Acer1

Alkaline ceramidase 1

Identifiers

ACER1; ALKCDase1; ASAH3

External IDs

OMIM: 613491 MGI: 2181962 HomoloGene: 15853 GeneCards: ACER1 Gene

3.5.1.23

Gene Ontology
Molecular function	• hydrolase activity • ceramidase activity
Cellular component	• endoplasmic reticulum • endoplasmic reticulum membrane • membrane • integral to membrane
Biological process	• sphingolipid metabolic process • regulation of lipid metabolic process • sphingolipid biosynthetic process • small molecule metabolic process • ceramide catabolic process
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 19:
6.31 – 6.33 Mb

Chr 17:
57.09 – 57.12 Mb

PubMed search

[1]

[2]

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

Function [link]

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

References [link]

^ ^a ^b 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.

Further reading [link]

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. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
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. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2394760.
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. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
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.

Metabolism: lipid metabolism · glycolipid enzymes

Sphingolipid

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