2024-05-03 15:53:47, GGRNA.v2 : RefSeq release 222 (Jan, 2024)
LOCUS NM_001348246 1237 bp mRNA linear ROD 22-DEC-2022 DEFINITION Mus musculus selenoprotein S (Selenos), transcript variant 2, mRNA. ACCESSION NM_001348246 VERSION NM_001348246.1 KEYWORDS RefSeq. SOURCE Mus musculus (house mouse) ORGANISM Mus musculus Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus. REFERENCE 1 (bases 1 to 1237) AUTHORS Qiao L, Men L, Yu S, Yao J, Li Y, Wang M, Yu Y, Wang N, Ran L, Wu Y and Du J. TITLE Hepatic deficiency of selenoprotein S exacerbates hepatic steatosis and insulin resistance JOURNAL Cell Death Dis 13 (3), 275 (2022) PUBMED 35347118 REMARK Publication Status: Online-Only REFERENCE 2 (bases 1 to 1237) AUTHORS Addinsall AB, Wright CR, Kotsiakos TL, Smith ZM, Cook TR, Andrikopoulos S, van der Poel C and Stupka N. TITLE Impaired exercise performance is independent of inflammation and cellular stress following genetic reduction or deletion of selenoprotein S JOURNAL Am J Physiol Regul Integr Comp Physiol 318 (5), R981-R996 (2020) PUBMED 32186893 REMARK GeneRIF: Impaired exercise performance with Seps1 reduction or deletion cannot be attributed to heightened cellular stress or inflammation, but it may potentially be mediated, in part, by the effects of Seps1 on the microvasculature. REFERENCE 3 (bases 1 to 1237) AUTHORS Men L, Yao J, Yu S, Li Y, Cui S, Jin S, Zhang G, Ren D and Du J. TITLE Selenoprotein S regulates adipogenesis through IRE1alpha-XBP1 pathway JOURNAL J Endocrinol 244 (3), 431-443 (2020) PUBMED 31846435 REMARK GeneRIF: Selenoprotein S regulates adipogenesis through IRE1alpha-XBP1 pathway. REFERENCE 4 (bases 1 to 1237) AUTHORS Men L, Sun J and Ren D. TITLE Deficiency of VCP-Interacting Membrane Selenoprotein (VIMP) Leads to G1 Cell Cycle Arrest and Cell Death in MIN6 Insulinoma Cells JOURNAL Cell Physiol Biochem 51 (5), 2185-2197 (2018) PUBMED 30537728 REMARK GeneRIF: These results suggest that VIMP may function as a novel regulator to modulate beta-cell survival, proliferation, cell cycle, unfolded protein response and insulin secretion in MIN6 cells. VIMP knockdown (KD) decreases cell proliferation and G1 cell cycle arrest. REFERENCE 5 (bases 1 to 1237) AUTHORS Gladyshev VN, Arner ES, Berry MJ, Brigelius-Flohe R, Bruford EA, Burk RF, Carlson BA, Castellano S, Chavatte L, Conrad M, Copeland PR, Diamond AM, Driscoll DM, Ferreiro A, Flohe L, Green FR, Guigo R, Handy DE, Hatfield DL, Hesketh J, Hoffmann PR, Holmgren A, Hondal RJ, Howard MT, Huang K, Kim HY, Kim IY, Kohrle J, Krol A, Kryukov GV, Lee BJ, Lee BC, Lei XG, Liu Q, Lescure A, Lobanov AV, Loscalzo J, Maiorino M, Mariotti M, Sandeep Prabhu K, Rayman MP, Rozovsky S, Salinas G, Schmidt EE, Schomburg L, Schweizer U, Simonovic M, Sunde RA, Tsuji PA, Tweedie S, Ursini F, Whanger PD and Zhang Y. TITLE Selenoprotein Gene Nomenclature JOURNAL J Biol Chem 291 (46), 24036-24040 (2016) PUBMED 27645994 REFERENCE 6 (bases 1 to 1237) AUTHORS Bubenik JL, Miniard AC and Driscoll DM. TITLE Alternative transcripts and 3'UTR elements govern the incorporation of selenocysteine into selenoprotein S JOURNAL PLoS One 8 (4), e62102 (2013) PUBMED 23614019 REMARK Publication Status: Online-Only REFERENCE 7 (bases 1 to 1237) AUTHORS Fradejas N, Pastor MD, Mora-Lee S, Tranque P and Calvo S. TITLE SEPS1 gene is activated during astrocyte ischemia and shows prominent antiapoptotic effects JOURNAL J Mol Neurosci 35 (3), 259-265 (2008) PUBMED 18498015 REMARK GeneRIF: We found that suppression of SEPS1 by small interfering RNA severely increases astrocyte injure caused by OGD, suggesting that selenoprotein S protects astrocytes against ischemia. REFERENCE 8 (bases 1 to 1237) AUTHORS Kim KH, Gao Y, Walder K, Collier GR, Skelton J and Kissebah AH. TITLE SEPS1 protects RAW264.7 cells from pharmacological ER stress agent-induced apoptosis JOURNAL Biochem Biophys Res Commun 354 (1), 127-132 (2007) PUBMED 17210132 REMARK GeneRIF: These findings suggest that SEPS1 could be a new ER stress-dependent survival factor that protects macrophage against ER stress-induced cellular dysfunction. REFERENCE 9 (bases 1 to 1237) AUTHORS Curran JE, Jowett JB, Elliott KS, Gao Y, Gluschenko K, Wang J, Abel Azim DM, Cai G, Mahaney MC, Comuzzie AG, Dyer TD, Walder KR, Zimmet P, MacCluer JW, Collier GR, Kissebah AH and Blangero J. TITLE Genetic variation in selenoprotein S influences inflammatory response JOURNAL Nat Genet 37 (11), 1234-1241 (2005) PUBMED 16227999 REFERENCE 10 (bases 1 to 1237) AUTHORS Kryukov GV, Castellano S, Novoselov SV, Lobanov AV, Zehtab O, Guigo R and Gladyshev VN. TITLE Characterization of mammalian selenoproteomes JOURNAL Science 300 (5624), 1439-1443 (2003) PUBMED 12775843 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from AC124695.4, AK005204.1 and AI836862.1. Summary: This gene encodes a transmembrane protein that is localized in the endoplasmic reticulum (ER). It is involved in the degradation process of misfolded proteins in the ER, and may also have a role in inflammation control. This protein is a selenoprotein, containing the rare amino acid selenocysteine (Sec). Sec is encoded by the UGA codon, which normally signals translation termination. The 3' UTRs of selenoprotein mRNAs contain a conserved stem-loop structure, designated the Sec insertion sequence (SECIS) element, that is necessary for the recognition of UGA as a Sec codon, rather than as a stop signal. Two additional phylogenetically conserved stem-loop structures (Stem-loop 1 and Stem-loop 2) in the 3' UTR of this mRNA have been shown to function as modulators of Sec insertion (PMID:23614019). Alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Jul 2017]. Transcript Variant: This variant (2) uses an alternate donor splice site at the 5' terminal exon, which results in translation initiation from an alternate start codon, compared to variant 1. The resulting isoform (2) has a shorter and distinct N-terminus compared to isoform 1. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BU938591.1, BU936537.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMN00849380, SAMN00849381 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## protein contains selenocysteine :: PMID: 12775843 ##RefSeq-Attributes-END## COMPLETENESS: complete on the 3' end. PRIMARY REFSEQ_SPAN PRIMARY_IDENTIFIER PRIMARY_SPAN COMP 1-170 AC124695.4 43929-44098 c 171-1104 AK005204.1 125-1058 1105-1237 AI836862.1 1-133 c FEATURES Location/Qualifiers source 1..1237 /organism="Mus musculus" /mol_type="mRNA" /strain="C57BL/6" /db_xref="taxon:10090" /chromosome="7" /map="7 35.49 cM" gene 1..1237 /gene="Selenos" /gene_synonym="1500011E07Rik; H-4; H-47; H4; H47; Sels; Seps1; Vimp" /note="selenoprotein S" /db_xref="GeneID:109815" /db_xref="MGI:MGI:95994" exon 1..170 /gene="Selenos" /gene_synonym="1500011E07Rik; H-4; H-47; H4; H47; Sels; Seps1; Vimp" /inference="alignment:Splign:2.1.0" misc_feature 77..79 /gene="Selenos" /gene_synonym="1500011E07Rik; H-4; H-47; H4; H47; Sels; Seps1; Vimp" /note="upstream in-frame stop codon" CDS 164..667 /gene="Selenos" /gene_synonym="1500011E07Rik; H-4; H-47; H4; H47; Sels; Seps1; Vimp" /note="UGA stop codon recoded as selenocysteine; isoform 2 is encoded by transcript variant 2; VCP-interacting membrane protein; minor histocompatibility antigen H47" /codon_start=1 /transl_except=(pos:659..661,aa:Sec) /product="selenoprotein S isoform 2" /protein_id="NP_001335175.1" /db_xref="GeneID:109815" /db_xref="MGI:MGI:95994" /translation="
MLVGSLLASYGWYILFSCILLYIVIQRLSLRLRALRQRQLDQAETVLEPDVVVKRQEALAAARLRMQEDLNAQVEKHKEKLRQLEEEKRRQKIEMWDSMQEGRSYKRNSGRPQEEDGPGPSTSSVIPKGKSDKKPLRGGGYNPLTGEGGGTCSWRPGRRGPSSGGUN"
misc_feature 170..658 /gene="Selenos" /gene_synonym="1500011E07Rik; H-4; H-47; H4; H47; Sels; Seps1; Vimp" /note="Selenoprotein S (SelS); Region: Selenoprotein_S; pfam06936" /db_xref="CDD:429198" misc_feature 659..661 /gene="Selenos" /gene_synonym="1500011E07Rik; H-4; H-47; H4; H47; Sels; Seps1; Vimp" /note="Selenocysteine; other site" exon 171..305 /gene="Selenos" /gene_synonym="1500011E07Rik; H-4; H-47; H4; H47; Sels; Seps1; Vimp" /inference="alignment:Splign:2.1.0" exon 306..412 /gene="Selenos" /gene_synonym="1500011E07Rik; H-4; H-47; H4; H47; Sels; Seps1; Vimp" /inference="alignment:Splign:2.1.0" exon 413..502 /gene="Selenos" /gene_synonym="1500011E07Rik; H-4; H-47; H4; H47; Sels; Seps1; Vimp" /inference="alignment:Splign:2.1.0" exon 503..581 /gene="Selenos" /gene_synonym="1500011E07Rik; H-4; H-47; H4; H47; Sels; Seps1; Vimp" /inference="alignment:Splign:2.1.0" exon 582..1220 /gene="Selenos" /gene_synonym="1500011E07Rik; H-4; H-47; H4; H47; Sels; Seps1; Vimp" /inference="alignment:Splign:2.1.0" regulatory 670..702 /regulatory_class="recoding_stimulatory_region" /gene="Selenos" /gene_synonym="1500011E07Rik; H-4; H-47; H4; H47; Sels; Seps1; Vimp" /note="Stem-loop 1" /function="promotes selenocysteine insertion" regulatory 981..1068 /regulatory_class="recoding_stimulatory_region" /gene="Selenos" /gene_synonym="1500011E07Rik; H-4; H-47; H4; H47; Sels; Seps1; Vimp" /note="SECIS_element" /function="essential for recoding UGA to specify selenocysteine" regulatory 1073..1099 /regulatory_class="other" /gene="Selenos" /gene_synonym="1500011E07Rik; H-4; H-47; H4; H47; Sels; Seps1; Vimp" /note="recoding_inhibitory_region; Stem-loop 2" /function="inhibits selenocysteine insertion" ORIGIN
gaaccggaagcgcagagcagagaggagcagcgggcttgtcgttggtggcggtggcggtggccgccatggatcgcgatgaggaacctctgtccgcgaggccggcgctggagaccgagagcctgcgattcctgcacgtgacaggtcaggggcggcgggcgccgccatgctcgtgggctccctgctggccagctatggctggtacatcctcttcagctgcatcctactctacattgtcatccagaggctctcccttcgactgagggctttgaggcagagacagctggaccaagccgagactgttctggaacctgatgttgttgttaagcggcaagaggctttagcagctgctcgtttgagaatgcaggaagatctaaatgcccaagttgaaaaacataaggaaaaactaagacagcttgaagaagagaaaagaagacagaagattgaaatgtgggacagcatgcaagaaggcagaagttacaaaagaaattcaggaaggcctcaggaagaagatggtcctggaccttctacttcatctgtcatccccaaaggaaaatctgacaaaaagcctttgcgaggaggtggttataaccctctgacgggtgaagggggtggaacctgctcctggagacctggacgcaggggcccatcatctggcggctgaaactaagactcttgttagtgtcgctctgacattagcaaggtgaacctttaaccctcaactcaattgccttacgcacactttcacagtgactggccaaggagaggtggggcttttctctgttctaaactacttgtactttaagggctttggtcagcatgagatatagacattgccattaggccacactctagacaagacagccatggcttttatggctgctggctagttggtaggttgaaggcttcttgctgtttagcagacttcataaagaaggcccagtgatgatactttggggtagaagtccttgctggcaggatggtctctgtgacgggatgcgttgaatgatgtcttccttataaatggtgaacccaccagtgaggattactgatgttcacagttgacggggtttgcttctgtatatttattttatgtacagaactttgtaaaaaaaaaaaaaagttaaatacttaaaaagtaacatttttagcatctttattaaactcaaggaaatttctttgtgagcttgactttgtcagacagtaaacagctttgtatcattaaaaaaaaaaaaaaaaa
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Creative Commons Attribution 4.0 International License (CC BY 4.0).
If you use GGRNA in your work, please cite:
Naito Y, Bono H. (2012)
GGRNA: an ultrafast, transcript-oriented search engine for genes and transcripts.
Nucleic Acids Res., 40, W592-W596.
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