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Identification
HMDB Protein ID HMDBP10638
Secondary Accession Numbers
  • 16867
Name Alkaline ceramidase 1
Synonyms
  1. Acylsphingosine deacylase 3
  2. AlkCDase 1
  3. Alkaline CDase 1
  4. N-acylsphingosine amidohydrolase 3
Gene Name ACER1
Protein Type Enzyme
Biological Properties
General Function Involved in hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
Specific Function 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 (By similarity).
Pathways
  • Fabry disease
  • Gaucher Disease
  • Globoid Cell Leukodystrophy
  • Krabbe disease
  • Metachromatic Leukodystrophy (MLD)
  • Sphingolipid Metabolism
  • sphingolipid metabolism
Reactions
N-acylsphingosine + Water → a carboxylate + Sphingosine details
N-Acylsphingosine + Water → Fatty acid + Sphingosine details
Dihydroceramide + Water → Fatty acid + Sphinganine details
Phytoceramide + Water → Fatty acid + Phytosphingosine details
GO Classification
Biological Process
cellular response to calcium ion
ceramide catabolic process
keratinocyte differentiation
phospholipid metabolic process
regulation of lipid metabolic process
response to alkalinity
sphingosine biosynthetic process
Cellular Component
endoplasmic reticulum membrane
integral to membrane
Component
cell part
membrane part
intrinsic to membrane
integral to membrane
Function
catalytic activity
hydrolase activity
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
Molecular Function
dihydroceramidase activity
Process
sphingoid metabolic process
metabolic process
ceramide metabolic process
sphingolipid metabolic process
membrane lipid metabolic process
primary metabolic process
lipid metabolic process
cellular lipid metabolic process
Cellular Location
  1. Endoplasmic reticulum membrane
  2. Multi-pass membrane protein
Gene Properties
Chromosome Location 19
Locus 19p13.3
SNPs ACER1
Gene Sequence
>795 bp
ATGCCTAGCATCTTCGCCTATCAGAGCTCCGAGGTGGACTGGTGTGAGAGCAACTTCCAG
TACTCGGAGCTGGTGGCCGAGTTCTACAACACGTTCTCCAATATCCCCTTCTTCATCTTC
GGGCCACTGATGATGCTCCTGATGCACCCGTATGCCCAGAAGCGCTCCCGCTACATTTAC
GTTGTCTGGGTCCTCTTCATGATCATAGGCCTGTTCTCCATGTATTTCCACATGACGCTC
AGCTTCCTGGGCCAGCTGCTGGACGAGATCGCCATCCTGTGGCTCCTGGGCAGTGGCTAT
AGCATATGGATGCCCCGCTGCTATTTCCCCTCCTTCCTTGGGGGGAACAGGTCCCAGTTC
ATCCGCCTGGTCTTCATCACCACTGTGGTCAGCACCCTTCTGTCCTTCCTGCGGCCCACG
GTCAACGCCTACGCCCTCAACAGCATTGCCCTGCACATTCTCTACATCGTGTGCCAGGAG
TACAGGAAGACCAGCAATAAGGAGCTTCGGCACCTGATTGAGGTCTCCGTGGTTTTATGG
GCTGTTGCTCTGACCAGCTGGATCAGTGACCGTCTGCTTTGCAGCTTCTGGCAGAGGATT
CATTTCTTCTATCTGCACAGCATCTGGCATGTGCTCATCAGCATCACCTTCCCTTATGGC
ATGGTCACCATGGCCTTGGTGGATGCCAACTATGAGATGCCAGGTGAAACCCTCAAAGTC
CGCTACTGGCCTCGGGACAGTTGGCCCGTGGGGCTGCCCTACGTGGAAATCCGGGGTGAT
GACAAGGACTGCTGA
Protein Properties
Number of Residues 264
Molecular Weight 31095.165
Theoretical pI 7.133
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Alkaline ceramidase 1
MPSIFAYQSSEVDWCESNFQYSELVAEFYNTFSNIPFFIFGPLMMLLMHPYAQKRSRYIY
VVWVLFMIIGLFSMYFHMTLSFLGQLLDEIAILWLLGSGYSIWMPRCYFPSFLGGNRSQF
IRLVFITTVVSTLLSFLRPTVNAYALNSIALHILYIVCQEYRKTSNKELRHLIEVSVVLW
AVALTSWISDRLLCSFWQRIHFFYLHSIWHVLISITFPYGMVTMALVDANYEMPGETLKV
RYWPRDSWPVGLPYVEIRGDDKDC
GenBank ID Protein 19070367
UniProtKB/Swiss-Prot ID Q8TDN7
UniProtKB/Swiss-Prot Entry Name ACER1_HUMAN
PDB IDs Not Available
GenBank Gene ID AF347024
GeneCard ID ACER1
GenAtlas ID ACER1
HGNC ID HGNC:18356
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Mao C, Xu R, Szulc ZM, Bielawski J, Becker KP, Bielawska A, Galadari SH, Hu W, Obeid LM: Cloning and characterization of a mouse endoplasmic reticulum alkaline ceramidase: an enzyme that preferentially regulates metabolism of very long chain ceramides. J Biol Chem. 2003 Aug 15;278(33):31184-91. Epub 2003 Jun 3. [PubMed:12783875 ]
  3. Houben E, Holleran WM, Yaginuma T, Mao C, Obeid LM, Rogiers V, Takagi Y, Elias PM, Uchida Y: Differentiation-associated expression of ceramidase isoforms in cultured keratinocytes and epidermis. J Lipid Res. 2006 May;47(5):1063-70. Epub 2006 Feb 13. [PubMed:16477081 ]