| IED ID | IndEnz0005001237 |
| Enzyme Type ID | lipase001237 |
| Protein Name |
Cell death activator CIDE-3 Cell death-inducing DFFA-like effector protein C Fat-specific protein FSP27 homolog |
| Gene Name | CIDEC FSP27 |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MEYAMKSLSLLYPKSLSRHVSVRTSVVTQQLLSEPSPKAPRARPCRVSTADRSVRKGIMAYSLEDLLLKVRDTLMLADKPFFLVLEEDGTTVETEEYFQALAGDTVFMVLQKGQKWQPPSEQGTRHPLSLSHKPAKKIDVARVTFDLYKLNPQDFIGCLNVKATFYDTYSLSYDLHCCGAKRIMKEAFRWALFSMQATGHVLLGTSCYLQQLLDATEEGQPPKGKASSLIPTCLKILQ |
| Enzyme Length | 238 |
| Uniprot Accession Number | Q96AQ7 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a triacyl-sn-glycerol(in) = a triacyl-sn-glycerol(out); Xref=Rhea:RHEA:39011, ChEBI:CHEBI:64615; Evidence={ECO:0000250|UniProtKB:P56198}; |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Binds to lipid droplets and regulates their enlargement, thereby restricting lipolysis and favoring storage. At focal contact sites between lipid droplets, promotes directional net neutral lipid transfer from the smaller to larger lipid droplets. The transfer direction may be driven by the internal pressure difference between the contacting lipid droplet pair. Its role in neutral lipid transfer and lipid droplet enlargement is activated by the interaction with PLIN1. May 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. When overexpressed in preadipocytes, induces apoptosis or increases cell susceptibility to apoptosis induced by serum deprivation or TGFB treatment. As mature adipocytes, that express high CIDEC levels, are quite resistant to apoptotic stimuli, the physiological significance of its role in apoptosis is unclear. May play a role in the modulation of the response to osmotic stress by preventing NFAT5 to translocate into the nucleus and activate its target genes expression. {ECO:0000269|PubMed:12429024, ECO:0000269|PubMed:18334488, ECO:0000269|PubMed:19843876, ECO:0000269|PubMed:20049731, ECO:0000269|PubMed:23399566}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (4); Chain (1); Domain (1); Sequence conflict (1) |
| Keywords | Activator;Alternative splicing;Apoptosis;Endoplasmic reticulum;Lipid droplet;Lipid transport;Nucleus;Reference proteome;Transcription;Transcription regulation;Transport;Ubl conjugation |
| Interact With | Q9BS75; A6NJ78-4; Q15466; Q7Z6I5; Q6NVU6; B2RXF5 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Endoplasmic reticulum. Lipid droplet. 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. |
| Modified Residue | |
| Post Translational Modification | PTM: Ubiquitinated and targeted to proteasomal degradation, resulting in a short half-life. Protein stability depends on triaclyglycerol synthesis, fatty acid availability and lipid droplet formation (By similarity). {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 18702959; 19661960; 20154362; 21636835; 21666694; 21865223; 22262056; 23220584; 23233732; 23475172; 24025675; 24126816; 24627478; 24742676; 25210844; 26099526; 26322308; 26367078; 28415694; 29080839; 29486327; 30139016; 31433737; 31560287; |
| Motif | |
| Gene Encoded By | |
| Mass | 26,754 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:39011 |
| Cross Reference Brenda |