CERS6
entrez
253782
canonical
uniprot
Q6ZMG9
canonical
ensembl
ENSG00000172292
resolver
ensp
ENSP00000306579
resolver
ensp
ENSP00000376453
resolver
genesymbol
CERS6
resolver
genesymbol_syn
LASS6
resolver
hgnc
HGNC:23826
resolver
uniprot
Q32M63
resolver
uniprot
Q8N617
resolver
uniprot_entry
CERS6_HUMAN
resolver
uniprot_sec
Q32M63
resolver
uniprot_sec
Q8N617
resolver
amino_acid_sequence
MAGILAWFWNERFWLPHNVTWADLKNTEEATFPQAEDLYLAFPLAFCIFMVRLIFERFVAKPCAIALNIQANGPQIAPPNAILEKVFTAITKHPDEKRLEGLSKQLDWDVRSIQRWFRQRRNQEKPSTLTRFCESMWRFSFYLYVFTYGVRFLKKTPWLWNTRHCWYNYPYQPLTTDLHYYYILELSFYWSLMFSQFTDIKRKDFGIMFLHHLVSIFLITFSYVNNMARVGTLVLCLHDSADALLEAAKMANYAKFQKMCDLLFVMFAVVFITTRLGIFPLWVLNTTLFESWEIVGPYPSWWVFNLLLLLVQGLNCFWSYLIVKIACKAVSRGKVSKDDRSDIESSSDEEDSEPPGKNPHTATTTNGTSGTNGYLLTGSCSMDD
uniprot
proteins
ec_number
2.3.1.-
uniprot
proteins
ec_number
2.3.1.24
uniprot
proteins
ec_number
2.3.1.291
uniprot
proteins
function
FUNCTION: Ceramide synthase that catalyzes the transfer of the fatty acyl chain from acyl-CoA to a sphingoid base, with high selectivity toward palmitoyl-CoA (hexadecanoyl-CoA; C16:0-CoA) (PubMed:17609214, PubMed:17977534, PubMed:23530041, PubMed:26887952, PubMed:31916624, PubMed:39528795). Can use different sphingoid bases as substrates for ceramide synthesis, such as sphinganine in de novo synthesis, and sphing-4E-enine (sphingosine), (4R)-hydroxysphinganine (phytosphingosine) or sphinga-4E,14Z-dienine in salvage pathways (PubMed:17977534, PubMed:23530041, PubMed:26887952, PubMed:31916624). Other fatty acyl-CoAs such as long-chain saturated stearoyl-CoA (octadecanoyl-CoA; C18:0-CoA), myristoyl-CoA (tetradecanoyl-CoA; C14:0-CoA), and monounsaturated oleoyl-CoA (9Z-octadecenoyl-CoA; C18:1-CoA) can also act as acyl donors, but with less efficiency than hexadecanoyl-CoA (PubMed:39528795). Ceramides generated by CERS6 play a role in inflammatory response (By similarity). Acts as a regulator of metabolism and hepatic lipid accumulation (By similarity). Under high fat diet, palmitoyl- (C16:0-) ceramides generated by CERS6 specifically bind the mitochondrial fission factor MFF, thereby promoting mitochondrial fragmentation and contributing to the development of obesity (By similarity). {ECO:0000250|UniProtKB:Q8C172, ECO:0000269|PubMed:17609214, ECO:0000269|PubMed:17977534, ECO:0000269|PubMed:23530041, ECO:0000269|PubMed:26887952, ECO:0000269|PubMed:31916624, ECO:0000269|PubMed:39528795}.
uniprot
proteins
mass_dalton
44890
uniprot
proteins
mutagenesis
MUTAGEN 131; /note="R->A: Abolished ceramide synthase activity."; /evidence="ECO:0000269|PubMed:17609214"; MUTAGEN 131; /note="R->K: Does not affect ceramide synthase activity."; /evidence="ECO:0000269|PubMed:17609214"; MUTAGEN 211; /note="H->A,N: Abolishes ceramide synthase activity."; /evidence="ECO:0000269|PubMed:39528795"; MUTAGEN 212; /note="H->A: Abolishes ceramide synthase activity."; /evidence="ECO:0000269|PubMed:39528795"; MUTAGEN 238; /note="H->A: Impairs ceramide synthase activity."; /evidence="ECO:0000269|PubMed:39528795"; MUTAGEN 275; /note="R->K: Impairs ceramide synthase activity."; /evidence="ECO:0000269|PubMed:39528795"; MUTAGEN 315; /note="N->A: Impairs ceramide synthase activity."; /evidence="ECO:0000269|PubMed:39528795"; MUTAGEN 341..347; /note="SDIESSS->ADIEAAA: Decreased phosphorylation."; /evidence="ECO:0000269|PubMed:26887952
uniprot
proteins
pathway_participation
PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000269|PubMed:17977534, ECO:0000269|PubMed:23530041, ECO:0000269|PubMed:26887952, ECO:0000269|PubMed:39528795}.
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at the C-terminus by CK2. {ECO:0000269|PubMed:26887952}.; PTM: Acetylated. Deacetylation by SIRT3 increases enzyme activity and promotes mitochondrial ceramide accumulation. {ECO:0000250|UniProtKB:Q8C172}.
uniprot
proteins
protein_family
Sphingosine N-acyltransferase family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
17609214
uniprot
proteins
pubmed
17977534
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
23530041
uniprot
proteins
pubmed
25295788
uniprot
proteins
pubmed
26887952
uniprot
proteins
pubmed
29632068
uniprot
proteins
pubmed
31916624
uniprot
proteins
pubmed
39528795
uniprot
proteins
sequence_length
384
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8C172}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8C172}.
uniprot
proteins
transmembrane_region
TRANSMEM 38..55; /note="Helical; Name=1"; /evidence="ECO:0000269|PubMed:39528795, ECO:0007744|PDB:8QZ6, ECO:0007744|PDB:8QZ7, ECO:0007744|PDB:9EOT"; TRANSMEM 132..153; /note="Helical; Name=2"; /evidence="ECO:0000269|PubMed:39528795, ECO:0007744|PDB:8QZ6, ECO:0007744|PDB:8QZ7, ECO:0007744|PDB:9EOT"; TRANSMEM 178..198; /note="Helical; Name=3"; /evidence="ECO:0000269|PubMed:39528795, ECO:0007744|PDB:8QZ6, ECO:0007744|PDB:8QZ7, ECO:0007744|PDB:9EOT"; TRANSMEM 206..224; /note="Helical; Name=4"; /evidence="ECO:0000269|PubMed:39528795, ECO:0007744|PDB:8QZ6, ECO:0007744|PDB:8QZ7, ECO:0007744|PDB:9EOT"; TRANSMEM 230..248; /note="Helical; Name=5"; /evidence="ECO:0000269|PubMed:39528795, ECO:0007744|PDB:8QZ6, ECO:0007744|PDB:8QZ7, ECO:0007744|PDB:9EOT"; TRANSMEM 262..284; /note="Helical; Name=6"; /evidence="ECO:0000269|PubMed:39528795, ECO:0007744|PDB:8QZ6, ECO:0007744|PDB:8QZ7, ECO:0007744|PDB:9EOT"; TRANSMEM 303..323; /note="Helical; Name=7"; /evidence="ECO:0000269|PubMed:39528795, ECO:0007744|PDB:8QZ6, ECO:0007744|PDB:8QZ7, ECO:0007744|PDB:9EOT
uniprot
proteins