Cidec
entrez
14311
canonical
uniprot
P56198
canonical
ensembl
ENSMUSG00000030278
resolver
ensp
ENSMUSP00000032416
resolver
ensp
ENSMUSP00000108712
resolver
ensp
ENSMUSP00000108714
resolver
enst
ENSMUST00000032416
resolver
enst
ENSMUST00000113089
resolver
enst
ENSMUST00000113091
resolver
genesymbol
Cidec
resolver
genesymbol_syn
Fsp27
resolver
uniprot
E9QMZ0
resolver
uniprot
Q499X5
resolver
uniprot
Q8BNV7
resolver
uniprot_entry
CIDEC_MOUSE
resolver
uniprot_entry
E9QMZ0_MOUSE
resolver
uniprot_sec
Q499X5
resolver
uniprot_sec
Q8BNV7
resolver
amino_acid_sequence
MDYAMKSLSLLYPRSLSRHVAVSTAVVTQQLVSKPSRETPRARPCRVSTADRKVRKGIMAHSLEDLLNKVQDILKLKDKPFSLVLEEDGTIVETEEYFQALAKDTMFMVLLKGQKWKPPSEQRKKRAQLALSQKPTKKIDVARVTFDLYKLNPQDFIGCLNVKATLYDTYSLSYDLHCYKAKRIVKEMLRWTLFSMQATGHMLLGTSSYMQQFLDATEEEQPAKAKPSSLLPACLKMLQ
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:22144693, PubMed:26733203, PubMed:30361435, PubMed:36477540). Lipid droplet fusion promotes their enlargement, restricting lipolysis and favoring lipid storage (PubMed:18334488, PubMed:18682832, PubMed:22144693, PubMed:26733203). 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:22144693). The transfer direction may be driven by the internal pressure difference between the contacting lipid droplet pair (PubMed:18334488, PubMed:22144693). Its role in neutral lipid transfer and lipid droplet enlargement is activated by the interaction with PLIN1 (PubMed:23481402). 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 (PubMed:22245780). When overexpressed in preadipocytes, induces apoptosis or increases cell susceptibility to apoptosis induced by serum deprivation or TGFB treatment (By similarity). {ECO:0000250|UniProtKB:Q96AQ7, ECO:0000269|PubMed:18334488, ECO:0000269|PubMed:18682832, ECO:0000269|PubMed:22144693, ECO:0000269|PubMed:22245780, ECO:0000269|PubMed:23481402, ECO:0000269|PubMed:26733203, ECO:0000269|PubMed:30361435, ECO:0000269|PubMed:36477540}.
uniprot
proteins
mass_dalton
27324
uniprot
proteins
mutagenesis
MUTAGEN 1..40; /note="Missing: Abolished ability to undergo liquid-liquid phase separation (LLPS)."; /evidence="ECO:0000269|PubMed:34508658"; MUTAGEN 46; /note="R->E: Abolishes CIDE-N/CIDE-N interaction between the 2 homodimer subunits."; /evidence="ECO:0000269|PubMed:23481402"; MUTAGEN 53; /note="K->A: Slightly inhibits interaction with PLIN1."; /evidence="ECO:0000269|PubMed:23481402"; MUTAGEN 55; /note="R->E: Abolishes CIDE-N/CIDE-N interaction between the 2 homodimer subunits."; /evidence="ECO:0000269|PubMed:23481402"; MUTAGEN 75; /note="K->A: Inhibits interaction with PLIN1; when associated with A-77."; /evidence="ECO:0000269|PubMed:23481402"; MUTAGEN 77; /note="K->A: Inhibits interaction with PLIN1; when associated with A-75."; /evidence="ECO:0000269|PubMed:23481402"; MUTAGEN 86..88; /note="EED->QQN: Abolishes CIDE-N/CIDE-N interaction between the 2 homodimer subunits and inhibits lipid droplet enlargement. No effect on homodimerization."; /evidence="ECO:0000269|PubMed:23481402, ECO:0000269|PubMed:34508658"; MUTAGEN 87..88; /note="ED->QN: Reduces CIDE-N/CIDE-N interaction between the 2 homodimer subunits and inhibits lipid droplet enlargement."; /evidence="ECO:0000269|PubMed:23481402"; MUTAGEN 112; /note="K->A: Slightly inhibits interaction with PLIN1; when associated with A-115."; /evidence="ECO:0000269|PubMed:23481402"; MUTAGEN 115; /note="K->A: Slightly inhibits interaction with PLIN1; when associated with A-112 or A-117."; /evidence="ECO:0000269|PubMed:23481402"; MUTAGEN 117; /note="K->A: Slightly inhibits interaction with PLIN1; when associated with A-115."; /evidence="ECO:0000269|PubMed:23481402"; MUTAGEN 121; /note="E->Q: Abolished ability to mediate lipid droplet fusion."; /evidence="ECO:0000269|PubMed:30361435"; MUTAGEN 122; /note="Q->A: Abolished ability to mediate lipid droplet fusion."; /evidence="ECO:0000269|PubMed:30361435"; MUTAGEN 123..126; /note="RKKR->AAAA: Abolished ability to bind acidic phospholipids and inhibit lipid droplet fusion."; /evidence="ECO:0000269|PubMed:30361435"; MUTAGEN 123; /note="R->A: Does not affect ability to mediate lipid droplet fusion."; /evidence="ECO:0000269|PubMed:30361435"; MUTAGEN 124; /note="K->A: Does not affect ability to mediate lipid droplet fusion."; /evidence="ECO:0000269|PubMed:30361435"; MUTAGEN 125..126; /note="KR->AA: Abolished ability to bind acidic phospholipids and inhibit lipid droplet fusion."; /evidence="ECO:0000269|PubMed:30361435"; MUTAGEN 125; /note="K->A: Does not affect ability to mediate lipid droplet fusion."; /evidence="ECO:0000269|PubMed:30361435"; MUTAGEN 126; /note="R->A: Does not affect ability to mediate lipid droplet fusion."; /evidence="ECO:0000269|PubMed:30361435"; MUTAGEN 128; /note="Q->A: Abolished ability to mediate lipid droplet fusion."; /evidence="ECO:0000269|PubMed:30361435"; MUTAGEN 130; /note="A->F,V: Abolished ability to mediate lipid droplet fusion."; /evidence="ECO:0000269|PubMed:30361435"; MUTAGEN 131; /note="L->A: Abolished ability to mediate lipid droplet fusion."; /evidence="ECO:0000269|PubMed:30361435"; MUTAGEN 132; /note="S->A: Abolished ability to mediate lipid droplet fusion."; /evidence="ECO:0000269|PubMed:30361435"; MUTAGEN 134; /note="K->A: Abolished ability to mediate lipid droplet fusion."; /evidence="ECO:0000269|PubMed:30361435"; MUTAGEN 182; /note="K->A: Abolishes lipid droplet enlargement activity, but not localization to lipid droplets, nor enrichement at contact sites; when associated with A-186 and A-190."; /evidence="ECO:0000269|PubMed:22144693"; MUTAGEN 186; /note="K->A: Abolishes lipid droplet enlargement activity, but not localization to lipid droplets, nor enrichement at contact sites; when associated with A-182 and A-190."; /evidence="ECO:0000269|PubMed:22144693"; MUTAGEN 190; /note="R->A: Abolishes lipid droplet enlargement activity, but not localization to lipid droplets, nor enrichement at contact sites; when associated with A-182 and A-186."; /evidence="ECO:0000269|PubMed:22144693"; MUTAGEN 224; /note="K->A: No effect on protein stability; when associated with A-226. Drastically increased protein stability and decreased ubiquitination; when associated with A-226 and A-236."; /evidence="ECO:0000269|PubMed:20089860"; MUTAGEN 226; /note="K->A: No effect on protein stability; when associated with A-226. Drastically increased protein stability and decreased ubiquitination; when associated with A-224 and A-236."; /evidence="ECO:0000269|PubMed:20089860"; MUTAGEN 236; /note="K->A: No effect on protein stability. Drastically increased protein stability and decreased ubiquitination; when associated with A-224 and A-226."; /evidence="ECO:0000269|PubMed:20089860
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) (PubMed:20089860). Protein stability depends on triaclyglycerol synthesis, fatty acid availability and lipid droplet formation (PubMed:20089860). {ECO:0000269|PubMed:20089860}.
uniprot
proteins
protein_family
CIDE family
uniprot
proteins
pubmed
12910269
uniprot
proteins
pubmed
1339452
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
18334488
uniprot
proteins
pubmed
18509062
uniprot
proteins
pubmed
18654663
uniprot
proteins
pubmed
18682832
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
20089860
uniprot
proteins
pubmed
22144693
uniprot
proteins
pubmed
22245780
uniprot
proteins
pubmed
23233732
uniprot
proteins
pubmed
23481402
uniprot
proteins
pubmed
24025675
uniprot
proteins
pubmed
26733203
uniprot
proteins
pubmed
30361435
uniprot
proteins
pubmed
34508658
uniprot
proteins
pubmed
36477540
uniprot
proteins
sequence_length
239
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:18334488, ECO:0000269|PubMed:18654663, ECO:0000269|PubMed:20089860, ECO:0000269|PubMed:22144693, ECO:0000269|PubMed:26733203, ECO:0000269|PubMed:30361435, ECO:0000269|PubMed:34508658}. Endoplasmic reticulum {ECO:0000269|PubMed:20089860}. Nucleus {ECO:0000269|PubMed:22245780}. 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:0000269|PubMed:22144693, ECO:0000269|PubMed:26733203, ECO:0000269|PubMed:34508658}.
uniprot
proteins