Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9WV54

- ASAH1_MOUSE

UniProt

Q9WV54 - ASAH1_MOUSE

Protein

Acid ceramidase

Gene

Asah1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    ReactomeiREACT_199008. 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: Chromosome 8

    Organism-specific databases

    MGIiMGI:1277124. Asah1.

    Subcellular locationi

    GO - Cellular componenti

    1. lysosome Source: UniProtKB-SubCell

    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

    ArrayExpressiQ9WV54.
    BgeeiQ9WV54.
    CleanExiMM_ASAH1.
    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

    MRGQSLLTWV LAAAVTCAQA QDVPPWTEDC RKSTYPPSGP TYRGPVPWHT    50
    INLDLPPYKR WHELLAQKAP ALRILVNSIT SLVNTFVPSG KLMKMVDQKL 100
    PGMIGSLPDP FGEEMRGIAD VTGIPLGEII SFNIFYELFT MCTSIITEDE 150
    KGHLLHGRNM DFGIFLGWNI NNNTWVVTEE LKPLTVNLDF QRNNKTVFKA 200
    TSFVGYVGML TGFKPGLFSL SLNERFSING GYLGILEWMF GRKDAQWVGF 250
    ITRSVLENTT SYEEAKNTLT KTKIMAPVYF ILGGKKSGEG CVITRERKES 300
    LDVYELDPKH GRWYVVQTNY DRWKNTLFID DRRTPAKKCL NHTTQKNLSF 350
    ATIYDVLSTK PVLNKLTVFT TLMDVTKGQF ESHLRDCPDP CIGW 394
    Length:394
    Mass (Da):44,670
    Last modified:November 1, 1999 - v1
    Checksum:iDA7BFBFDC45C9F65
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF157500 mRNA. Translation: AAD39551.1 .
    AK075666 mRNA. Translation: BAC35884.1 .
    BC003204 mRNA. Translation: AAH03204.1 .
    CCDSi CCDS22262.1.
    RefSeqi NP_062708.1. NM_019734.2.
    UniGenei Mm.22547.

    3D structure databases

    ProteinModelPortali Q9WV54.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9WV54. 1 interaction.
    MINTi MINT-4088419.

    Protein family/group databases

    MEROPSi C89.001.

    PTM databases

    PhosphoSitei Q9WV54.

    Proteomic databases

    MaxQBi Q9WV54.
    PaxDbi Q9WV54.
    PRIDEi Q9WV54.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000034000 ; ENSMUSP00000034000 ; ENSMUSG00000031591 .
    GeneIDi 11886.
    KEGGi mmu:11886.
    UCSCi uc009lnw.2. mouse.

    Organism-specific databases

    CTDi 427.
    MGIi MGI:1277124. Asah1.

    Phylogenomic databases

    eggNOGi NOG84249.
    GeneTreei ENSGT00530000063548.
    HOGENOMi HOG000007253.
    HOVERGENi HBG050586.
    InParanoidi Q9WV54.
    KOi K12348.
    OMAi YTINLDL.
    OrthoDBi EOG7TTQ7P.
    PhylomeDBi Q9WV54.
    TreeFami TF313219.

    Enzyme and pathway databases

    Reactomei REACT_199008. Glycosphingolipid metabolism.

    Miscellaneous databases

    NextBioi 279921.
    PROi Q9WV54.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9WV54.
    Bgeei Q9WV54.
    CleanExi MM_ASAH1.
    Genevestigatori Q9WV54.

    Family and domain databases

    InterProi IPR016699. Acid_ceramidase-like.
    IPR029130. Acid_ceramidase_N.
    IPR029132. CBAH/NAAA_C.
    [Graphical view ]
    Pfami PF02275. CBAH. 1 hit.
    PF15508. NAAA-beta. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF017632. Acid_ceramidase-like. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    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: October 1, 2014
    This is version 103 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