, UniProtKB/Swiss-Prot Q23498 (ASM2_CAEEL)

Last modified January 19, 2010. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

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Names and origin

Protein namesRecommended name:
    Sphingomyelin phosphodiesterase 2
    EC=3.1.4.12
Alternative name(s):
    Acid sphingomyelinase 2
Gene names
Name: asm-2
ORF Names: ZK455.4
OrganismCaenorhabditis elegans [Complete proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

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Protein attributes

Sequence length618 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Converts sphingomyelin to ceramide. Ref.1

Catalytic activity

Sphingomyelin + H2O = N-acylsphingosine + choline phosphate. Ref.1

Subcellular location

Secreted Ref.1.

Developmental stage

Preferentially expressed in post-embryonic development. Ref.1

Miscellaneous

Fully active upon secretion independent of zinc ions. Ref.1

There are two types of sphingomyelinases: asm (acid), and nsm (neutral). Only acid sphingomyelinase has been found in worms. Ref.1 UniProtKB P17405

Sequence similarities

Belongs to the acid sphingomyelinase family.

Contains 1 saposin B-type domain.

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Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processceramide biosynthetic process Ref.1

Inferred from direct assay. Source: UniProtKB

sphingomyelin catabolic process Ref.1

Inferred from direct assay. Source: UniProtKB

   Cellular componentextracellular region Ref.1

Inferred from direct assay. Source: UniProtKB

   Molecular functionhydrolase activity, acting on glycosyl bonds

Inferred from electronic annotation. Source: UniProtKB-KW

sphingomyelin phosphodiesterase activity Ref.1

Inferred from direct assay. Source: UniProtKB

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 618596Sphingomyelin phosphodiesterase 2
PRO_0000002326

Regions

Domain68 – 15184Saposin B-type

Amino acid modifications

Glycosylation891N-linked (GlcNAc...) Potential
Glycosylation1591N-linked (GlcNAc...) Potential
Glycosylation2981N-linked (GlcNAc...) Potential
Glycosylation5251N-linked (GlcNAc...) Ref.3
Glycosylation5681N-linked (GlcNAc...) Potential
Disulfide bond72 ↔ 147 By similarity
Disulfide bond75 ↔ 140 By similarity
Disulfide bond103 ↔ 114 By similarity UniProtKB P17405
Disulfide bond204 ↔ 216 By similarity UniProtKB P17405
Disulfide bond217 ↔ 249 By similarity UniProtKB P17405
Disulfide bond387 ↔ 435 By similarity UniProtKB P17405
Disulfide bond588 ↔ 594 By similarity UniProtKB P17405
Disulfide bond600 ↔ 613 By similarity UniProtKB P17405

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Sequences

Sequence LengthMass (Da)Tools
Q23498-1 [UniParc].

Last modified June 1, 2003. Version 3.
Checksum: CF24C82DC09BA115

FASTA61871,925
        10         20         30         40         50         60 
MQQPLIILGI GIVLALVSNV ESGVLRKPVD EHEYEKWTNA RGNEAAVPPP KYKMLRYAKK 

        70         80         90        100        110        120 
AINEPENRKM SCLFCTFAVD GVQALIAQNS TDNEIAAFLV NLCDLFDVEQ PHVCKNIIYA 

       130        140        150        160        170        180 
FKDEVVFVLE RSVFTPEEIC GAFIANCGHS DKPLTHMWNI TIPGGKPPIK PWPKIPDNKP 

       190        200        210        220        230        240 
TFKVLHLSDI HIDHQYVVGT EAYCQLDSAL GTYAMCCRDY SQDSQGAPTN LKDKPIYVPA 

       250        260        270        280        290        300 
GPWGMPYLCD LPYQTFESAM KHISKTFKDL DYIIITGDFE AHDSWDYTED LTRENMNNMT 

       310        320        330        340        350        360 
NVFLEYFPGV PVYVSIGNHE GVPQDAMAPH TMPEYDTRGP QWLYKIMSEM WSHWIPQEAL 

       370        380        390        400        410        420 
DTVQYRASYA VYPKPGLKLI SLNTIYCSEF NFYLYVNEVD PDATLEWLIE ELQDSENKGE 

       430        440        450        460        470        480 
LVHIISHIPP GDNYCLKGWS WNFFEIVKRY ENTIAQMFYG HTHYDQFMVY YDMDDPNRRP 

       490        500        510        520        530        540 
FHFNWISPSL TTYDWLNPAY RIYEIDGGYE GATYTVKDAK TYFANVTEAN MKNKEPEWVL 

       550        560        570        580        590        600 
SYDTREHYQM ADFSPQSWSD LSDKLWTNTT LFRDYVRLYY RNHYNNECYT DYKCRYTFVC 

       610 
DIKKGRSYDE SFCDHLTK

« Hide

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References

« Hide 'large scale' references
[1]"Caenorhabditis elegans contains two distinct acid sphingomyelinases."
Lin X., Hengartner M.O., Kolesnick R.
J. Biol. Chem. 273:14374-14379(1998) [PubMed: 9603947] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
[2]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
[3]"Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis elegans and suggests an atypical translocation mechanism for integral membrane proteins."
Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T., Taoka M., Takahashi N., Isobe T.
Mol. Cell. Proteomics 6:2100-2109(2007) [PubMed: 17761667] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-525, MASS SPECTROMETRY.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z66567 Genomic DNA. Translation: CAA91493.2.
PIRT27869.
RefSeqNP_509894.2.
UniGeneCel.16898

3D structure databases

SMRQ23498. Positions 70-147, 179-467.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ23498.

Genome annotation databases

EnsemblZK455.4; ZK455.4; ZK455.4; Caenorhabditis elegans. [Genome view]
GeneID181323.
KEGGcel:ZK455.4.
UCSCZK455.4. c. elegans.

Organism-specific databases

CTD181323.
WormBaseWBGene00000212. asm-2.
WormPepZK455.4. CE31674. [WorfDB]

Phylogenomic databases

eggNOGmeNOG05776.
HOGENOMHBG390117.
InParanoidQ23498.
OMAMVYWTGD.
PhylomeDBQ23498.

Enzyme and pathway databases

BRENDA3.1.4.12. 672.

Gene expression databases

ArrayExpressQ23498.

Family and domain databases

InterProIPR004843. M-pesterase.
IPR007856. SapB_1.
IPR011001. Saposin-like.
IPR008139. SaposinB.
IPR011160. Sphingomy_PDE.
[Graphical view]
Gene3DG3DSA:1.10.225.10. Saposin_like. 1 hit.
PfamPF00149. Metallophos. 1 hit.
PF05184. SapB_1. 1 hit.
[Graphical view]
PIRSFPIRSF000948. Sphingomy_PDE. 1 hit.
SMARTSM00741. SapB. 1 hit.
[Graphical view]
PROSITEPS50015. SAP_B. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio913444.

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Entry information

Entry nameASM2_CAEEL
AccessionPrimary (citable) accession number: Q23498
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2003
Last sequence update: June 1, 2003
Last modified: January 19, 2010
This is version 62 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectCaenorhabditis annotation project

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Relevant documents

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormPep

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