2eel
From Proteopedia
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{{STRUCTURE_2eel| PDB=2eel | SCENE= }} | {{STRUCTURE_2eel| PDB=2eel | SCENE= }} | ||
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===Solution structure of the CIDE-N domain of human cell death activator CIDE-A=== | ===Solution structure of the CIDE-N domain of human cell death activator CIDE-A=== | ||
| + | ==Disease== | ||
| + | [[http://www.uniprot.org/uniprot/CIDEA_HUMAN CIDEA_HUMAN]] Note=In omental and subcutaneous adipose tissue of obese patients matched for BMI, expression levels correlate with insulin sensitivity. Expression is increased 5-6 fold in the group of patients with high insulin sensitivity, compared to the insulin-resistant group. This observation is consistent with the idea that triglyceride storage in adipocytes plays an important role in sequestering triglycerides and fatty acids away from the circulation and peripheral tissues, thus enhancing insulin sensitivity in liver and muscle.<ref>PMID:18509062</ref> | ||
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| + | ==Function== | ||
| + | [[http://www.uniprot.org/uniprot/CIDEA_HUMAN CIDEA_HUMAN]] Acts as a CEBPB coactivator in mammary epithelial cells to control the expression of a subset of CEBPB downstream target genes, including ID2, IGF1, PRLR, SOCS1, SOCS3, XDH, but not casein. By interacting with CEBPB, strengthens the association of CEBPB with the XDH promoter, increases histone acetylation and dissociates HDAC1 from the promoter (By similarity). 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 and occurs at a lower rate than that promoted by CIDEC. When overexpressed, induces apoptosis. The physiological significance of its role in apoptosis is unclear.<ref>PMID:19843876</ref> | ||
==About this Structure== | ==About this Structure== | ||
[[2eel]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EEL OCA]. | [[2eel]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EEL OCA]. | ||
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| + | ==Reference== | ||
| + | <references group="xtra"/><references/> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Hayashi, F.]] | [[Category: Hayashi, F.]] | ||
Revision as of 23:36, 24 March 2013
Contents |
Solution structure of the CIDE-N domain of human cell death activator CIDE-A
Disease
[CIDEA_HUMAN] Note=In omental and subcutaneous adipose tissue of obese patients matched for BMI, expression levels correlate with insulin sensitivity. Expression is increased 5-6 fold in the group of patients with high insulin sensitivity, compared to the insulin-resistant group. This observation is consistent with the idea that triglyceride storage in adipocytes plays an important role in sequestering triglycerides and fatty acids away from the circulation and peripheral tissues, thus enhancing insulin sensitivity in liver and muscle.[1]
Function
[CIDEA_HUMAN] Acts as a CEBPB coactivator in mammary epithelial cells to control the expression of a subset of CEBPB downstream target genes, including ID2, IGF1, PRLR, SOCS1, SOCS3, XDH, but not casein. By interacting with CEBPB, strengthens the association of CEBPB with the XDH promoter, increases histone acetylation and dissociates HDAC1 from the promoter (By similarity). 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 and occurs at a lower rate than that promoted by CIDEC. When overexpressed, induces apoptosis. The physiological significance of its role in apoptosis is unclear.[2]
About this Structure
2eel is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA.
Reference
- ↑ Puri V, Ranjit S, Konda S, Nicoloro SM, Straubhaar J, Chawla A, Chouinard M, Lin C, Burkart A, Corvera S, Perugini RA, Czech MP. Cidea is associated with lipid droplets and insulin sensitivity in humans. Proc Natl Acad Sci U S A. 2008 Jun 3;105(22):7833-8. doi:, 10.1073/pnas.0802063105. Epub 2008 May 28. PMID:18509062 doi:10.1073/pnas.0802063105
- ↑ Liu K, Zhou S, Kim JY, Tillison K, Majors D, Rearick D, Lee JH, Fernandez-Boyanapalli RF, Barricklow K, Houston MS, Smas CM. Functional analysis of FSP27 protein regions for lipid droplet localization, caspase-dependent apoptosis, and dimerization with CIDEA. Am J Physiol Endocrinol Metab. 2009 Dec;297(6):E1395-413. doi:, 10.1152/ajpendo.00188.2009. Epub 2009 Oct 20. PMID:19843876 doi:10.1152/ajpendo.00188.2009
Categories: Homo sapiens | Hayashi, F. | Nagashima, T. | Qin, X R. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Yokoyama, S. | Apoptosis | Cell death activator cide-a | Cell death-inducing dffa-like effector some | Cide-n domain | National project on protein structural and functional analyse | Nppsfa | Riken structural genomics/proteomics initiative | Rsgi | Structural genomic
