Elovl3
entrez
12686
canonical
uniprot
O35949
canonical
ensembl
ENSMUSG00000038754
resolver
ensp
ENSMUSP00000036357
resolver
ensp
ENSMUSP00000157465
resolver
enst
ENSMUST00000043739
resolver
enst
ENSMUST00000237098
resolver
genesymbol
Elovl3
resolver
genesymbol_syn
Cig30
resolver
uniprot
A0A498WFQ4
resolver
uniprot_entry
A0A498WFQ4_MOUSE
resolver
uniprot_entry
ELOV3_MOUSE
resolver
amino_acid_sequence
MDTSMNFSRGLKMDLMQPYDFETFQDLRPFLEEYWVSSFLIVVVYLLLIVVGQTYMRTRKSFSLQRPLILWSFFLAIFSILGTLRMWKFMATVMFTVGLKQTVCFAIYTDDAVVRFWSFLFLLSKVVELGDTAFIILRKRPLIFVHWYHHSTVLLFTSFGYKNKVPSGGWFMTMNFGVHSVMYTYYTMKAAKLKHPNLLPMVITSLQILQMVLGTIFGILNYIWRQEKGCHTTTEHFFWSFMLYGTYFILFAHFFHRAYLRPKGKVASKSQ
uniprot
proteins
ec_number
2.3.1.199
uniprot
proteins
function
FUNCTION: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that exhibits activity toward saturated and unsaturated acyl-CoA substrates with higher activity toward C18 acyl-CoAs, especially C18:0 acyl-CoAs. May participate in the production of saturated and monounsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. Participates in the formation of certain VLCFA and triglycerides in certain cells of the hair follicles and the sebaceous glands, required for skin barrier function. Critical enzyme for lipid accumulation and metabolic activity in brown adipocytes during the early phase of the tissue recruitment. Plays a role in lipid storage and in resistance to diet-induced obesity. {ECO:0000255|HAMAP-Rule:MF_03203, ECO:0000269|PubMed:10791983, ECO:0000269|PubMed:14581464, ECO:0000269|PubMed:16326704, ECO:0000269|PubMed:20605947}.
uniprot
proteins
mass_dalton
32060
uniprot
proteins
pathway_participation
PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03203}.
uniprot
proteins
post_translational_modification
PTM: N-Glycosylated. {ECO:0000255|HAMAP-Rule:MF_03203, ECO:0000269|PubMed:10429212}.
uniprot
proteins
protein_family
ELO family
uniprot
proteins
protein_family
ELOVL3 subfamily
uniprot
proteins
pubmed
10429212
uniprot
proteins
pubmed
10473596
uniprot
proteins
pubmed
10791983
uniprot
proteins
pubmed
14581464
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16326704
uniprot
proteins
pubmed
20605947
uniprot
proteins
pubmed
9395518
uniprot
proteins
sequence_length
271
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03203, ECO:0000269|PubMed:10429212}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03203}.
uniprot
proteins
transmembrane_region
TRANSMEM 30..50; /note="Helical"; /evidence="ECO:0000255|HAMAP-Rule:MF_03203"; TRANSMEM 67..87; /note="Helical"; /evidence="ECO:0000255|HAMAP-Rule:MF_03203"; TRANSMEM 116..136; /note="Helical"; /evidence="ECO:0000255|HAMAP-Rule:MF_03203"; TRANSMEM 141..161; /note="Helical"; /evidence="ECO:0000255|HAMAP-Rule:MF_03203"; TRANSMEM 165..187; /note="Helical"; /evidence="ECO:0000255|HAMAP-Rule:MF_03203"; TRANSMEM 199..219; /note="Helical"; /evidence="ECO:0000255|HAMAP-Rule:MF_03203"; TRANSMEM 236..256; /note="Helical"; /evidence="ECO:0000255|HAMAP-Rule:MF_03203
uniprot
proteins