CIDEC_RAT
ID CIDEC_RAT Reviewed; 238 AA.
AC Q5XI33;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Cell death activator CIDE-3;
DE AltName: Full=Cell death-inducing DFFA-like effector protein C;
DE AltName: Full=Fat-specific protein FSP27;
GN Name=Cidec; Synonyms=Fsp27;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP FUNCTION IN OSMOTIC STRESS, INTERACTION WITH NFAT5, AND INDUCTION.
RX PubMed=23233732; DOI=10.1194/jlr.m033365;
RA Ueno M., Shen W.J., Patel S., Greenberg A.S., Azhar S., Kraemer F.B.;
RT "Fat-specific protein 27 modulates nuclear factor of activated T cells 5
RT and the cellular response to stress.";
RL J. Lipid Res. 54:734-743(2013).
CC -!- FUNCTION: Binds to lipid droplets and regulates their enlargement,
CC thereby restricting lipolysis and favoring storage. At focal contact
CC sites between lipid droplets, promotes directional net neutral lipid
CC transfer from the smaller to larger lipid droplets. The transfer
CC direction may be driven by the internal pressure difference between the
CC contacting lipid droplet pair. Its role in neutral lipid transfer and
CC lipid droplet enlargement is activated by the interaction with PLIN1.
CC May act as a CEBPB coactivator in the white adipose tissue to control
CC the expression of a subset of CEBPB downstream target genes, including
CC SOCS1, SOCS3, TGFB1, TGFBR1, ID2 and XDH. When overexpressed in
CC preadipocytes, induces apoptosis or increases cell susceptibility to
CC apoptosis induced by serum deprivation or TGFB treatment. The
CC physiological significance of its role in apoptosis is unclear (By
CC similarity). May play a role in the modulation of the response to
CC osmotic stress by preventing NFAT5 to translocate into the nucleus and
CC activate its target genes expression. {ECO:0000250,
CC ECO:0000269|PubMed:23233732}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a triacyl-sn-glycerol(in) = a triacyl-sn-glycerol(out);
CC Xref=Rhea:RHEA:39011, ChEBI:CHEBI:64615;
CC Evidence={ECO:0000250|UniProtKB:P56198};
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with CEBPB (By
CC similarity). Interacts with CIDEA (By similarity). Interacts with PLIN1
CC (By similarity). Interacts with NFAT5; this interaction is direct and
CC retains NFAT5 in the cytoplasm. {ECO:0000250,
CC ECO:0000269|PubMed:23233732}.
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000250}. Endoplasmic
CC reticulum {ECO:0000250}. Nucleus {ECO:0000250}. Note=Diffuses quickly
CC on lipid droplet surface, but becomes trapped and clustered at lipid
CC droplet contact sites, thereby enabling its rapid enrichment at lipid
CC droplet contact sites. {ECO:0000250}.
CC -!- INDUCTION: Down-regulated upon hypertonic conditions.
CC {ECO:0000269|PubMed:23233732}.
CC -!- DOMAIN: The CIDE-N domain is involved in homodimerization which is
CC crucial for its function in promoting lipid exchange and transfer.
CC {ECO:0000250}.
CC -!- PTM: Ubiquitinated and targeted to proteasomal degradation, resulting
CC in a short half-life (about 15 minutes in 3T3-L1 cells). Protein
CC stability depends on triaclyglycerol synthesis, fatty acid availability
CC and lipid droplet formation (By similarity). {ECO:0000250}.
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DR EMBL; BC083860; AAH83860.1; -; mRNA.
DR RefSeq; NP_001019504.2; NM_001024333.2.
DR RefSeq; NP_001231726.1; NM_001244797.1.
DR RefSeq; NP_001231727.1; NM_001244798.1.
DR AlphaFoldDB; Q5XI33; -.
DR SMR; Q5XI33; -.
DR STRING; 10116.ENSRNOP00000012136; -.
DR iPTMnet; Q5XI33; -.
DR PhosphoSitePlus; Q5XI33; -.
DR PaxDb; Q5XI33; -.
DR PRIDE; Q5XI33; -.
DR Ensembl; ENSRNOT00000012136; ENSRNOP00000012136; ENSRNOG00000009153.
DR GeneID; 500292; -.
DR KEGG; rno:500292; -.
DR UCSC; RGD:1562113; rat.
DR CTD; 63924; -.
DR RGD; 1562113; Cidec.
DR eggNOG; ENOG502QU28; Eukaryota.
DR GeneTree; ENSGT00390000018596; -.
DR HOGENOM; CLU_090011_1_0_1; -.
DR InParanoid; Q5XI33; -.
DR OrthoDB; 1421916at2759; -.
DR PhylomeDB; Q5XI33; -.
DR TreeFam; TF334321; -.
DR Reactome; R-RNO-8964572; Lipid particle organization.
DR PRO; PR:Q5XI33; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000009153; Expressed in liver and 15 other tissues.
DR ExpressionAtlas; Q5XI33; baseline and differential.
DR Genevisible; Q5XI33; RN.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0006915; P:apoptotic process; ISO:RGD.
DR GO; GO:0097194; P:execution phase of apoptosis; ISO:RGD.
DR GO; GO:0034389; P:lipid droplet organization; ISO:RGD.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
DR InterPro; IPR003508; CIDE-N_dom.
DR Pfam; PF02017; CIDE-N; 1.
DR SMART; SM00266; CAD; 1.
DR PROSITE; PS51135; CIDE_N; 1.
PE 1: Evidence at protein level;
KW Activator; Apoptosis; Endoplasmic reticulum; Lipid droplet;
KW Lipid transport; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Transport; Ubl conjugation.
FT CHAIN 1..238
FT /note="Cell death activator CIDE-3"
FT /id="PRO_0000419721"
FT DOMAIN 41..118
FT /note="CIDE-N"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00447"
SQ SEQUENCE 238 AA; 27214 MW; E6489A38F1CA5277 CRC64;
MDYAMKSLSL LYPRSLSRHV AVSTAVVTQQ LVSEPSRETP RARPCRVSTA DRKVRKGIMA
HSLEDLLGKV QDILKLKDKP FSLVLEEDGT IVETEEYFQA LPRDTVFMVL QKGQKWKSPS
EQRKKKAQLS LSQKPTKKID VARVTFDLYK LNPQDFIGCL NVKATLYDTY SLSYDLHCYR
AKRIVKEMLR WTLFSMQATG HMLLGTSSYM QQFLDATEEE QPSKAKASLL PACLKMLQ
