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Q8R4X1

- ACER1_MOUSE

UniProt

Q8R4X1 - ACER1_MOUSE

Protein

Alkaline ceramidase 1

Gene

Acer1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 1 (01 Jun 2002)
      Previous versions | rss
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    Functioni

    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.1 Publication

    Catalytic activityi

    N-acylsphingosine + H2O = a carboxylate + sphingosine.

    Enzyme regulationi

    Inhibited by sphingosine. Inhibited by Mn2+, Zn2+, and Cu2+ in a dose-dependent manner. Slightly activated by Ca2+ in a dose-dependent manner.1 Publication

    pH dependencei

    Optimum pH is 8.0.1 Publication

    GO - Molecular functioni

    1. ceramidase activity Source: MGI
    2. dihydroceramidase activity Source: Ensembl

    GO - Biological processi

    1. cellular response to calcium ion Source: Ensembl
    2. ceramide catabolic process Source: MGI
    3. keratinocyte differentiation Source: Ensembl
    4. regulation of lipid metabolic process Source: MGI
    5. response to alkaline pH Source: Ensembl
    6. sphingolipid metabolic process Source: MGI
    7. sphingosine biosynthetic process Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Lipid metabolism

    Enzyme and pathway databases

    BRENDAi3.5.1.23. 3474.
    ReactomeiREACT_198151. Sphingolipid de novo biosynthesis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alkaline ceramidase 1 (EC:3.5.1.23)
    Short name:
    AlkCDase 1
    Short name:
    Alkaline CDase 1
    Short name:
    maCER1
    Alternative name(s):
    Acylsphingosine deacylase 3
    N-acylsphingosine amidohydrolase 3
    Gene namesi
    Name:Acer1
    Synonyms:Asah3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:2181962. Acer1.

    Subcellular locationi

    Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication

    GO - Cellular componenti

    1. endoplasmic reticulum Source: MGI
    2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 273273Alkaline ceramidase 1PRO_0000247746Add
    BLAST

    Proteomic databases

    PRIDEiQ8R4X1.

    Expressioni

    Tissue specificityi

    Highly expressed in skin. Weakly or not expressed in other tissues.1 Publication

    Gene expression databases

    BgeeiQ8R4X1.
    GenevestigatoriQ8R4X1.

    Structurei

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 3636LumenalSequence AnalysisAdd
    BLAST
    Topological domaini58 – 7215CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini115 – 12612CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini148 – 1492LumenalSequence Analysis
    Topological domaini168 – 17710CytoplasmicSequence Analysis
    Topological domaini199 – 21517LumenalSequence AnalysisAdd
    BLAST
    Topological domaini237 – 27337CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei37 – 5721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei73 – 9321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei94 – 11421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei127 – 14721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei150 – 16718HelicalSequence AnalysisAdd
    BLAST
    Transmembranei178 – 19821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei216 – 23621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the alkaline ceramidase family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG323012.
    GeneTreeiENSGT00730000110920.
    HOGENOMiHOG000220878.
    InParanoidiA1L3S2.
    KOiK01441.
    OMAiFQYSELV.
    OrthoDBiEOG7F5127.
    PhylomeDBiQ8R4X1.
    TreeFamiTF313019.

    Family and domain databases

    InterProiIPR008901. Ceramidase.
    [Graphical view]
    PfamiPF05875. Ceramidase. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8R4X1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MHVPGTRAKM SSIFAYQSSE VDWCESNFQH SELVAEFYNT FSNVFFLIFG    50
    PLMMFLMHPY AQKRTRCFYG VSVLFMLIGL FSMYFHMTLS FLGQLLDEIS 100
    ILWLLASGYS VWLPRCYFPK FVKGNRFYFS CLVTITTIIS TFLTFVKPTV 150
    NAYALNSIAI HILYIVRTEY KKIRDDDLRH LIAVSVVLWA AALTSWISDR 200
    VLCSFWQRIH FYYLHSIWHV LISITFPYGI VTMALVDAKY EMPDKTLKVH 250
    YWPRDSWVIG LPYVEIQEND KNC 273
    Length:273
    Mass (Da):32,082
    Last modified:June 1, 2002 - v1
    Checksum:i0B84D015D7870219
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF347023 mRNA. Translation: AAL83821.1.
    AK028901 mRNA. Translation: BAC26186.1.
    AK075884 mRNA. Translation: BAC36029.1.
    BC130254 mRNA. Translation: AAI30255.1.
    CCDSiCCDS28919.1.
    RefSeqiNP_783858.1. NM_175731.4.
    UniGeneiMm.218784.

    Genome annotation databases

    EnsembliENSMUST00000056113; ENSMUSP00000062037; ENSMUSG00000045019.
    GeneIDi171168.
    KEGGimmu:171168.
    UCSCiuc008ddl.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF347023 mRNA. Translation: AAL83821.1 .
    AK028901 mRNA. Translation: BAC26186.1 .
    AK075884 mRNA. Translation: BAC36029.1 .
    BC130254 mRNA. Translation: AAI30255.1 .
    CCDSi CCDS28919.1.
    RefSeqi NP_783858.1. NM_175731.4.
    UniGenei Mm.218784.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q8R4X1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000056113 ; ENSMUSP00000062037 ; ENSMUSG00000045019 .
    GeneIDi 171168.
    KEGGi mmu:171168.
    UCSCi uc008ddl.1. mouse.

    Organism-specific databases

    CTDi 125981.
    MGIi MGI:2181962. Acer1.

    Phylogenomic databases

    eggNOGi NOG323012.
    GeneTreei ENSGT00730000110920.
    HOGENOMi HOG000220878.
    InParanoidi A1L3S2.
    KOi K01441.
    OMAi FQYSELV.
    OrthoDBi EOG7F5127.
    PhylomeDBi Q8R4X1.
    TreeFami TF313019.

    Enzyme and pathway databases

    BRENDAi 3.5.1.23. 3474.
    Reactomei REACT_198151. Sphingolipid de novo biosynthesis.

    Miscellaneous databases

    NextBioi 370572.
    PROi Q8R4X1.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8R4X1.
    Genevestigatori Q8R4X1.

    Family and domain databases

    InterProi IPR008901. Ceramidase.
    [Graphical view ]
    Pfami PF05875. Ceramidase. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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].

    Entry informationi

    Entry nameiACER1_MOUSE
    AccessioniPrimary (citable) accession number: Q8R4X1
    Secondary accession number(s): A1L3S2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 25, 2006
    Last sequence update: June 1, 2002
    Last modified: October 1, 2014
    This is version 83 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