CIDEC_BOVIN
ID CIDEC_BOVIN Reviewed; 222 AA.
AC F1MN90; Q1LZ93;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 58.
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 homolog;
GN Name=CIDEC; Synonyms=FSP27;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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. May
CC play a role in the modulation of the response to osmotic stress by
CC preventing NFAT5 to translocate into the nucleus and activate its
CC target genes expression (By similarity). {ECO:0000250}.
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. Interacts with CEBPB. Interacts with CIDEA.
CC Interacts with PLIN1. Interacts with NFAT5; this interaction is direct
CC and retains NFAT5 in the cytoplasm. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000250}. Nucleus
CC {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Note=Diffuses
CC quickly on lipid droplet surface, but becomes trapped and clustered at
CC lipid droplet contact sites, thereby enabling its rapid enrichment at
CC lipid droplet contact sites. {ECO:0000250}.
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. Protein stability depends on triaclyglycerol
CC synthesis, fatty acid availability and lipid droplet formation (By
CC similarity). {ECO:0000250}.
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DR EMBL; DAAA02053757; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC116135; AAI16136.1; -; mRNA.
DR RefSeq; NP_001069499.1; NM_001076031.1.
DR AlphaFoldDB; F1MN90; -.
DR SMR; F1MN90; -.
DR STRING; 9913.ENSBTAP00000010479; -.
DR PaxDb; F1MN90; -.
DR PRIDE; F1MN90; -.
DR GeneID; 534607; -.
DR KEGG; bta:534607; -.
DR CTD; 63924; -.
DR eggNOG; ENOG502QU28; Eukaryota.
DR HOGENOM; CLU_090011_0_0_1; -.
DR InParanoid; F1MN90; -.
DR OrthoDB; 1421916at2759; -.
DR TreeFam; TF334321; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005829; C:cytosol; ISS:AgBase.
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:0097194; P:execution phase of apoptosis; ISS:AgBase.
DR GO; GO:0034389; P:lipid droplet organization; ISS:AgBase.
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 2: Evidence at transcript level;
KW Activator; Apoptosis; Endoplasmic reticulum; Lipid droplet;
KW Lipid transport; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Transport; Ubl conjugation.
FT CHAIN 1..222
FT /note="Cell death activator CIDE-3"
FT /id="PRO_0000419720"
FT DOMAIN 26..103
FT /note="CIDE-N"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00447"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 56
FT /note="R -> Q (in Ref. 2; AAI16136)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="K -> R (in Ref. 2; AAI16136)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="R -> Q (in Ref. 2; AAI16136)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 222 AA; 25056 MW; 2A89A175C92A88DE CRC64;
MAMYTAVSTS VVTQQQLSEP SAEAPRARPC RVTTADRSVR KGIMVHSLED LHVKVRDTLM
LAYKPFFLVL EEDGTTVETE EYFQSLADDT VFMVLHKGQK WQPPSEQSTR YQLALSHKPA
KIDVARVTFD LYKVNPQDFI GCLNVKATLY GTYSVSYDLH CSGAKRIMKE ALRWALFSMR
TTGHMLLGTS CYLQQLLDAT EREQPPKSKA ASLIPTSLKM LQ
