ACER1

Alkaline ceramidase 1

Identifiers

ACER1 ; ALKCDase1; ASAH3

External IDs

Gene ontology
Molecular function	• ceramidase activity • dihydroceramidase activity
Cellular component	• endoplasmic reticulum • endoplasmic reticulum membrane • integral to membrane
Biological process	• sphingolipid metabolic process • epidermis development • response to alkalinity • regulation of lipid metabolic process • sphingolipid biosynthetic process • cell differentiation • keratinocyte differentiation • small molecule metabolic process • sphingosine biosynthetic process • ceramide catabolic process • cellular response to calcium ion
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

PubMed search

Alkaline ceramidase 1 also known as ACER1 is a ceramidase enzyme which in humans is encoded by the ACER1 gene.^[1]

Function

ACER1 mediates cellular differentiation by controlling the generation of sphingosine (SPH) and sphingosine-1-phosphate (S1P).^[1]

↑ 1.0 1.1 Mao C, Xu R, Szulc ZM, Bielawski J, Becker KP, Bielawska A, Galadari SH, Hu W, Obeid LM (August 2003). "Cloning and characterization of a mouse endoplasmic reticulum alkaline ceramidase: an enzyme that preferentially regulates metabolism of very long chain ceramides". J. Biol. Chem. 278 (33): 31184–91. doi:10.1074/jbc.M303875200. PMID 12783875.

Sun W, Xu R, Hu W et al. (2008). "Upregulation of the human alkaline ceramidase 1 and acid ceramidase mediates calcium-induced differentiation of epidermal keratinocytes.". J. Invest. Dermatol. 128 (2): 389–97. doi:10.1038/sj.jid.5701025. PMID 17713573.
Strausberg RL, Feingold EA, Grouse LH et al. (2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Toulza E, Mattiuzzo NR, Galliano MF et al. (2007). "Large-scale identification of human genes implicated in epidermal barrier function.". Genome Biol. 8 (6): R107. doi:10.1186/gb-2007-8-6-r107. PMC 2394760. PMID 17562024.
Ito M, Okino N, Tani M et al. (2002). "[Molecular evolution of neutral ceramidase: signalling molecule and virulence factor]". Tanpakushitsu Kakusan Koso 47 (4 Suppl): 455–62. PMID 11915342.
Gerhard DS, Wagner L, Feingold EA et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Houben E, Holleran WM, Yaginuma T et al. (2006). "Differentiation-associated expression of ceramidase isoforms in cultured keratinocytes and epidermis.". J. Lipid Res. 47 (5): 1063–70. doi:10.1194/jlr.M600001-JLR200. PMID 16477081.

To glycosphingolipid	Glycosyltransferase Sulfotransferase

To ceramide	From ganglioside Beta-galactosidase Hexosaminidase A Neuraminidase Glucocerebrosidase From globoside Hexosaminidase B Alpha-galactosidase Beta-galactosidase Glucocerebrosidase From sphingomyelin Sphingomyelin phosphodiesterase Sphingomyelin phosphodiesterase 1 From sulfatide Arylsulfatase A Galactosylceramidase

To sphingosine	Ceramidase ACER1 ACER2 ACER3 ASAH1 ASAH2 ASAH2B ASAH2C

Other	Sphingosine kinase

Index of inborn errors of metabolism

Description	Metabolism Enzymes and pathways: citric acid cycle enzymes pentose phosphate intermediates glycoproteins enzymes glycosaminoglycans proteoglycan enzymes phospholipid metabolism cholesterol and steroid intermediates sphingolipids enzymes eicosanoids enzymes amino acid intermediates urea cycle enzymes nucleotide intermediates

Disorders	Citric acid cycle and electron transport chain Glycoprotein Proteoglycan Fatty-acid Phospholipid Cholesterol and steroid Eicosanoid Amino acid Purine-pyrimidine Heme metabolism Symptoms and signs

Treatment	Drugs other