Cers1
entrez
93898
canonical
uniprot
P27545
canonical
ensembl
ENSMUSG00000087408
resolver
ensp
ENSMUSP00000120598
resolver
enst
ENSMUST00000140239
resolver
genesymbol
Cers1
resolver
genesymbol_syn
Lass1
resolver
genesymbol_syn
Uog-1
resolver
genesymbol_syn
Uog1
resolver
uniprot
A2RT05
resolver
uniprot_entry
A2RT05_MOUSE
resolver
uniprot_entry
CERS1_MOUSE
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by fumonisin B1. {ECO:0000269|PubMed:16951403}.
uniprot
proteins
amino_acid_sequence
MAAAAATPRLEAPEPMPSYAQMLQRSWASALAAAQGCGDCGWGLARRGLAEHAHLAAPELLLAVLCALGWTALRWAATTHIFRPLAKRCRLQPRDAARLPESAWKLLFYLACWSYCAYLLLGTSYPFFHDPPSVFYDWRSGMAVPWDIAVAYLLQGSFYCHSIYATVYMDSWRKDSVVMLVHHVVTLLLIASSYAFRYHNVGLLVFFLHDVSDVQLEFTKLNIYFKARGGAYHRLHGLVANLGCLSFCFCWFWFRLYWFPLKVLYATCHCSLQSVPDIPYYFFFNILLLLLMVMNIYWFLYIVAFAAKVLTGQMRELEDLREYDTLEAQTAKPCKAEKPLRNGLVKDKLF
uniprot
proteins
disease_involvement
DISEASE: Note=Defects in CERS1 cause cerebellar ataxia and Purkinje cell degeneration. Two mouse strains flincher (fln) and toppler (to) carry spontaneous recessive mutations at the TLC domain of CERS1, resulting in complete loss of the catalytic activity associated with a reduction in sphingolipid biosynthesis and accumulation of lipofuscin in many brain regions. {ECO:0000269|PubMed:21625621}.
uniprot
proteins
ec_number
2.3.1.24
uniprot
proteins
ec_number
2.3.1.299
uniprot
proteins
function
FUNCTION: Ceramide synthase that catalyzes the transfer of the acyl chain from acyl-CoA to a sphingoid base, with high selectivity toward stearoyl-CoA (octadecanoyl-CoA; C18:0-CoA). N-acylates sphinganine and sphingosine bases to form dihydroceramides and ceramides in de novo synthesis and salvage pathways, respectively (PubMed:12105227, PubMed:16951403, PubMed:17977534, PubMed:18541923, PubMed:30605666). Plays a predominant role in skeletal muscle in regulating C18 ceramide and dihydroceramide levels with an impact on whole-body glucose metabolism and insulin sensitivity. Protects from diet-induced obesity by suppressing the uptake of glucose in multiple organs in a FGF21-dependent way (PubMed:30605666). Generates C18 ceramides in the brain, playing a critical role in cerebellar development and Purkinje cell function (PubMed:21625621). In response to cellular stress mediates mitophagy, a known defense mechanism against cell transformation and aging. Upon mitochondria fission, generates C18 ceramides that anchor lipidated MAP1LC3B/LC3B-II autophagolysosomes to outer mitochondrial membranes to eliminate damaged mitochondria (By similarity). {ECO:0000250|UniProtKB:P27544, ECO:0000269|PubMed:12105227, ECO:0000269|PubMed:16951403, ECO:0000269|PubMed:17977534, ECO:0000269|PubMed:18541923, ECO:0000269|PubMed:21625621, ECO:0000269|PubMed:30605666}.
uniprot
proteins
mass_dalton
40100
uniprot
proteins
mutagenesis
MUTAGEN 182; /note="H->D: Decreased ceramide synthase activity."; /evidence="ECO:0000269|PubMed:16951403"; MUTAGEN 183; /note="H->D: Decreased ceramide synthase activity."; /evidence="ECO:0000269|PubMed:16951403"; MUTAGEN 189; /note="L->E: Decreased ceramide synthase activity."; /evidence="ECO:0000269|PubMed:16951403"; MUTAGEN 193; /note="S->A: Does not affect ceramide synthase activity."; /evidence="ECO:0000269|PubMed:16951403"; MUTAGEN 210; /note="D->N: Decreased ceramide synthase activity."; /evidence="ECO:0000269|PubMed:16951403"; MUTAGEN 213; /note="D->N: Decreased ceramide synthase activity."; /evidence="ECO:0000269|PubMed:16951403"; MUTAGEN 216; /note="L->E: Decreased ceramide synthase activity."; /evidence="ECO:0000269|PubMed:16951403"; MUTAGEN 220; /note="K->L: Does not affect ceramide synthase activity."; /evidence="ECO:0000269|PubMed:16951403
uniprot
proteins
pathway_participation
PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000269|PubMed:12105227, ECO:0000269|PubMed:16951403, ECO:0000269|PubMed:17977534, ECO:0000269|PubMed:18541923, ECO:0000269|PubMed:30605666}.
uniprot
proteins
post_translational_modification
PTM: Acetylated (PubMed:26620563). Deacetylation by SIRT3 increases enzyme activity and promotes mitochondrial ceramide accumulation (PubMed:26620563). {ECO:0000269|PubMed:26620563}.
uniprot
proteins
protein_family
Sphingosine N-acyltransferase family
uniprot
proteins
pubmed
12105227
uniprot
proteins
pubmed
15823095
uniprot
proteins
pubmed
16951403
uniprot
proteins
pubmed
17977534
uniprot
proteins
pubmed
18541923
uniprot
proteins
pubmed
2034669
uniprot
proteins
pubmed
21625621
uniprot
proteins
pubmed
26620563
uniprot
proteins
pubmed
30605666
uniprot
proteins
sequence_length
350
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P27544}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 53..73; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 103..123; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 148..168; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 176..196; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 239..259; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 287..307; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins