Cers5
entrez
71949
canonical
uniprot
Q9D6K9
canonical
ensembl
ENSMUSG00000023021
resolver
ensp
ENSMUSP00000023762
resolver
genesymbol
Cers5
resolver
genesymbol_syn
Lass5
resolver
genesymbol_syn
Trh4
resolver
uniprot
Q3UL17
resolver
uniprot
Q80YB2
resolver
uniprot
Q8BPH6
resolver
uniprot
Q921T8
resolver
uniprot
Q924Z3
resolver
uniprot_entry
CERS5_MOUSE
resolver
uniprot_sec
Q3UL17
resolver
uniprot_sec
Q80YB2
resolver
uniprot_sec
Q8BPH6
resolver
uniprot_sec
Q921T8
resolver
uniprot_sec
Q924Z3
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by fumonisin B1. {ECO:0000269|PubMed:16100120}.
uniprot
proteins
amino_acid_sequence
MATAAAETLGLLWGWLWSESFWLPQNVSWADLEGPGDGYGYPRAQHVLSVFPLAVCIFSVRMLFERFIAKPCALRVGIKDSPVNKVEPNDTLEKVFVSVTKYPDEKRLKGLSKQLDWSVRKIQCWFRHRRNQDKPPTLTKFCESMWRFTYYLCIFCYGIRFLWSMPWFWDTRQCWYNYPYQPLSRELYYYYITQLAFYWSLMFSQFIDVKRKDFLMMFIHHMIGIMLTTFSYVNNMVRVGALIFCLHDFADPLLEAAKMANYARRERLCTTLFVIFGAAFIVSRLAIFPLWILNTTLFESWEIIGPYPSWWLFNALLLILQVLHAIWSYLIVQTASKALSRGKVSKDDRSDVESSSEEEDETTHKNNLSGSSSSNGANCMNGYMGGSHLAEEQGTCKATGNLHFRASPHLHSCD
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 fatty acyl-CoA to a sphingoid base, with high selectivity toward palmitoyl-CoA (hexadecanoyl-CoA; C16:0-CoA) (PubMed:12912983, PubMed:15823095, PubMed:16100120, PubMed:17609214, PubMed:17977534, PubMed:26853464, PubMed:38961186). 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 (By similarity) (PubMed:12912983, PubMed:15772421, PubMed:15823095, PubMed:17977534). 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:15823095). Plays a role in de novo ceramide synthesis and surfactant homeostasis in pulmonary epithelia (PubMed:15772421). {ECO:0000250|UniProtKB:Q8N5B7, ECO:0000269|PubMed:12912983, ECO:0000269|PubMed:15772421, ECO:0000269|PubMed:15823095, ECO:0000269|PubMed:16100120, ECO:0000269|PubMed:17609214, ECO:0000269|PubMed:17977534, ECO:0000269|PubMed:26853464, ECO:0000269|PubMed:38961186}.
uniprot
proteins
mass_dalton
48167
uniprot
proteins
mutagenesis
MUTAGEN 129..140; /note="Missing: Abolished ceramide synthase activity."; /evidence="ECO:0000269|PubMed:17609214"; MUTAGEN 134; /note="K->A: Abolished ceramide synthase activity."; /evidence="ECO:0000269|PubMed:17609214"; MUTAGEN 134; /note="K->R: Does not affect ceramide synthase activity."; /evidence="ECO:0000269|PubMed:17609214"; MUTAGEN 136..140; /note="Missing: Abolished ceramide synthase activity."; /evidence="ECO:0000269|PubMed:17609214"; MUTAGEN 140; /note="K->A: Abolished ceramide synthase activity."; /evidence="ECO:0000269|PubMed:17609214"; MUTAGEN 140; /note="K->R: Does not affect ceramide synthase activity."; /evidence="ECO:0000269|PubMed:17609214
uniprot
proteins
pathway_participation
PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000269|PubMed:12912983, ECO:0000269|PubMed:15823095, ECO:0000269|PubMed:16100120, ECO:0000269|PubMed:17609214, ECO:0000269|PubMed:17977534}.
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at the C-terminus by CK2. {ECO:0000250|UniProtKB:Q8N5B7}.
uniprot
proteins
protein_family
Sphingosine N-acyltransferase family
uniprot
proteins
pubmed
12912983
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15772421
uniprot
proteins
pubmed
15823095
uniprot
proteins
pubmed
16100120
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17609214
uniprot
proteins
pubmed
17977534
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
26853464
uniprot
proteins
pubmed
31150623
uniprot
proteins
pubmed
38961186
uniprot
proteins
sequence_length
414
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12912983}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 44..64; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 148..168; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 187..207; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 214..234; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 272..292; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 312..332; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins