FADS3
entrez
3995
canonical
uniprot
Q9Y5Q0
canonical
ensembl
ENSG00000221968
resolver
ensp
ENSP00000278829
resolver
ensp
ENSP00000431533
resolver
ensp
ENSP00000639849
resolver
ensp
ENSP00000639857
resolver
enst
ENST00000278829
resolver
enst
ENST00000527697
resolver
enst
ENST00000969790
resolver
genesymbol
FADS3
resolver
genesymbol_syn
CYB5RP
resolver
hgnc
HGNC:3576
resolver
uniprot
E9PKP8
resolver
uniprot
O60426
resolver
uniprot_entry
E9PKP8_HUMAN
resolver
uniprot_entry
FADS3_HUMAN
resolver
uniprot_sec
O60426
resolver
amino_acid_sequence
MGGVGEPGPREGPAQPGAPLPTFCWEQIRAHDQPGDKWLVIERRVYDISRWAQRHPGGSRLIGHHGAEDATDAFRAFHQDLNFVRKFLQPLLIGELAPEEPSQDGPLNAQLVEDFRALHQAAEDMKLFDASPTFFAFLLGHILAMEVLAWLLIYLLGPGWVPSALAAFILAISQAQSWCLQHDLGHASIFKKSWWNHVAQKFVMGQLKGFSAHWWNFRHFQHHAKPNIFHKDPDVTVAPVFLLGESSVEYGKKKRRYLPYNQQHLYFFLIGPPLLTLVNFEVENLAYMLVCMQWADLLWAASFYARFFLSYLPFYGVPGVLLFFVAVRVLESHWFVWITQMNHIPKEIGHEKHRDWVSSQLAATCNVEPSLFTNWFSGHLNFQIEHHLFPRMPRHNYSRVAPLVKSLCAKHGLSYEVKPFLTALVDIVRSLKKSGDIWLDAYLHQ
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 (PubMed:31862735, PubMed:31916624). 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 (PubMed:31862735, PubMed:31916624, PubMed:37209771). Prefers SPH-containing ceramides (N-acylsphing-4-enines) as substrates (PubMed:31862735, PubMed:31916624, PubMed:37209771). Capable of metabolizing also the SPH in its free form (PubMed:31862735). SPD ceramides occur widely in mammalian tissues and cells (PubMed:31916624). 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 (PubMed:31916624). 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) (Probable). 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,which can be found in patients with DEGS1 mutations (PubMed:37209771). Its desaturase mechanism involves an electron transfer facilitated by cytochrome b5 (PubMed:37209771). 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 (By similarity). 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:0000269|PubMed:31862735, ECO:0000269|PubMed:31916624, ECO:0000269|PubMed:37209771, ECO:0000305|PubMed:31862735}.
uniprot
proteins
mass_dalton
51145
uniprot
proteins
pathway_participation
PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000305|PubMed:31862735, ECO:0000305|PubMed:31916624, ECO:0000305|PubMed:37209771}.; PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis. {ECO:0000250|UniProtKB:Q8K1P9}.
uniprot
proteins
protein_family
Fatty acid desaturase type 1 family
uniprot
proteins
pubmed
10860662
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16554811
uniprot
proteins
pubmed
19752397
uniprot
proteins
pubmed
31862735
uniprot
proteins
pubmed
31916624
uniprot
proteins
pubmed
37209771
uniprot
proteins
sequence_length
445
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:31916624}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 134..154; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 160..180; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 264..284; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 307..327; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins