CIDEA_HUMAN
ID CIDEA_HUMAN Reviewed; 219 AA.
AC O60543; B0YIY7; Q6UPR7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Cell death activator CIDE-A;
DE AltName: Full=Cell death-inducing DFFA-like effector A;
GN Name=CIDEA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9564035; DOI=10.1093/emboj/17.9.2526;
RA Inohara N., Koseki T., Chen S., Wu X., Nunez G.;
RT "CIDE, a novel family of cell death activators with homology to the 45 kDa
RT subunit of the DNA fragmentation factor.";
RL EMBO J. 17:2526-2533(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PHE-115.
RC TISSUE=Brain;
RA Liang L., Xu Z., Li T., Zhao M.;
RT "Homo sapiens cell death activator CIDE-A mRNA.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SUBCELLULAR LOCATION, DISEASE, AND TISSUE SPECIFICITY.
RX PubMed=18509062; DOI=10.1073/pnas.0802063105;
RA Puri V., Ranjit S., Konda S., Nicoloro S.M., Straubhaar J., Chawla A.,
RA Chouinard M., Lin C., Burkart A., Corvera S., Perugini R.A., Czech M.P.;
RT "Cidea is associated with lipid droplets and insulin sensitivity in
RT humans.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:7833-7838(2008).
RN [5]
RP FUNCTION, AND INTERACTION WITH CIDEC.
RX PubMed=19843876; DOI=10.1152/ajpendo.00188.2009;
RA Liu K., Zhou S., Kim J.Y., Tillison K., Majors D., Rearick D., Lee J.H.,
RA Fernandez-Boyanapalli R.F., Barricklow K., Houston M.S., Smas C.M.;
RT "Functional analysis of FSP27 protein regions for lipid droplet
RT localization, caspase-dependent apoptosis, and dimerization with CIDEA.";
RL Am. J. Physiol. 297:E1395-E1413(2009).
RN [6]
RP STRUCTURE BY NMR OF 33-110.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the CIDE-N domain of human cell death activator
RT CIDE-A.";
RL Submitted (AUG-2007) to the PDB data bank.
CC -!- FUNCTION: Acts as a CEBPB coactivator in mammary epithelial cells to
CC control the expression of a subset of CEBPB downstream target genes,
CC including ID2, IGF1, PRLR, SOCS1, SOCS3, XDH, but not casein. By
CC interacting with CEBPB, strengthens the association of CEBPB with the
CC XDH promoter, increases histone acetylation and dissociates HDAC1 from
CC the promoter (By similarity). Binds to lipid droplets and regulates
CC their enlargement, thereby restricting lipolysis and favoring storage.
CC At focal contact sites between lipid droplets, promotes directional net
CC neutral lipid transfer from the smaller to larger lipid droplets. The
CC transfer direction may be driven by the internal pressure difference
CC between the contacting lipid droplet pair and occurs at a lower rate
CC than that promoted by CIDEC. When overexpressed, induces apoptosis. The
CC physiological significance of its role in apoptosis is unclear.
CC {ECO:0000250, ECO:0000269|PubMed:19843876}.
CC -!- SUBUNIT: Directly interacts with CEBPB (By similarity). Interacts with
CC CIDEC. {ECO:0000250, ECO:0000269|PubMed:19843876}.
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:18509062}.
CC Nucleus {ECO:0000250}. Note=Enriched at lipid droplet contact sites.
CC Has been shown to localize to mitochondria, where it could interact
CC with UCP1 and hence inhibit UCP1 uncoupling activity (By similarity).
CC These data could not be confirmed (PubMed:18509062). {ECO:0000250,
CC ECO:0000269|PubMed:18509062}.
CC -!- TISSUE SPECIFICITY: Expressed in omental and subcutaneous adipose
CC tissue (at protein level). {ECO:0000269|PubMed:18509062}.
CC -!- DISEASE: Note=In omental and subcutaneous adipose tissue of obese
CC patients matched for BMI, expression levels correlate with insulin
CC sensitivity. Expression is increased 5-6 fold in the group of patients
CC with high insulin sensitivity, compared to the insulin-resistant group.
CC This observation is consistent with the idea that triglyceride storage
CC in adipocytes plays an important role in sequestering triglycerides and
CC fatty acids away from the circulation and peripheral tissues, thus
CC enhancing insulin sensitivity in liver and muscle.
CC {ECO:0000269|PubMed:18509062}.
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DR EMBL; AF041378; AAC34987.1; -; mRNA.
DR EMBL; AY364639; AAQ65241.1; -; mRNA.
DR EMBL; EF444967; ACA05966.1; -; Genomic_DNA.
DR CCDS; CCDS11856.1; -.
DR RefSeq; NP_001270.1; NM_001279.3.
DR PDB; 2EEL; NMR; -; A=33-110.
DR PDBsum; 2EEL; -.
DR AlphaFoldDB; O60543; -.
DR BMRB; O60543; -.
DR SMR; O60543; -.
DR BioGRID; 107570; 14.
DR IntAct; O60543; 8.
DR MINT; O60543; -.
DR STRING; 9606.ENSP00000320209; -.
DR BioMuta; CIDEA; -.
DR jPOST; O60543; -.
DR MassIVE; O60543; -.
DR PaxDb; O60543; -.
DR PeptideAtlas; O60543; -.
DR PRIDE; O60543; -.
DR ProteomicsDB; 49464; -.
DR Antibodypedia; 6758; 318 antibodies from 35 providers.
DR DNASU; 1149; -.
DR Ensembl; ENST00000320477.10; ENSP00000320209.8; ENSG00000176194.18.
DR GeneID; 1149; -.
DR KEGG; hsa:1149; -.
DR MANE-Select; ENST00000320477.10; ENSP00000320209.8; NM_001279.4; NP_001270.1.
DR UCSC; uc002kqt.5; human.
DR CTD; 1149; -.
DR DisGeNET; 1149; -.
DR GeneCards; CIDEA; -.
DR HGNC; HGNC:1976; CIDEA.
DR HPA; ENSG00000176194; Group enriched (adipose tissue, breast).
DR MIM; 604440; gene.
DR neXtProt; NX_O60543; -.
DR OpenTargets; ENSG00000176194; -.
DR PharmGKB; PA26514; -.
DR VEuPathDB; HostDB:ENSG00000176194; -.
DR eggNOG; ENOG502RG9M; Eukaryota.
DR GeneTree; ENSGT00390000018596; -.
DR HOGENOM; CLU_090011_2_0_1; -.
DR InParanoid; O60543; -.
DR OMA; KCMGAKS; -.
DR PhylomeDB; O60543; -.
DR TreeFam; TF334321; -.
DR PathwayCommons; O60543; -.
DR Reactome; R-HSA-8964572; Lipid particle organization.
DR SignaLink; O60543; -.
DR BioGRID-ORCS; 1149; 12 hits in 1072 CRISPR screens.
DR ChiTaRS; CIDEA; human.
DR EvolutionaryTrace; O60543; -.
DR GeneWiki; CIDEA; -.
DR GenomeRNAi; 1149; -.
DR Pharos; O60543; Tbio.
DR PRO; PR:O60543; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; O60543; protein.
DR Bgee; ENSG00000176194; Expressed in adipose tissue of abdominal region and 108 other tissues.
DR ExpressionAtlas; O60543; baseline and differential.
DR Genevisible; O60543; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0005740; C:mitochondrial envelope; ISS:BHF-UCL.
DR GO; GO:0005739; C:mitochondrion; ISS:BHF-UCL.
DR GO; GO:0005634; C:nucleus; ISS:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:BHF-UCL.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0070417; P:cellular response to cold; IEA:Ensembl.
DR GO; GO:0006629; P:lipid metabolic process; ISS:BHF-UCL.
DR GO; GO:0019915; P:lipid storage; ISS:BHF-UCL.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0001818; P:negative regulation of cytokine production; IMP:BHF-UCL.
DR GO; GO:1900118; P:negative regulation of execution phase of apoptosis; ISS:BHF-UCL.
DR GO; GO:0050995; P:negative regulation of lipid catabolic process; IMP:BHF-UCL.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISS:BHF-UCL.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IMP:BHF-UCL.
DR GO; GO:0010890; P:positive regulation of sequestering of triglyceride; ISS:BHF-UCL.
DR GO; GO:1902510; P:regulation of apoptotic DNA fragmentation; ISS:BHF-UCL.
DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0035634; P:response to stilbenoid; IEA:Ensembl.
DR GO; GO:0001659; P:temperature homeostasis; ISS:BHF-UCL.
DR InterPro; IPR032936; CIDE-A.
DR InterPro; IPR003508; CIDE-N_dom.
DR PANTHER; PTHR12306:SF8; PTHR12306:SF8; 1.
DR Pfam; PF02017; CIDE-N; 1.
DR SMART; SM00266; CAD; 1.
DR PROSITE; PS51135; CIDE_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Apoptosis; Lipid droplet; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..219
FT /note="Cell death activator CIDE-A"
FT /id="PRO_0000144718"
FT DOMAIN 33..110
FT /note="CIDE-N"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00447"
FT VARIANT 115
FT /note="V -> F (in dbSNP:rs11545881)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_048738"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:2EEL"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:2EEL"
FT HELIX 55..65
FT /evidence="ECO:0007829|PDB:2EEL"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:2EEL"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:2EEL"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:2EEL"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:2EEL"
FT STRAND 95..103
FT /evidence="ECO:0007829|PDB:2EEL"
SQ SEQUENCE 219 AA; 24687 MW; 05F704823CE71C0E CRC64;
MEAARDYAGA LIRPLTFMGS QTKRVLFTPL MHPARPFRVS NHDRSSRRGV MASSLQELIS
KTLDALVIAT GLVTLVLEED GTVVDTEEFF QTLGDNTHFM ILEKGQKWMP GSQHVPTCSP
PKRSGIARVT FDLYRLNPKD FIGCLNVKAT MYEMYSVSYD IRCTGLKGLL RSLLRFLSYS
AQVTGQFLIY LGTYMLRVLD DKEERPSLRS QAKGRFTCG
