SELS (gene)

VCP-interacting membrane protein

PDB rendering based on 2q2f.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
2Q2F

Identifiers

Symbols

VIMP ; ADO15; SBBI8; SELS; SEPS1

External IDs

OMIM: 607918 MGI: 95994 HomoloGene: 10200 GeneCards: VIMP Gene

Gene ontology
Molecular function	• receptor activity • protein binding • selenium binding • antioxidant activity • enzyme binding
Cellular component	• endoplasmic reticulum • cytoplasmic microtubule • plasma membrane • integral component of endoplasmic reticulum membrane • very-low-density lipoprotein particle • low-density lipoprotein particle
Biological process	• negative regulation of acute inflammatory response to antigenic stimulus • regulation of gluconeogenesis • ER overload response • response to glucose • ER-associated ubiquitin-dependent protein catabolic process • endoplasmic reticulum unfolded protein response • retrograde protein transport, ER to cytosol • negative regulation of interleukin-6 production • negative regulation of tumor necrosis factor production • cellular response to insulin stimulus • cellular response to oxidative stress • establishment of protein localization • cell redox homeostasis • negative regulation of glycogen biosynthetic process • negative regulation of glucose import • negative regulation of inflammatory response • negative regulation of nitric-oxide synthase biosynthetic process • response to redox state • cellular response to lipopolysaccharide • regulation of nitric oxide metabolic process • negative regulation of intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress • negative regulation of macrophage apoptotic process
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 15:
101.81 – 101.82 Mb

Chr 7:
66.08 – 66.09 Mb

PubMed search

Selenoprotein S, also known as SELS, is a human gene.^[1]

This gene encodes a selenoprotein, which contains a selenocysteine (Sec) residue at its active site. The selenocysteine is encoded by the UGA codon that normally signals translation termination. The 3' UTR of selenoprotein genes have a common stem-loop structure, the sec insertion sequence (SECIS), that is necessary for the recognition of UGA as a Sec codon rather than as a stop signal. Studies suggest that this protein may regulate cytokine production, and thus play a key role in the control of the inflammatory response. Two alternatively spliced transcript variants encoding the same protein have been found for this gene.^[1]

Interactions

SELS (gene) has been shown to interact with Valosin-containing protein.^[2]^[3]

References

↑ 1.0 1.1 "Entrez Gene: SELS selenoprotein S".
↑ Ye, Yihong; Shibata Yoko; Yun Chi; Ron David; Rapoport Tom A (Jun 2004). "A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol". Nature (England) 429 (6994): 841–7. doi:10.1038/nature02656. PMID 15215856.
↑ Wang, Qiuyan; Li Lianyun; Ye Yihong (Mar 2008). "Inhibition of p97-dependent Protein Degradation by Eeyarestatin I". J. Biol. Chem. (United States) 283 (12): 7445–54. doi:10.1074/jbc.M708347200. ISSN 0021-9258. PMC 2276333. PMID 18199748.

Robertson NG, Khetarpal U, Gutiérrez-Espeleta GA et al. (1995). "Isolation of novel and known genes from a human fetal cochlear cDNA library using subtractive hybridization and differential screening". Genomics 23 (1): 42–50. doi:10.1006/geno.1994.1457. PMID 7829101.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Hu RM, Han ZG, Song HD et al. (2000). "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning". Proc. Natl. Acad. Sci. U.S.A. 97 (17): 9543–8. doi:10.1073/pnas.160270997. PMC 16901. PMID 10931946.
Walder K, Kantham L, McMillan JS et al. (2002). "Tanis: a link between type 2 diabetes and inflammation?". Diabetes 51 (6): 1859–66. doi:10.2337/diabetes.51.6.1859. PMID 12031974.
Strausberg RL, Feingold EA, Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Gao Y, Walder K, Sunderland T et al. (2003). "Elevation in Tanis expression alters glucose metabolism and insulin sensitivity in H4IIE cells". Diabetes 52 (4): 929–34. doi:10.2337/diabetes.52.4.929. PMID 12663463.
Kryukov GV, Castellano S, Novoselov SV et al. (2003). "Characterization of mammalian selenoproteomes". Science 300 (5624): 1439–43. doi:10.1126/science.1083516. PMID 12775843.
Ota T, Suzuki Y, Nishikawa T et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Gao Y, Feng HC, Walder K et al. (2004). "Regulation of the selenoprotein SelS by glucose deprivation and endoplasmic reticulum stress - SelS is a novel glucose-regulated protein". FEBS Lett. 563 (1–3): 185–90. doi:10.1016/S0014-5793(04)00296-0. PMID 15063746.
Karlsson HK, Tsuchida H, Lake S et al. (2004). "Relationship between serum amyloid A level and Tanis/SelS mRNA expression in skeletal muscle and adipose tissue from healthy and type 2 diabetic subjects". Diabetes 53 (6): 1424–8. doi:10.2337/diabetes.53.6.1424. PMID 15161744.
Ye Y, Shibata Y, Yun C et al. (2004). "A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol". Nature 429 (6994): 841–7. doi:10.1038/nature02656. PMID 15215856.
Gerhard DS, Wagner L, Feingold EA et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Lilley BN, Ploegh HL (2006). "Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane". Proc. Natl. Acad. Sci. U.S.A. 102 (40): 14296–301. doi:10.1073/pnas.0505014102. PMC 1242303. PMID 16186509.
Ye Y, Shibata Y, Kikkert M et al. (2006). "Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane". Proc. Natl. Acad. Sci. U.S.A. 102 (40): 14132–8. doi:10.1073/pnas.0505006102. PMC 1242302. PMID 16186510.
Curran JE, Jowett JB, Elliott KS et al. (2006). "Genetic variation in selenoprotein S influences inflammatory response". Nat. Genet. 37 (11): 1234–41. doi:10.1038/ng1655. PMID 16227999.
Gao Y, Hannan NR, Wanyonyi S et al. (2006). "Activation of the selenoprotein SEPS1 gene expression by pro-inflammatory cytokines in HepG2 cells". Cytokine 33 (5): 246–51. doi:10.1016/j.cyto.2006.02.005. PMID 16574427.
Gao Y, Pagnon J, Feng HC et al. (2007). "Secretion of the glucose-regulated selenoprotein SEPS1 from hepatoma cells". Biochem. Biophys. Res. Commun. 356 (3): 636–41. doi:10.1016/j.bbrc.2007.03.018. PMID 17374524.
Seiderer J, Dambacher J, Kühnlein B et al. (2007). "The role of the selenoprotein S (SELS) gene -105G>A promoter polymorphism in inflammatory bowel disease and regulation of SELS gene expression in intestinal inflammation". Tissue Antigens 70 (3): 238–46. doi:10.1111/j.1399-0039.2007.00888.x. PMID 17661913.

PDB gallery

2q2f: Structure of the human Selenoprotein S (VCP-interacting membrane protein)

SELS (gene)

Interactions

References

Further reading