CIDEC
entrez
63924
canonical
uniprot
Q96AQ7
canonical
ensembl
ENSG00000187288
resolver
ensp
ENSP00000338642
resolver
ensp
ENSP00000373328
resolver
ensp
ENSP00000392975
resolver
ensp
ENSP00000400649
resolver
ensp
ENSP00000483641
resolver
ensp
ENSP00000502377
resolver
ensp
ENSP00000504614
resolver
ensp
ENSP00000619841
resolver
ensp
ENSP00000619842
resolver
enst
ENST00000383817
resolver
genesymbol
CIDEC
resolver
genesymbol_syn
FSP27
resolver
hgnc
HGNC:24229
resolver
uniprot
A0A0A0MRY9
resolver
uniprot
C9JMN7
resolver
uniprot
Q67DW9
resolver
uniprot
Q9GZY9
resolver
uniprot_entry
A0A0A0MRY9_HUMAN
resolver
uniprot_entry
CIDEC_HUMAN
resolver
uniprot_sec
C9JMN7
resolver
uniprot_sec
Q67DW9
resolver
uniprot_sec
Q9GZY9
resolver
amino_acid_sequence
MEYAMKSLSLLYPKSLSRHVSVRTSVVTQQLLSEPSPKAPRARPCRVSTADRSVRKGIMAYSLEDLLLKVRDTLMLADKPFFLVLEEDGTTVETEEYFQALAGDTVFMVLQKGQKWQPPSEQGTRHPLSLSHKPAKKIDVARVTFDLYKLNPQDFIGCLNVKATFYDTYSLSYDLHCCGAKRIMKEAFRWALFSMQATGHVLLGTSCYLQQLLDATEEGQPPKGKASSLIPTCLKILQ
uniprot
proteins
disease_involvement
DISEASE: Note=In omental adipose tissue of obese patients matched for BMI, expression levels tend to correlate with insulin sensitivity. Expression is increased 2-3 fold in the group of patients with high insulin sensitivity, compared to the insulin-resistant group. This observation is consistent with the idea that triglyceride storage in adipocytes plays an important role in sequestering triglycerides and fatty acids away from the circulation and peripheral tissues, thus enhancing insulin sensitivity in liver and muscle. This effect is not significant in subcutaneous adipose tissue (PubMed:18509062). In subcutaneous adipose tissue of diabetic patients, tends to negatively correlate with body mass index and total fat mass, independently of insulin sensitivity (PubMed:18334488). {ECO:0000269|PubMed:18334488, ECO:0000269|PubMed:18509062}.; DISEASE: Lipodystrophy, familial partial, 5 (FPLD5) [MIM:615238]: An autosomal recessive form of lipodystrophy characterized by loss of subcutaneous adipose tissue affecting limb, femorogluteal and subcutaneous abdominal fat, preservation of visceral, neck and axilliary fat, hepatomegaly, hepatic steatosis and insulin-resistant diabetes. {ECO:0000269|PubMed:20049731}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Lipid transferase specifically expressed in white adipose tissue, which promotes unilocular lipid droplet formation by mediating lipid droplet fusion (PubMed:18334488, PubMed:19843876, PubMed:20049731, PubMed:23399566, PubMed:30361435). Lipid droplet fusion promotes their enlargement, restricting lipolysis and favoring lipid storage (PubMed:18334488, PubMed:19843876, PubMed:20049731, PubMed:23399566). Localizes on the lipid droplet surface, at focal contact sites between lipid droplets, and mediates atypical lipid droplet fusion by undergoing liquid-liquid phase separation (LLPS) and promoting directional net neutral lipid transfer from the smaller to larger lipid droplets (PubMed:18334488, PubMed:19843876, PubMed:20049731, PubMed:23399566). The transfer direction may be driven by the internal pressure difference between the contacting lipid droplet pair (PubMed:18334488, PubMed:19843876, PubMed:20049731, PubMed:23399566). Its role in neutral lipid transfer and lipid droplet enlargement is activated by the interaction with PLIN1 (PubMed:23399566). May also act as a CEBPB coactivator in the white adipose tissue to control the expression of a subset of CEBPB downstream target genes, including SOCS1, SOCS3, TGFB1, TGFBR1, ID2 and XDH (By similarity). When overexpressed in preadipocytes, induces apoptosis or increases cell susceptibility to apoptosis induced by serum deprivation or TGFB treatment (PubMed:12429024). {ECO:0000250|UniProtKB:P56198, ECO:0000269|PubMed:12429024, ECO:0000269|PubMed:18334488, ECO:0000269|PubMed:19843876, ECO:0000269|PubMed:20049731, ECO:0000269|PubMed:23399566, ECO:0000269|PubMed:30361435}.
uniprot
proteins
mass_dalton
26754
uniprot
proteins
mutagenesis
MUTAGEN 125; /note="R->A,Q: Does not affect ability to mediate lipid droplet fusion."; /evidence="ECO:0000269|PubMed:30361435
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated and targeted to proteasomal degradation, resulting in a short half-life (about 15 minutes in 3T3-L1 cells). Protein stability depends on triaclyglycerol synthesis, fatty acid availability and lipid droplet formation. {ECO:0000250|UniProtKB:P56198}.
uniprot
proteins
protein_family
CIDE family
uniprot
proteins
pubmed
12429024
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
18334488
uniprot
proteins
pubmed
18509062
uniprot
proteins
pubmed
19843876
uniprot
proteins
pubmed
20049731
uniprot
proteins
pubmed
23399566
uniprot
proteins
pubmed
30361435
uniprot
proteins
sequence_length
238
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:18334488, ECO:0000269|PubMed:23399566}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P56198}. Nucleus {ECO:0000250|UniProtKB:P56198}. Note=Diffuses quickly on lipid droplet surface, but becomes trapped and clustered at lipid droplet contact sites, thereby enabling its rapid enrichment at lipid droplet contact sites. {ECO:0000250|UniProtKB:P56198}.
uniprot
proteins