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Reviewed, UniProtKB/Swiss-Prot Q6P7S1 (ASAH1_RAT)

Last modified November 3, 2009. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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

Names and origin

Protein namesRecommended name:
    Acid ceramidase
      Short name=AC
    EC=3.5.1.23
Alternative name(s):
    Acylsphingosine deacylase
    N-acylsphingosine amidohydrolase
Gene names
Name: Asah1
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

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

General annotation (Comments)

Function

Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid By similarity.

Catalytic activity

N-acylsphingosine + H2O = a carboxylate + sphingosine.

Subunit structure

Heterodimer of one alpha and one beta subunit By similarity.

Subcellular location

Lysosome By similarity.

Sequence similarities

Belongs to the acid ceramidase family.

Ontologies

Keywords
   Cellular componentLysosome
   DomainSignal
   Molecular functionHydrolase
   PTMGlycoprotein
Gene Ontology (GO)
   Biological processlipid metabolic process

Inferred from electronic annotation. Source: InterPro

lung development

Inferred from direct assay. Source: RGD

response to organic substance

Inferred from direct assay. Source: RGD

   Cellular componentlysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionceramidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 394374Acid ceramidase
PRO_0000378102

Amino acid modifications

Glycosylation1941N-linked (GlcNAc...) Potential
Glycosylation2581N-linked (GlcNAc...) Potential
Glycosylation2851N-linked (GlcNAc...) Potential
Glycosylation3411N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict3751V → G in AAG43956. Ref.1
Sequence conflict3791Q → P in AAG43956. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q6P7S1-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 27608539E1E9ED20

FASTA39444,443
        10         20         30         40         50         60 
MLGRSLLTWV LAAAVTCAQA QQVPPWTEDC RKSTYPPSGP TYRGPVPWYT INLDLPPYKR 

        70         80         90        100        110        120 
WHELLAHKAP VLRTLVNSIS NLVNAFVPSG KIMQMVDEKL PGLIGSIPGP FGEEMRGIAD 

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

       190        200        210        220        230        240 
LKPLTVNLDF QRNNKTVFKA TSFAGYVGML TGFKPGLLSL TLNERFSLNG GYLGILEWMF 

       250        260        270        280        290        300 
GKKNAQWVGF ITRSVLENST SYEEAKNILT KTKITAPAYF ILGGNQSGEG CVITRERKES 

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

       370        380        390 
PVLNKLTVFT TLIDVTKDQF ESHLRDCPDP CIGW 

« Hide

References

« Hide 'large scale' references
[1]"Complete coding sequence of rat ceramidase."
Frenck J., Sol-Church K., McKay C., Mason R.
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"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].
Tissue: Pituitary.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF214647 mRNA. Translation: AAG43956.1.
BC061540 mRNA. Translation: AAH61540.1.
IPIIPI00421601.
RefSeqNP_445859.2.
UniGeneRn.127798

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ6P7S1.

Proteomic databases

PRIDEQ6P7S1.

Genome annotation databases

EnsemblENSRNOT00000013463; ENSRNOP00000013463; ENSRNOG00000010034; Rattus norvegicus. [Genome view]
GeneID84431.
KEGGrno:84431.
NMPDRfig|10116.3.peg.12488.
UCSCNM_053407. rat.

Organism-specific databases

CTD84431.
RGD621568. Asah1.

Phylogenomic databases

HOVERGENQ6P7S1.
OMANYDRWKN.

Gene expression databases

ArrayExpressQ6P7S1.
GenevestigatorQ6P7S1.

Family and domain databases

InterProIPR016699. Acid_ceramidase-like.
IPR003199. Chologlycine_hydro.
[Graphical view]
PfamPF02275. CBAH. 1 hit.
[Graphical view]
PIRSFPIRSF017632. Acid_ceramidase-like. 1 hit.
ProtoNetSearch...

Other Resources

NextBio616940.

Entry information

Entry nameASAH1_RAT
AccessionPrimary (citable) accession number: Q6P7S1
Secondary accession number(s): Q9EQJ6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2009
Last sequence update: July 5, 2004
Last modified: November 3, 2009
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

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