Fads3
entrez
60527
canonical
uniprot
Q9JJE7
canonical
ensembl
ENSMUSG00000024664
resolver
ensp
ENSMUSP00000111659
resolver
enst
ENSMUST00000115995
resolver
genesymbol
Fads3
resolver
uniprot
Q3T9H9
resolver
uniprot
Q7TND7
resolver
uniprot
Q8C4Y5
resolver
uniprot
Q8CDZ4
resolver
uniprot_entry
FADS3_MOUSE
resolver
uniprot_entry
Q3T9H9_MOUSE
resolver
uniprot_sec
Q7TND7
resolver
uniprot_sec
Q8C4Y5
resolver
uniprot_sec
Q8CDZ4
resolver
amino_acid_sequence
MGGVGEPGGGPGPREGPAPLGAPLPIFRWEQIRQHDLPGDKWLVIERRVYDISRWAQRHPGGSRLIGHHGAEDATDAFHAFHQDLHFVRKFLKPLLIGELAPEEPSQDGAQNAQLIEDFRALRQAAEDMKLFEADTTFFALLLGHILAMELLAWLIIYLLGPGWVSSILAALILAISQAQCWCLQHDLGHASIFTKSRWNHVAQQFVMGQLKGFSAHWWNFRHFQHHAKPNIFHKDPDVTVAPVFLLGESSVEYGKKKRRYLPYNHQHLYFFLIGPPLLTLVNFEVENLAYMLVCMQWTDLLWAASFYSRFFLSYSPFYGATGTLLLFVAVRVLESHWFVWITQMNHIPKEIGHEKHRDWASSQLAATCNVEPSLFIDWFSGHLNFQIEHHLFPTMPRHNYRRVAPLVKAFCAKHGLHYEVKPFLTALVDIIGSLKKSGDIWLDAYLHQ
uniprot
proteins
ec_number
1.14.19.-
uniprot
proteins
function
FUNCTION: Mammals have different sphingoid bases that differ in their length and/or pattern of desaturation and hydroxyl groups. The predominant sphingoid base that comprises mammalian ceramides is sphing-4-enine (sphingosine or SPH) which has a trans (E) desaturation at carbon 4. FADS3 is a desaturase that introduces a cis (Z) double bond between carbon 14 and carbon 15 of the sphingoid base (also known as long chain base, LCB), producing LCBs such as sphinga-4,14-dienine (SPD, d18:2(4E,14Z)) from SPH. Prefers SPH-containing ceramides (N-acylsphing-4-enines) as substrates. Capable of metabolizing also the SPH in its free form. SPD ceramides occur widely in mammalian tissues and cells. Due to their unusual structure containing a cis double bond, SPD ceramides may have an opposite, negative role in lipid microdomain formation relative to conventional ceramides. Could be involved in the detoxification of 1-deoxy sphingolipids, by desaturating the cytotoxic 1-deoxysphinganine (1-deoxySA, m18:0), produced under pathological conditions, to 1-deoxysphingenine (1-deoxysphingosine, 1-deoxySO, m18:1). Although prefers SPH-containing ceramides (N-acylsphing-4-enines) as substrates, it also exhibits activity toward dihydrosphingosine-containing CERs (N-acylsphinganines) and produces 14Z-SPH-containing sphingolipids. Its desaturase mechanism involves an electron transfer facilitated by cytochrome b5 (By similarity). FADS3 also acts as a methyl-end fatty acyl coenzyme A (CoA) desaturase that introduces a cis double bond between the preexisting double bond and the terminal methyl group of the fatty acyl chain. Desaturates (11E)-octadecenoate (trans-vaccenoate, the predominant trans fatty acid in human milk) at carbon 13 to generate (11E,13Z)-octadecadienoate (also known as conjugated linoleic acid 11E,13Z-CLA) (By similarity). {ECO:0000250|UniProtKB:Q8K1P9, ECO:0000250|UniProtKB:Q9Y5Q0}.
uniprot
proteins
mass_dalton
51469
uniprot
proteins
pathway_participation
PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis. {ECO:0000250|UniProtKB:Q8K1P9}.; PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000250|UniProtKB:Q9Y5Q0}.
uniprot
proteins
protein_family
Fatty acid desaturase type 1 family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
19752397
uniprot
proteins
sequence_length
449
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Y5Q0}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 135..155; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 164..184; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 269..289; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 311..331; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins