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Q9WV54 (ASAH1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 101. 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:
Acid ceramidase

Short name=AC
Short name=ACDase
Short name=Acid CDase
EC=3.5.1.23
Alternative name(s):
Acylsphingosine deacylase
N-acylsphingosine amidohydrolase
Gene names
Name:Asah1
Synonyms:Asah
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length394 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid.

Catalytic activity

N-acylsphingosine + H2O = a carboxylate + sphingosine.

Subunit structure

Heterodimer of one alpha and one beta subunit.

Subcellular location

Lysosome.

Sequence similarities

Belongs to the acid ceramidase family.

Ontologies

Keywords
   Cellular componentLysosome
   DomainSignal
   Molecular functionHydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processlipid metabolic process

Inferred from electronic annotation. Source: InterPro

lung development

Inferred from electronic annotation. Source: Ensembl

response to organic substance

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentlysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionceramidase activity

Inferred from direct assay Ref.1. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 141123Acid ceramidase subunit alpha
PRO_0000002316
Chain142 – 394253Acid ceramidase subunit beta
PRO_0000002317

Amino acid modifications

Glycosylation1721N-linked (GlcNAc...) Potential
Glycosylation1941N-linked (GlcNAc...) Potential
Glycosylation2581N-linked (GlcNAc...) Ref.4
Glycosylation3411N-linked (GlcNAc...) Potential
Glycosylation3471N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q9WV54 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: DA7BFBFDC45C9F65

FASTA39444,670
        10         20         30         40         50         60 
MRGQSLLTWV LAAAVTCAQA QDVPPWTEDC RKSTYPPSGP TYRGPVPWHT INLDLPPYKR 

        70         80         90        100        110        120 
WHELLAQKAP ALRILVNSIT SLVNTFVPSG KLMKMVDQKL PGMIGSLPDP FGEEMRGIAD 

       130        140        150        160        170        180 
VTGIPLGEII SFNIFYELFT MCTSIITEDE KGHLLHGRNM DFGIFLGWNI NNNTWVVTEE 

       190        200        210        220        230        240 
LKPLTVNLDF QRNNKTVFKA TSFVGYVGML TGFKPGLFSL SLNERFSING GYLGILEWMF 

       250        260        270        280        290        300 
GRKDAQWVGF ITRSVLENTT SYEEAKNTLT KTKIMAPVYF ILGGKKSGEG CVITRERKES 

       310        320        330        340        350        360 
LDVYELDPKH GRWYVVQTNY DRWKNTLFID DRRTPAKKCL NHTTQKNLSF ATIYDVLSTK 

       370        380        390 
PVLNKLTVFT TLMDVTKGQF ESHLRDCPDP CIGW 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of the full-length cDNA and genomic sequences encoding murine acid ceramidase."
Li C.-M., Hong S.-B., Kopal G., He X., Linke T., Hou W.-S., Koch J., Gatt S., Sandhoff K., Schuchman E.H.
Genomics 50:267-274(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ICR.
Tissue: Brain.
[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.
[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].
Strain: Czech II.
Tissue: Mammary gland.
[4]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-258.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF157500 mRNA. Translation: AAD39551.1.
AK075666 mRNA. Translation: BAC35884.1.
BC003204 mRNA. Translation: AAH03204.1.
CCDSCCDS22262.1.
RefSeqNP_062708.1. NM_019734.2.
UniGeneMm.22547.

3D structure databases

ProteinModelPortalQ9WV54.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9WV54. 1 interaction.
MINTMINT-4088419.

Protein family/group databases

MEROPSC89.001.

PTM databases

PhosphoSiteQ9WV54.

Proteomic databases

MaxQBQ9WV54.
PaxDbQ9WV54.
PRIDEQ9WV54.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034000; ENSMUSP00000034000; ENSMUSG00000031591.
GeneID11886.
KEGGmmu:11886.
UCSCuc009lnw.2. mouse.

Organism-specific databases

CTD427.
MGIMGI:1277124. Asah1.

Phylogenomic databases

eggNOGNOG84249.
GeneTreeENSGT00530000063548.
HOGENOMHOG000007253.
HOVERGENHBG050586.
InParanoidQ9WV54.
KOK12348.
OMAYTINLDL.
OrthoDBEOG7TTQ7P.
PhylomeDBQ9WV54.
TreeFamTF313219.

Gene expression databases

ArrayExpressQ9WV54.
BgeeQ9WV54.
CleanExMM_ASAH1.
GenevestigatorQ9WV54.

Family and domain databases

InterProIPR016699. Acid_ceramidase-like.
IPR029130. Acid_ceramidase_N.
IPR029132. CBAH/NAAA_C.
[Graphical view]
PfamPF02275. CBAH. 1 hit.
PF15508. NAAA-beta. 1 hit.
[Graphical view]
PIRSFPIRSF017632. Acid_ceramidase-like. 1 hit.
ProtoNetSearch...

Other

NextBio279921.
PROQ9WV54.
SOURCESearch...

Entry information

Entry nameASAH1_MOUSE
AccessionPrimary (citable) accession number: Q9WV54
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 101 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