Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8R4X1

- ACER1_MOUSE

UniProt

Q8R4X1 - ACER1_MOUSE

(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)

Protein

Alkaline ceramidase 1

Gene

Acer1

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

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
Complete GO annotation...

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. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

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.
InParanoidiQ8R4X1.
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

        10         20         30         40         50
MHVPGTRAKM SSIFAYQSSE VDWCESNFQH SELVAEFYNT FSNVFFLIFG
60 70 80 90 100
PLMMFLMHPY AQKRTRCFYG VSVLFMLIGL FSMYFHMTLS FLGQLLDEIS
110 120 130 140 150
ILWLLASGYS VWLPRCYFPK FVKGNRFYFS CLVTITTIIS TFLTFVKPTV
160 170 180 190 200
NAYALNSIAI HILYIVRTEY KKIRDDDLRH LIAVSVVLWA AALTSWISDR
210 220 230 240 250
VLCSFWQRIH FYYLHSIWHV LISITFPYGI VTMALVDAKY EMPDKTLKVH
260 270
YWPRDSWVIG LPYVEIQEND KNC
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 Q8R4X1.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 84 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