CERS5
entrez
91012
canonical
uniprot
Q8N5B7
canonical
ensembl
ENSG00000139624
resolver
ensp
ENSP00000325485
resolver
ensp
ENSP00000389050
resolver
ensp
ENSP00000667057
resolver
ensp
ENSP00000701413
resolver
ensp
ENSP00000701414
resolver
genesymbol
CERS5
resolver
genesymbol_syn
LASS5
resolver
hgnc
HGNC:23749
resolver
uniprot
B4DV54
resolver
uniprot_entry
CERS5_HUMAN
resolver
uniprot_sec
B4DV54
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by fumonisin B1. {ECO:0000269|PubMed:16951403}.
uniprot
proteins
amino_acid_sequence
MATAAQGPLSLLWGWLWSERFWLPENVSWADLEGPADGYGYPRGRHILSVFPLAAGIFFVRLLFERFIAKPCALCIGIEDSGPYQAQPNAILEKVFISITKYPDKKRLEGLSKQLDWNVRKIQCWFRHRRNQDKPPTLTKFCESMWRFTFYLCIFCYGIRFLWSSPWFWDIRQCWHNYPFQPLSSGLYHYYIMELAFYWSLMFSQFTDIKRKDFLIMFVHHLVTIGLISFSYINNMVRVGTLIMCLHDVSDFLLEAAKLANYAKYQRLCDTLFVIFSAVFMVTRLGIYPFWILNTTLFESWEIIGPYASWWLLNGLLLTLQLLHVIWSYLIARIALKALIRGKVSKDDRSDVESSSEEEDVTTCTKSPCDSSSSNGANRVNGHMGGSYWAEE
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:16951403, PubMed:18541923, PubMed:22144673, PubMed:22661289, PubMed:23530041, PubMed:26887952, PubMed:29632068, PubMed:31916624). 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: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 (By similarity). Plays a role in de novo ceramide synthesis and surfactant homeostasis in pulmonary epithelia (By similarity). {ECO:0000250|UniProtKB:Q9D6K9, ECO:0000269|PubMed:16951403, ECO:0000269|PubMed:18541923, ECO:0000269|PubMed:22144673, ECO:0000269|PubMed:22661289, ECO:0000269|PubMed:23530041, ECO:0000269|PubMed:26887952, ECO:0000269|PubMed:29632068, ECO:0000269|PubMed:31916624}.
uniprot
proteins
mass_dalton
45752
uniprot
proteins
mutagenesis
MUTAGEN 26; /note="N->Q: Reduced N-glycosylation."; /evidence="ECO:0000269|PubMed:29632068"; MUTAGEN 153..165; /note="CIFCYGIRFLWSS->IAGMAVIVD: Does not affect specificity toward acyl donor."; /evidence="ECO:0000269|PubMed:29632068"; MUTAGEN 220; /note="H->D: Strongly decreased ceramide synthase activity."; /evidence="ECO:0000269|PubMed:16951403"; MUTAGEN 231; /note="S->A: Does not affect ceramide synthase activity."; /evidence="ECO:0000269|PubMed:16951403"; MUTAGEN 254; /note="L->E: Strongly decreased ceramide synthase activity."; /evidence="ECO:0000269|PubMed:16951403"; MUTAGEN 254; /note="L->M: Does not affect ceramide synthase activity."; /evidence="ECO:0000269|PubMed:16951403"; MUTAGEN 299..309; /note="ESWEIIGPYAS->YPLELYPAFFG: Altered specificity toward acyl donor; generates C22-C24 ceramides instead of C16-ceramide."; /evidence="ECO:0000269|PubMed:29632068"; MUTAGEN 350..356; /note="SDVESSS->ADVEAAA: Decreased phosphorylation."; /evidence="ECO:0000269|PubMed:26887952
uniprot
proteins
pathway_participation
PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000269|PubMed:18541923, ECO:0000269|PubMed:22144673, ECO:0000269|PubMed:22661289, ECO:0000269|PubMed:23530041, ECO:0000269|PubMed:26887952}.
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at the C-terminus by CK2. {ECO:0000269|PubMed:26887952}.
uniprot
proteins
protein_family
Sphingosine N-acyltransferase family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
16951403
uniprot
proteins
pubmed
18541923
uniprot
proteins
pubmed
22144673
uniprot
proteins
pubmed
22661289
uniprot
proteins
pubmed
23530041
uniprot
proteins
pubmed
26887952
uniprot
proteins
pubmed
29632068
uniprot
proteins
pubmed
31916624
uniprot
proteins
pubmed
38961186
uniprot
proteins
sequence_length
392
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9D6K9}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 47..67; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 148..168; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 183..203; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 214..234; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 272..292; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 311..331; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins