Reviewed, UniProtKB/Swiss-Prot Q10916 (ASM1_CAEEL)

Names and origin

Protein names

Recommended name:
    Sphingomyelin phosphodiesterase 1
    EC=3.1.4.12
Alternative name(s):
    Acid sphingomyelinase 1

Gene names

Name:	asm-1
ORF Names:	B0252.2

Organism

Caenorhabditis elegans [Complete proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	564 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Converts sphingomyelin to ceramide. Ref.1
Catalytic activity	Sphingomyelin + H2O = N-acylsphingosine + choline phosphate. Ref.1
Cofactor	Zinc. Ref.1
Subcellular location	Secreted. Ref.1
Developmental stage	Preferentially expressed in embryos, lower expression in later development. Ref.1
Miscellaneous	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. UniProtKB P17405 Contains 1 saposin B-type domain.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ceramide biosynthetic process Ref.1 Inferred from direct assay. Source: UniProtKB sphingomyelin catabolic process Ref.1 Inferred from direct assay. Source: UniProtKB
Cellular component	extracellular region Ref.1 Inferred from direct assay. Source: UniProtKB
Molecular function	hydrolase 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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 17	17	Potential
	Chain	18 – 564	547	Sphingomyelin phosphodiesterase 1		PRO_0000002325
Regions
	Domain	37 – 121	85	Saposin B-type
Amino acid modifications
	Glycosylation	151	1	N-linked (GlcNAc...) Potential
	Glycosylation	221	1	N-linked (GlcNAc...) Potential
	Glycosylation	351	1	N-linked (GlcNAc...) Potential
	Glycosylation	430	1	N-linked (GlcNAc...) Potential
	Glycosylation	556	1	N-linked (GlcNAc...) Potential
	Disulfide bond	41 ↔ 117		By similarity
	Disulfide bond	44 ↔ 110		By similarity
	Disulfide bond	72 ↔ 83		By similarity UniProtKB P17405
	Disulfide bond	180 ↔ 185		By similarity UniProtKB P17405
	Disulfide bond	186 ↔ 206		By similarity UniProtKB P17405
	Disulfide bond	341 ↔ 389		By similarity UniProtKB P17405
	Disulfide bond	538 ↔ 542		By similarity UniProtKB P17405
	Disulfide bond	548 ↔ 561		By similarity UniProtKB P17405

Sequences

	Sequence		Length	Mass (Da)
	Q10916-1 [UniParc]. Last modified June 1, 2002. Version 2. Checksum: EE3C424B5D905159	FASTA	564	65,201
	10 20 30 40 50 60 MRIIYLISTV LLIYTNATVL RTKESIQNKV TYDKYGFQPL CISCTGLISV ASFFLKFDVS 70 80 90 100 110 120 EPVILEFATI VCKLFAKQPW AVCDGISSQF RDEFFYVFRR LANESPSQIC GIILPDCADP 130 140 150 160 170 180 TDPSESGWMV ALPPKPKRTR ISKKKVQKKP NMSMSQNLNV LQLTDLHVDF EYKYPSEANC 190 200 210 220 230 240 DDPVCCRVSV SEPKKAAGYW GSVGKCDIPF WTVENMLSHI NKTHMIDMVI MTGDYINHVD 250 260 270 280 290 300 WEYSIEEHLS VLRKLHRLVQ NTFPSTPIYW ALGNHEGVPV NSFAPHSVDE RFWPTWLYKE 310 320 330 340 350 360 FQTMSGPWLS EGAKDSLLKR GSYSTQVMDG LKLITLNTGF CEVTNFFLYL NQSDPDSSMS 370 380 390 400 410 420 WFVKELFESE KKGEQVYVLA HIPPGDSECL EGWAFNYYRV IQRFSSTIAA QFFGHDHLDY 430 440 450 460 470 480 FTVFYEDMHN VSSKPISVGY ASPSVTTFEY QNPAYRIYEI DPYNKFKIVD FTTYYADLEK 490 500 510 520 530 540 ATEDKKPVWE KLYSARQAHG MDDLSPLSWN KVIQKLFTSE KKREKFYQYA FRNFSPQCDS 550 560 TCQMQLMCNL RMGHHNSTLY CPTF

References

	« Hide 'large scale' referencesShow '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, COFACTOR, 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U23453 Genomic DNA. Translation: AAC46756.2.
PIR	T15291.
RefSeq	NP_495415.2.
UniGene	Cel.20294
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q10916.
Genome annotation databases
Ensembl	B0252.2; B0252.2; B0252.2; Caenorhabditis elegans. [Genome view]
GeneID	174131.
KEGG	cel:B0252.2.
NMPDR	fig|6239.3.peg.6071.
UCSC	B0252.2. c. elegans.
Organism-specific databases
CTD	174131.
WormBase	WBGene00000211. asm-1.
WormPep	B0252.2. CE30230. [WorfDB]
Phylogenomic databases
OMA	WALGNHE.
Enzyme and pathway databases
BRENDA	3.1.4.12. 672.
Gene expression databases
ArrayExpress	Q10916.
Family and domain databases
InterPro	IPR004843. M-pesterase. IPR008139. SaposinB. IPR011160. Sphingomy_PDE. [Graphical view]
Pfam	PF00149. Metallophos. 1 hit. [Graphical view]
PIRSF	PIRSF000948. Sphingomy_PDE. 1 hit.
SMART	SM00741. SapB. 1 hit. [Graphical view]
PROSITE	PS50015. SAP_B. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	882655.

Entry information

Entry name

ASM1_CAEEL

Accession

Primary (citable) accession number: Q10916

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2003
Last sequence update:	June 1, 2002
Last modified:	November 3, 2009
This is version 61 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Caenorhabditis annotation project