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Protein

Acid ceramidase

Gene

Asah1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid.

Catalytic activityi

N-acylsphingosine + H2O = a carboxylate + sphingosine.

GO - Molecular functioni

  1. ceramidase activity Source: MGI

GO - Biological processi

  1. lipid metabolic process Source: InterPro
  2. lung development Source: Ensembl
  3. response to organic substance Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BRENDAi3.5.1.23. 3474.
ReactomeiREACT_339900. Glycosphingolipid metabolism.

Protein family/group databases

MEROPSiC89.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Acid ceramidase (EC:3.5.1.23)
Short name:
AC
Short name:
ACDase
Short name:
Acid CDase
Alternative name(s):
Acylsphingosine deacylase
N-acylsphingosine amidohydrolase
Cleaved into the following 2 chains:
Gene namesi
Name:Asah1
Synonyms:Asah
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1277124. Asah1.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: MGI
  2. lysosome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 141123Acid ceramidase subunit alphaPRO_0000002316Add
BLAST
Chaini142 – 394253Acid ceramidase subunit betaPRO_0000002317Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi172 – 1721N-linked (GlcNAc...)Sequence Analysis
Glycosylationi194 – 1941N-linked (GlcNAc...)Sequence Analysis
Glycosylationi258 – 2581N-linked (GlcNAc...)1 Publication
Glycosylationi341 – 3411N-linked (GlcNAc...)Sequence Analysis
Glycosylationi347 – 3471N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ9WV54.
PaxDbiQ9WV54.
PRIDEiQ9WV54.

PTM databases

PhosphoSiteiQ9WV54.

Expressioni

Gene expression databases

BgeeiQ9WV54.
CleanExiMM_ASAH1.
ExpressionAtlasiQ9WV54. baseline and differential.
GenevestigatoriQ9WV54.

Interactioni

Subunit structurei

Heterodimer of one alpha and one beta subunit.

Protein-protein interaction databases

IntActiQ9WV54. 1 interaction.
MINTiMINT-4088419.

Structurei

3D structure databases

ProteinModelPortaliQ9WV54.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the acid ceramidase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG84249.
GeneTreeiENSGT00530000063548.
HOGENOMiHOG000007253.
HOVERGENiHBG050586.
InParanoidiQ9WV54.
KOiK12348.
OMAiYTINLDL.
OrthoDBiEOG7TTQ7P.
PhylomeDBiQ9WV54.
TreeFamiTF313219.

Family and domain databases

InterProiIPR016699. Acid_ceramidase-like.
IPR029130. Acid_ceramidase_N.
IPR029132. CBAH/NAAA_C.
[Graphical view]
PfamiPF02275. CBAH. 1 hit.
PF15508. NAAA-beta. 1 hit.
[Graphical view]
PIRSFiPIRSF017632. Acid_ceramidase-like. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9WV54-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRGQSLLTWV LAAAVTCAQA QDVPPWTEDC RKSTYPPSGP TYRGPVPWHT
60 70 80 90 100
INLDLPPYKR WHELLAQKAP ALRILVNSIT SLVNTFVPSG KLMKMVDQKL
110 120 130 140 150
PGMIGSLPDP FGEEMRGIAD VTGIPLGEII SFNIFYELFT MCTSIITEDE
160 170 180 190 200
KGHLLHGRNM DFGIFLGWNI NNNTWVVTEE LKPLTVNLDF QRNNKTVFKA
210 220 230 240 250
TSFVGYVGML TGFKPGLFSL SLNERFSING GYLGILEWMF GRKDAQWVGF
260 270 280 290 300
ITRSVLENTT SYEEAKNTLT KTKIMAPVYF ILGGKKSGEG CVITRERKES
310 320 330 340 350
LDVYELDPKH GRWYVVQTNY DRWKNTLFID DRRTPAKKCL NHTTQKNLSF
360 370 380 390
ATIYDVLSTK PVLNKLTVFT TLMDVTKGQF ESHLRDCPDP CIGW
Length:394
Mass (Da):44,670
Last modified:November 1, 1999 - v1
Checksum:iDA7BFBFDC45C9F65
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF157500 mRNA. Translation: AAD39551.1.
AK075666 mRNA. Translation: BAC35884.1.
BC003204 mRNA. Translation: AAH03204.1.
CCDSiCCDS22262.1.
RefSeqiNP_062708.1. NM_019734.2.
UniGeneiMm.22547.

Genome annotation databases

EnsembliENSMUST00000034000; ENSMUSP00000034000; ENSMUSG00000031591.
GeneIDi11886.
KEGGimmu:11886.
UCSCiuc009lnw.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF157500 mRNA. Translation: AAD39551.1.
AK075666 mRNA. Translation: BAC35884.1.
BC003204 mRNA. Translation: AAH03204.1.
CCDSiCCDS22262.1.
RefSeqiNP_062708.1. NM_019734.2.
UniGeneiMm.22547.

3D structure databases

ProteinModelPortaliQ9WV54.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9WV54. 1 interaction.
MINTiMINT-4088419.

Protein family/group databases

MEROPSiC89.001.

PTM databases

PhosphoSiteiQ9WV54.

Proteomic databases

MaxQBiQ9WV54.
PaxDbiQ9WV54.
PRIDEiQ9WV54.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034000; ENSMUSP00000034000; ENSMUSG00000031591.
GeneIDi11886.
KEGGimmu:11886.
UCSCiuc009lnw.2. mouse.

Organism-specific databases

CTDi427.
MGIiMGI:1277124. Asah1.

Phylogenomic databases

eggNOGiNOG84249.
GeneTreeiENSGT00530000063548.
HOGENOMiHOG000007253.
HOVERGENiHBG050586.
InParanoidiQ9WV54.
KOiK12348.
OMAiYTINLDL.
OrthoDBiEOG7TTQ7P.
PhylomeDBiQ9WV54.
TreeFamiTF313219.

Enzyme and pathway databases

BRENDAi3.5.1.23. 3474.
ReactomeiREACT_339900. Glycosphingolipid metabolism.

Miscellaneous databases

ChiTaRSiAsah1. mouse.
NextBioi279921.
PROiQ9WV54.
SOURCEiSearch...

Gene expression databases

BgeeiQ9WV54.
CleanExiMM_ASAH1.
ExpressionAtlasiQ9WV54. baseline and differential.
GenevestigatoriQ9WV54.

Family and domain databases

InterProiIPR016699. Acid_ceramidase-like.
IPR029130. Acid_ceramidase_N.
IPR029132. CBAH/NAAA_C.
[Graphical view]
PfamiPF02275. CBAH. 1 hit.
PF15508. NAAA-beta. 1 hit.
[Graphical view]
PIRSFiPIRSF017632. Acid_ceramidase-like. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1997) [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.
    , 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(2004) [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(2003) [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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-258.

Entry informationi

Entry nameiASAH1_MOUSE
AccessioniPrimary (citable) accession number: Q9WV54
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: April 1, 2015
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.