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Selenophosphate synthetase 2

SPS2, selenophosphate synthetase 2, Sephs2
This gene encodes an enzyme that synthesizes selenophosphate from selenide and ATP. Selenophosphate is the selenium donor used to synthesize selenocysteine, which is co-translationally incorporated into selenoproteins at in-frame UGA codons. This protein itself contains a selenocysteine residue in its predicted active site. The 3' UTR of the gene has a stem-loop secondary structure called a selenocysteine insertion sequence (SECIS) element, which allows UGA to direct the incorporation of selenocysteine rather than signal a translational stop. Alternatively spliced transcripts have been identified, but their biological validity has not been determined. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Ethanolaminephosphotransferase, ACID, Thioredoxin, gpx1, selenoprotein P
Papers on SPS2
Effects of Dietary Selenium Against Lead Toxicity on mRNA Levels of 25 Selenoprotein Genes in the Cartilage Tissue of Broiler Chicken.
Fu et al., Nanjing, China. In Biol Trace Elem Res, Jan 2016
In the sword cartilage, Se alleviated the downtrend of the expression of Gpx2, Gpx3, Gpx4, Txnrd1, Txnrd2, Dio2, Dio3, Seli, Selh, SPS2, Sepx1, Selk, Selw, Selo, Selm, Sep15, Selpb, Sepn1, and Selt induced by Pb exposure.
Selenoproteins and heat shock proteins play important roles in immunosuppression in the bursa of Fabricius of chickens with selenium deficiency.
Li et al., Harbin, China. In Cell Stress Chaperones, Nov 2015
The data showed that the mRNA expression levels of selenoproteins, such as Txnrd1, Txnrd2, Txnrd3, Dio1, Dio2, Dio3, GPx1, GPx2, GPx3 GPx4, Sepp1, Selo, Sel-15, Sepx1, Sels, Seli, Selu, Selh, and SPS2, were significantly lower (P < 0.05) in the L group compared with the control group.
Selenium Deficiency Influences the mRNA Expression of Selenoproteins and Cytokines in Chicken Erythrocytes.
Xu et al., Harbin, China. In Biol Trace Elem Res, Nov 2015
In both groups, glutathione peroxidase (GPX), thioredoxin 1 (Txnrd1), selenoprotein P1 (SELP), and selenoprotein synthetase (SPS2) were highly expressed compared to the other selenoproteins in chicken erythrocytes (P < 0.05).
Fibrillin 5 Is Essential for Plastoquinone-9 Biosynthesis by Binding to Solanesyl Diphosphate Synthases in Arabidopsis.
Kim et al., Chŏnju, South Korea. In Plant Cell, Oct 2015
FBN5 binding to the hydrophobic solanesyl moiety, which is generated by SPS1 and SPS2, in FBN5-B/SPS homodimeric complexes stimulates the enzyme activity of SPS1 and SPS2.
Selenium Deficiency Affects the mRNA Expression of Inflammatory Factors and Selenoprotein Genes in the Kidneys of Broiler Chicks.
Shan et al., Harbin, China. In Biol Trace Elem Res, Oct 2015
The mRNA levels of 14 selenoprotein genes (Dio1, Dio2, GPx3, Sepp1, SelH, SelI, SelK, Sepn1, SelO, SelW, Sep15, SelT, SelU, and SelS) decreased, and 9 selenoprotein genes (GPx1, GPx2, GPx4, SelPb, Txnrd1, Txnrd2, Txnrd3, SPS2, and SelM) increased in L group (p < 0.05), but the Dio3 and Sepx1 mRNA levels did not change.
Evolution of selenophosphate synthetases: emergence and relocation of function through independent duplications and recurrent subfunctionalization.
Guigó et al., Barcelona, Spain. In Genome Res, Sep 2015
Using complementation assays in fly mutants, we show that these genes share a common function, which appears to be distinct from the synthesis of selenophosphate carried out by the Sec- and Cys- SPS genes (termed SPS2), and unrelated to Sec synthesis.
Selenium Deficiency Downregulates Selenoproteins and Suppresses Immune Function in Chicken Thymus.
Li et al., Harbin, China. In Biol Trace Elem Res, Sep 2015
The messenger RNA (mRNA) levels of Txnrd1, Txnrd2, Txnrd3, Dio1, Dio2, Dio3, GPx1, GPx2, GPx3, Gpx4, Sepp1, Selo, Sep15, Sepx1, Sels, Seli, Selu, Selh, and SPS2 were all significantly decreased (P < 0.05) in the L group compared to the control group.
Effects of Se on the Diversity of SelT Synthesis and Distribution in Different Smooth Muscle Tissues in Rats.
Deng et al., Wuhan, China. In Biol Trace Elem Res, Sep 2015
The messenger RNA (mRNA) of selenocysteine-tRNA([Ser]Sec) synthase (SecS), selenophosphate synthetase 1 (SPS1), selenophosphate synthetase 2 (SPS2), and SelT were examined using qPCR, and SelT protein was detected by Western blotting.
Roles of selenoprotein antioxidant protection in zebrafish, Danio rerio, subjected to dietary oxidative stress.
Tocher et al., Stirling, United Kingdom. In Fish Physiol Biochem, Jun 2015
High dietary DHA decreased selenoprotein W expression in muscle and sps2 expression in liver regardless of the dietary Se content.
Selenium deficiency influences nitric oxide and selenoproteins in pancreas of chickens.
Xu et al., Harbin, China. In Biol Trace Elem Res, 2014
Among them, thioredoxin reductase 1 (TXNRD1), selenoprotein S (SELS), selenoprotein U (SELU), selenoprotein X1 (SEPX1), and selenoprotein synthetase 2 (SPS2) were highly and extensively expressed than other types of selenoproteins in pancreas of chickens (P < 0.05).
Selenium deficiency mainly influences the gene expressions of antioxidative selenoproteins in chicken muscles.
Xu et al., Harbin, China. In Biol Trace Elem Res, 2014
In 25 selenoproteins, Gpxs, Txnrd2, Txnrd 3, Dio1, Dio 3, Selk, Sels, Sepw1, Selh, Sep15, Selu, Selpb, Sepp1, Selo, Sepx1, and SPS2 were downregulated (P < 0.05), and other selenoproteins were not influenced (P > 0.05).
Biosynthesis of selenocysteine, the 21st amino acid in the genetic code, and a novel pathway for cysteine biosynthesis.
Hatfield et al., Boston, United States. In Adv Nutr, 2011
Sec tRNA, designated tRNA([Ser]Sec), is initially aminoacylated with serine by seryl-tRNA synthetase and the resulting seryl moiety is converted to phosphoserine by O-phosphoseryl-tRNA kinase to form O-phosphoseryl-tRNA([Ser]Sec). Sec synthase (SecS) then uses O-phosphoseryl-tRNA([Ser]Sec) and the active donor of selenium, selenophosphate, to form Sec-tRNA([Ser]Sec). Selenophosphate is synthesized from selenide and ATP by selenophosphate synthetase 2 (SPS2).
Active bovine selenophosphate synthetase 2, not having selenocysteine.
Mizutani et al., Nagoya, Japan. In Mol Biol Rep, 2008
Thus, bovine active selenophosphate synthetase 2 of molecular mass 33 kDa does not contain selenocysteine.
Selenoproteins and maternal nutrition.
Zervas et al., Athens, Greece. In Comp Biochem Physiol B Biochem Mol Biol, 2008
Sel include but not limited to glutathione peroxidases (GPx1-GPx6), thioredoxin reductases (TrxR1-TrxR3), iodothyronine deiodinases (ID1-ID3), selenophosphate synthetase 2 (SPS2), 15-kDa Sel (Sel15), SelH, SelI, SelK, SelM, SelN, SelO, SelP, SelR, SelS, SelT, SelV, SelW, as well as the 15-kDa Sel (Fep15), SelJ and SelU found in fish.
Selenophosphate synthetase 2 is essential for selenoprotein biosynthesis.
Hatfield et al., Bethesda, United States. In Biochem J, 2007
These in vivo studies indicate that SPS2 is essential for generating the selenium donor for selenocysteine biosynthesis in mammals.
Selenophosphate synthetase genes from lung adenocarcinoma cells: Sps1 for recycling L-selenocysteine and Sps2 for selenite assimilation.
Inagaki et al., Okayama, Japan. In Proc Natl Acad Sci U S A, 2004
the Sps1-encoded enzyme depends on a selenium salvage system that recycles l-selenocysteine, whereas the Sps2 enzyme can function with a selenite assimilation system
Mammalian selenium-containing proteins.
Kyriakopoulos et al., Berlin, Germany. In Annu Rev Nutr, 2000
Selenoproteins with known functions identified so far include five glutathione peroxidases, two deiodinases, several thioredoxin reductases, and selenophosphate synthetase 2. Alternative splicing leads to a greater variety of selenoproteins, as was shown in the cases of a specific sperm nuclei glutathione peroxidase and some thioredoxin reductases.
Selenium in biology: facts and medical perspectives.
Flohé et al., Würzburg, Germany. In Biol Chem, 2000
Enzyme activities have been assigned to the glutathione peroxidase family, to the thioredoxin reductases, which were recently identified as selenoproteins, to the iodothyronine deiodinases, which metabolize thyroid hormones, and to the selenophosphate synthetase 2, which is involved in selenoprotein biosynthesis.
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