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Reviewed, UniProtKB/Swiss-Prot Q8R4X1 (ACER1_MOUSE)

Last modified November 3, 2009. Version 47. 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:
    Alkaline ceramidase 1
      Short name=Alkaline CDase 1
      Short name=AlkCDase 1
      Short name=maCER1
    EC=3.5.1.23
Alternative name(s):
    N-acylsphingosine amidohydrolase 3
    Acylsphingosine deacylase 3
Gene names
Name: Acer1
Synonyms: Asah3
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length273 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid at an optimal pH of 8.0. Has a highly restricted substrate specificity for the natural stereoisomer of ceramide with D-erythro-sphingosine but not D-ribo-phytosphingosine or D-erythro-dihydrosphingosine as a backbone. May have a role in regulating the levels of bioactive lipids ceramide and sphingosine 1-phosphate, as well as complex sphingolipids. Ref.1

Catalytic activity

N-acylsphingosine + H2O = a carboxylate + sphingosine.

Enzyme regulation

Inhibited by sphingosine. Inhibited by Mn2+, Zn2+, and Cu2+ in a dose-dependent manner. Slightly activated by Ca2+ in a dose-dependent manner. Ref.1

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein. Ref.1

Tissue specificity

Highly expressed in skin. Weakly or not expressed in other tissues. Ref.1

Sequence similarities

Belongs to the alkaline ceramidase family.

Biophysicochemical properties

pH dependence:

Optimum pH is 8.0.

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Ontologies

Keywords
   Biological processLipid metabolism
   Cellular componentEndoplasmic reticulum
Membrane
   DomainTransmembrane
   Molecular functionHydrolase
Gene Ontology (GO)
   Biological processceramide catabolic process Ref.1

Inferred from direct assay. Source: MGI

regulation of lipid metabolic process Ref.1

Inferred from direct assay. Source: MGI

   Cellular componentGolgi membrane

Inferred from electronic annotation. Source: InterPro

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: InterPro

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionceramidase activity Ref.1

Inferred from direct assay. Source: MGI

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 273273Alkaline ceramidase 1
PRO_0000247746

Regions

Transmembrane37 – 5721 Potential
Transmembrane73 – 9321 Potential
Transmembrane94 – 11421 Potential
Transmembrane127 – 14721 Potential
Transmembrane150 – 16718 Potential
Transmembrane178 – 19821 Potential
Transmembrane216 – 23621 Potential

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Sequences

Sequence LengthMass (Da)Tools
Q8R4X1-1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 0B84D015D7870219

FASTA27332,082
        10         20         30         40         50         60 
MHVPGTRAKM SSIFAYQSSE VDWCESNFQH SELVAEFYNT FSNVFFLIFG PLMMFLMHPY 

        70         80         90        100        110        120 
AQKRTRCFYG VSVLFMLIGL FSMYFHMTLS FLGQLLDEIS ILWLLASGYS VWLPRCYFPK 

       130        140        150        160        170        180 
FVKGNRFYFS CLVTITTIIS TFLTFVKPTV NAYALNSIAI HILYIVRTEY KKIRDDDLRH 

       190        200        210        220        230        240 
LIAVSVVLWA AALTSWISDR VLCSFWQRIH FYYLHSIWHV LISITFPYGI VTMALVDAKY 

       250        260        270 
EMPDKTLKVH YWPRDSWVIG LPYVEIQEND KNC

« Hide

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References

« Hide 'large scale' references
[1]"Cloning and characterization of a mouse endoplasmic reticulum alkaline ceramidase: an enzyme that preferentially regulates metabolism of very long chain ceramides."
Mao C., Xu R., Szulc Z.M., Bielawski J., Becker K.P., Bielawska A., Galadari S.H., Hu W., Obeid L.M.
J. Biol. Chem. 278:31184-31191(2003) [PubMed: 12783875] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]"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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Skin and Tongue.
[3]"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].
+Additional computationally mapped references.

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Cross-references

Sequence databases

AF347023 mRNA. Translation: AAL83821.1.
AK028901 mRNA. Translation: BAC26186.1.
AK075884 mRNA. Translation: BAC36029.1.
BC130254 mRNA. Translation: AAI30255.1.
IPIIPI00153946.
RefSeqNP_783858.1.
UniGeneMm.218784

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ8R4X1.

Proteomic databases

PRIDEQ8R4X1.

Genome annotation databases

EnsemblENSMUST00000056113; ENSMUSP00000062037; ENSMUSG00000045019; Mus musculus. [Genome view]
GeneID171168.
KEGGmmu:171168.
UCSCuc008ddl.1. mouse.

Organism-specific databases

CTD171168.
MGIMGI:2181962. Acer1.

Phylogenomic databases

HOVERGENQ8R4X1.
OMAFQYSELV.

Enzyme and pathway databases

BRENDA3.5.1.23. 244.

Gene expression databases

ArrayExpressQ8R4X1.
BgeeQ8R4X1.
GenevestigatorQ8R4X1.
GermOnlineENSMUSG00000045019. Mus musculus.

Family and domain databases

InterProIPR008901. APHC.
[Graphical view]
PfamPF05875. aPHC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio370572.
SOURCESearch...

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Entry information

Entry nameACER1_MOUSE
AccessionPrimary (citable) accession number: Q8R4X1
Secondary accession number(s): A1L3S2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: June 1, 2002
Last modified: November 3, 2009
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

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

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