Cers2
entrez
76893
canonical
uniprot
Q924Z4
canonical
ensembl
ENSMUSG00000015714
resolver
ensp
ENSMUSP00000015858
resolver
ensp
ENSMUSP00000286168
resolver
ensp
ENSMUSP00000286177
resolver
enst
ENSMUST00000015858
resolver
genesymbol
Cers2
resolver
genesymbol_syn
Lass2
resolver
genesymbol_syn
Trh3
resolver
uniprot
Q3TXC5
resolver
uniprot
Q9DCN6
resolver
uniprot_entry
CERS2_MOUSE
resolver
uniprot_sec
Q3TXC5
resolver
uniprot_sec
Q9DCN6
resolver
activity_regulation
ACTIVITY REGULATION: Ceramide synthase activity is inhibited by sphingosine-1-phosphate. {ECO:0000250|UniProtKB:Q96G23}.
uniprot
proteins
amino_acid_sequence
MLQTLYDYFWWERLWLPVNLTWADLEDKDGRVYAKASDLYITLPLALLFLVIRYFFELYVATPLAALLNVKEKTRLRAPPNATLEHFYQTSGKQPKQVEVDLLSRQSGLSGRQVERWFRRRRNQDRPSLLKKFREASWRFTYYLIAFVAGMAVTVDKPWFYDLRKVWEGYPIQSIIPSQYWYYMIELSFYWSLLFSIASDVKRKDFKEQIIHHVATIILLCFSWFANYVRAGTLIMALHDASDYLLESAKMFNYAGWKNTCNNLFIVFAIVFIITRLVIMPFWILHCTMIYPLELYPAFFGYYFFNFMMAVLQMLHIFWAYFILRMAHKFITGKLIEDERSDREETESSEGEETAAGAGAKSRLLANGHPILNNNHPKND
uniprot
proteins
ec_number
2.3.1.24
uniprot
proteins
ec_number
2.3.1.297
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 very-long-chain fatty acyl-CoA (chain length C22-C27) (PubMed:15823095, PubMed:18165233, PubMed:20110363, PubMed:23275342, PubMed:38961186). N-acylates sphinganine and sphingosine bases to form dihydroceramides and ceramides in de novo synthesis and salvage pathways, respectively (PubMed:15823095, PubMed:18165233, PubMed:20110363, PubMed:23275342). Plays a non-redundant role in the synthesis of ceramides with very-long-chain fatty acids in kidney, liver and brain. Regulates the abundance of myelin-specific sphingolipids galactosylceramide and sulfatide that affects myelin sheath architecture and motor neuron functions (PubMed:19801672, PubMed:32279995). {ECO:0000269|PubMed:15823095, ECO:0000269|PubMed:18165233, ECO:0000269|PubMed:19801672, ECO:0000269|PubMed:20110363, ECO:0000269|PubMed:23275342, ECO:0000269|PubMed:32279995, ECO:0000269|PubMed:38961186}.
uniprot
proteins
mass_dalton
45024
uniprot
proteins
pathway_participation
PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000269|PubMed:15823095, ECO:0000269|PubMed:18165233, ECO:0000269|PubMed:20110363, ECO:0000269|PubMed:23275342}.
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}.; PTM: Phosphorylated at the C-terminus by CK2, leading to increase the ceramide synthase activity. {ECO:0000250|UniProtKB:Q96G23}.
uniprot
proteins
protein_family
Sphingosine N-acyltransferase family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15823095
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
18165233
uniprot
proteins
pubmed
19801672
uniprot
proteins
pubmed
20110363
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23275342
uniprot
proteins
pubmed
26620563
uniprot
proteins
pubmed
32279995
uniprot
proteins
pubmed
38961186
uniprot
proteins
sequence_length
380
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15823095}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 41..61; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 140..160; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 175..195; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 209..229; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 264..284; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 304..324; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins