Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q04519 (ASM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sphingomyelin phosphodiesterase

EC=3.1.4.12
Alternative name(s):
Acid sphingomyelinase
Short name=aSMase
Gene names
Name:Smpd1
Synonyms:Asm
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length627 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Converts sphingomyelin to ceramide. Also has phospholipase C activities toward 1,2-diacylglycerolphosphocholine and 1,2-diacylglycerolphosphoglycerol.

Catalytic activity

Sphingomyelin + H2O = N-acylsphingosine + phosphocholine.

Subunit structure

Monomer.

Subcellular location

Lysosome.

Miscellaneous

There are two types of sphingomyelinases: ASM (acid), and NSM (neutral).

Sequence similarities

Belongs to the acid sphingomyelinase family.

Contains 1 saposin B-type domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4444 Potential
Chain45 – 627583Sphingomyelin phosphodiesterase
PRO_0000002324

Regions

Domain83 – 16785Saposin B-type

Amino acid modifications

Glycosylation841N-linked (GlcNAc...) Potential
Glycosylation1731N-linked (GlcNAc...) Potential
Glycosylation3331N-linked (GlcNAc...) Potential
Glycosylation3931N-linked (GlcNAc...) Potential
Glycosylation5181N-linked (GlcNAc...) Potential
Glycosylation6111N-linked (GlcNAc...) Potential
Disulfide bond87 ↔ 163 By similarity
Disulfide bond90 ↔ 155 By similarity
Disulfide bond118 ↔ 129 By similarity
Disulfide bond219 ↔ 224 By similarity
Disulfide bond225 ↔ 248 By similarity
Disulfide bond383 ↔ 429 By similarity
Disulfide bond582 ↔ 586 By similarity
Disulfide bond592 ↔ 605 By similarity

Experimental info

Sequence conflict481S → T in AAH11304. Ref.4
Sequence conflict4501G → S in AAH11304. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q04519 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: 0FFC7EA74EE71E91

FASTA62769,927
        10         20         30         40         50         60 
MPHHRASSGQ DHLRAGWEQR LERSLPAPRV GLLWMGLGLA LVLALFDSTV LWVPARAYPL 

        70         80         90        100        110        120 
PSEGHSVKFS AIAPPLQSAF GWQNLTCPAC KVLFTALNHG LKKEPNVARV GSVAIKICKM 

       130        140        150        160        170        180 
LNIAPLDVCQ SAVHLFEDDV VEVWTRSVLS PSEACGLLLG SSCGHWDIFS TWNISLPSVP 

       190        200        210        220        230        240 
KPPPKPPSPP APGAPVSRVL FLTDLHWDHE YLEGTDPYCA DPLCCRRGSG WPPNSQKGAG 

       250        260        270        280        290        300 
FWGEYSKCDL PLRTLESLLK GLGPAGPFEM VYWTGDIPAH DVWQQSRQDQ LRALTTITDL 

       310        320        330        340        350        360 
VRKFLGPVPV YPAVGNHEST PVNGFPPPFI KGNQSSQWLY EAMAKAWEPW LPADALHTLR 

       370        380        390        400        410        420 
IGGFYALTPR PGLRLISLNM NFCSRENFWL LINSTDPAGQ LQWLVEELQA AENRGDKVHI 

       430        440        450        460        470        480 
IGHIPPGHCL KSWSWNYYKI IARYENTLAG QFFGHTHVDE FEIFYDEETL SRPLAVAFLA 

       490        500        510        520        530        540 
PSATTFINLN PGYRVYQIDG NYPGSSHVVL DHETYILNLT QANAAGGTPS WKRLYRARET 

       550        560        570        580        590        600 
YGLPDAMPAS WHNLVYRMRD DEQLFQTFWF LYHKGHPPSE PCGTPCRLAT LCAQLSARAD 

       610        620 
SPALCRHLMP NGSLPDANRL WSRPLLC 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of the acid sphingomyelinase of the mouse and the organization and complete nucleotide sequence of the gene."
Newrzella D., Stoffel W.
Biol. Chem. Hoppe-Seyler 373:1233-1238(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Liver.
[2]Hofmann K.
Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 224-225 AND 384.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Hippocampus and Thymus.
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z14252 mRNA. Translation: CAA78619.1.
Z14132 Genomic DNA. Translation: CAA78506.1.
AK088147 mRNA. Translation: BAC40171.1.
AK145534 mRNA. Translation: BAE26489.1.
AK145702 mRNA. Translation: BAE26598.1.
AK164167 mRNA. Translation: BAE37659.1.
BC011304 mRNA. Translation: AAH11304.1.
PIRS27393. A58720.
RefSeqNP_035551.1. NM_011421.2.
UniGeneMm.4628.

3D structure databases

ProteinModelPortalQ04519.
SMRQ04519. Positions 86-164, 255-322.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-1604473.

PTM databases

PhosphoSiteQ04519.

Proteomic databases

PaxDbQ04519.
PRIDEQ04519.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000046983; ENSMUSP00000042187; ENSMUSG00000037049.
GeneID20597.
KEGGmmu:20597.
UCSCuc009iyf.2. mouse.

Organism-specific databases

CTD6609.
MGIMGI:98325. Smpd1.

Phylogenomic databases

eggNOGNOG303902.
GeneTreeENSGT00530000063095.
HOGENOMHOG000008599.
HOVERGENHBG004288.
InParanoidQ04519.
KOK12350.
OMAADPLCCR.
OrthoDBEOG79PJP3.
TreeFamTF313674.

Gene expression databases

BgeeQ04519.
CleanExMM_SMPD1.
GenevestigatorQ04519.

Family and domain databases

Gene3D1.10.225.10. 1 hit.
InterProIPR004843. PEstase_dom.
IPR011001. Saposin-like.
IPR008139. SaposinB.
IPR011160. Sphingomy_PDE.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PIRSFPIRSF000948. Sphingomy_PDE. 1 hit.
SMARTSM00741. SapB. 1 hit.
[Graphical view]
SUPFAMSSF47862. SSF47862. 1 hit.
PROSITEPS50015. SAP_B. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSMPD1. mouse.
NextBio298915.
PROQ04519.
SOURCESearch...

Entry information

Entry nameASM_MOUSE
AccessionPrimary (citable) accession number: Q04519
Secondary accession number(s): Q3UL52
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: February 1, 1996
Last modified: February 19, 2014
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot