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Q8R4X1 (ACER1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 81. 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:
Alkaline ceramidase 1

Short name=AlkCDase 1
Short name=Alkaline CDase 1
Short name=maCER1
EC=3.5.1.23
Alternative name(s):
Acylsphingosine deacylase 3
N-acylsphingosine amidohydrolase 3
Gene names
Name:Acer1
Synonyms:Asah3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length273 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. Ref.1

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 273273Alkaline ceramidase 1
PRO_0000247746

Regions

Topological domain1 – 3636Lumenal Potential
Transmembrane37 – 5721Helical; Potential
Topological domain58 – 7215Cytoplasmic Potential
Transmembrane73 – 9321Helical; Potential
Transmembrane94 – 11421Helical; Potential
Topological domain115 – 12612Cytoplasmic Potential
Transmembrane127 – 14721Helical; Potential
Topological domain148 – 1492Lumenal Potential
Transmembrane150 – 16718Helical; Potential
Topological domain168 – 17710Cytoplasmic Potential
Transmembrane178 – 19821Helical; Potential
Topological domain199 – 21517Lumenal Potential
Transmembrane216 – 23621Helical; Potential
Topological domain237 – 27337Cytoplasmic Potential

Sequences

Sequence LengthMass (Da)Tools
Q8R4X1 [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

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF347023 mRNA. Translation: AAL83821.1.
AK028901 mRNA. Translation: BAC26186.1.
AK075884 mRNA. Translation: BAC36029.1.
BC130254 mRNA. Translation: AAI30255.1.
CCDSCCDS28919.1.
RefSeqNP_783858.1. NM_175731.4.
UniGeneMm.218784.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ8R4X1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000056113; ENSMUSP00000062037; ENSMUSG00000045019.
GeneID171168.
KEGGmmu:171168.
UCSCuc008ddl.1. mouse.

Organism-specific databases

CTD125981.
MGIMGI:2181962. Acer1.

Phylogenomic databases

eggNOGNOG323012.
GeneTreeENSGT00730000110920.
HOGENOMHOG000220878.
InParanoidA1L3S2.
KOK01441.
OMAFQYSELV.
OrthoDBEOG7F5127.
PhylomeDBQ8R4X1.
TreeFamTF313019.

Enzyme and pathway databases

BRENDA3.5.1.23. 3474.

Gene expression databases

BgeeQ8R4X1.
GenevestigatorQ8R4X1.

Family and domain databases

InterProIPR008901. Ceramidase.
[Graphical view]
PfamPF05875. Ceramidase. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio370572.
PROQ8R4X1.
SOURCESearch...

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: July 9, 2014
This is version 81 of the entry and version 1 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