Infobox rfam Name Pyrrolysine insertion sequence 1 image PHYLIS SS.png width caption Predicted secondary structure of PYLIS 1 RNA. Symbol PYLIS 1 AltSymbols Rfam RF01982 miRBase miRBase family RNA type Cis regulatory element Tax domain Archaea GO SO CAS number EntrezGene HGNCid OMIM PDB RefSeq Chromosome Arm Band LocusSupplementaryData In biology, the PYLIS downstream sequence PYLIS py rro l ysine i nsertion s equence is a stem loop structure which appears on some mRNA sequences. This structural motif causes the UAG amber stop codon to be translated to the amino acid pyrrolysine instead of ending the protein translation. In archaea the PYLIS downstream sequence is positioned straight after the UAG codon which is translated as pyrrolysine. ref name pmid16164991 cite journal author Th obald Dietrich A, Gieg R, Rudinger Thirion J title Evidence for the existence in mRNAs of a hairpin element responsible for ribosome dependent pyrrolysine insertion into proteins journal Biochimie volume 87 issue 9 10 pages 813 7 year 2005 pmid 16164991 doi 10.1016 j.biochi.2005.03.006 url ref ref name pmid15788401 cite journal author Zhang Y, Baranov PV, Atkins JF, Gladyshev VN title Pyrrolysine and selenocysteine use dissimilar decoding strategies journal J. Biol. Chem. volume 280 issue 21 pages 20740 51 year 2005 month May pmid 15788401 doi 10.1074 jbc.M501458200 url ref See also SECIS element Pyrrolysine References reflist Further reading cite journal author Longstaff DG, Blight SK, Zhang L, Green Church KB, Krzycki JA title In vivo contextual requirements for UAG translation as pyrrolysine journal Mol. Microbiol. volume 63 issue 1 pages 229 41 year 2007 month January pmid 17140411 doi 10.1111 j.1365 2958.2006.05500.x url cite journal author Namy O, Zhou Y, Gundllapalli S, et al. title Adding pyrrolysine to the Escherichia coli genetic code journal FEBS Lett. volume 581 issue 27 pages 5282 8 year 2007 month November pmid 17967457 doi 10.1016 j.febslet.2007.10.022 url External links ... more details
standard abbreviations for the following two amino acids gallery image L selenocysteine 2D skeletal.png Selenocysteine small L small Selenocysteine br Sec U image Pyrrolysine.svg Pyrrolysine ... 1.82 8.99 Serine S Ser 105.09344 5.68 2.19 9.21 Threonine T Thr 119.12034 5.60 2.09 9.10 Selenocysteine ... OH CH sub 3 sub 5.53 weak acidic X 93 Selenocysteine U Sec CH sub 2 sub Selenol SeH 5.73 acidic X X ..., UCA, UCG, AGU, AGC 6.8 No Threonine T Thr ACU, ACC, ACA, ACG 5.9 Yes Selenocysteine U Sec UGA selenonote ..., but encodes selenocysteine if a SECIS element is present. br span id stopnote span The stop codon ... sub H sub 7 sub NO sub 2 sub 101.04768 101.1051 Selenocysteine U Sec C sub 3 sub H sub 5 sub NOSe 150.95364 ... to serine. Selenocysteine U Sec Selenium Selenated form of cysteine, which replaces sulfur . Valine ... more details
Orphan date February 2009 PBB geneid 9403 15 kDa selenoprotein , also known as SEP15 , is a human gene . ref name entrez cite web title Entrez Gene SEP15 15 kDa selenoprotein url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 9403 accessdate ref The PBB Summary template is automatically maintained by Protein Box Bot. See Template PBB Controls to Stop updates. PBB Summary section title summary text 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 in mouse suggest that this selenoprotein may have redox function and may be involved in the quality control of protein folding. This gene is localized on chromosome 1p31, a genetic locus commonly mutated or deleted in human cancers. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene. ref name entrez References reflist Further reading refbegin 2 PBB Further reading citations cite journal author Maruyama K, Sugano S title Oligo capping a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides journal Gene volume 138 issue 1 2 pages 171 174 year 1994 pmid 8125298 doi 10.1016 0378 1119 94 90802 8 cite journal author Suzuki Y title Construction and characterization of a full length enriched and a 5 end enriched cDNA library journal Gene volume 200 issue 1 2 pages 149 156 year 1997 pmid 9373149 doi 10.1016 S0378 1119 97 00411 3 author separator , author2 Yoshitomo Nakagawa K author3 Maruyama K display authors 3 last4 Suyama first4 A last5 Sugano first5 S cite journal author Gladyshev VN, Jeang KT, Wootton JC, Hatfield DL title A new human selenium containing protein. Purificati ... more details
PBB geneid 2878 Glutathione peroxidase 3 GPx 3 , also known as plasma glutathione peroxidase GPx P or extracellular glutathione peroxidase is an enzyme that in humans is encoded by the GPX3 gene . ref name entrez cite web title Entrez Gene glutathione peroxidase 3 plasma url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 2878 accessdate ref ref name pmid3619451 cite journal author Takahashi K, Avissar N, Whitin J, Cohen H title Purification and characterization of human plasma glutathione peroxidase a selenoglycoprotein distinct from the known cellular enzyme journal Arch. Biochem. Biophys. volume 256 issue 2 pages 677 86 year 1987 month August pmid 3619451 doi 10.1016 0003 9861 87 90624 2 url issn ref ref name pmid8287691 cite journal author Chu FF title The human glutathione peroxidase genes GPX2, GPX3, and GPX4 map to chromosomes 14, 5, and 19, respectively journal Cytogenet. Cell Genet. volume 66 issue 2 pages 96 8 year 1994 pmid 8287691 doi 10.1159 000133675 url issn ref GPx 3belongs to the glutathione peroxidase family, which functions in the detoxification of hydrogen peroxide. It contains a selenocysteine Sec residue at its active site. The selenocysteine is encoded by the UGA codon, which normally signals translation termination. The 3 UTR of Sec containing genes have a common stem loop structure, the sec insertion sequence SECIS , which is necessary for the recognition of UGA as a Sec codon rather than as a stop signal. ref name entrez References reflist Further reading refbegin 2 cite journal author Guey LT, Garc a Closas M, Murta Nascimento C, et al. title Genetic susceptibility to distinct bladder cancer subphenotypes. journal Eur. Urol. volume 57 issue 2 pages 283 92 year 2010 pmid 19692168 doi 10.1016 j.eururo.2009.08.001 cite journal author Lin JC, Kuo WR, Chiang FY, et al. title Glutathione peroxidase 3 gene polymorphisms and risk of differentiated thyroid cancer. journal Surgery volume 145 issue 5 pages 508 13 year ... more details
month June pmid 1709933 doi url ref and the prokaryote prokaryotic selenocysteine specific elongation ... Identification of a novel translation factor necessary for the incorporation of selenocysteine into protein ... more details
Pfam box Symbol peroxidase Name Peroxidase image GlutPeroxidase 1GP1.png width caption Glutathione Peroxidase 1 Pfam PF00141 InterPro IPR002016 SMART Prosite PDOC00394 SCOP 1hsr TCDB OPM family OPM protein PDB Peroxidases Enzyme Commission number EC number http www.chem.qmul.ac.uk iubmb enzyme EC1 11 1 1.11.1.x are a large family of enzyme s that typically catalyze a reaction of the form ROOR electron donor 2 e sup sup 2H sup sup ROH R OH For many of these enzymes the optimal Substrate biochemistry substrate is hydrogen peroxide , but others are more active with organic hydroperoxides such as lipid peroxides. Peroxidases can contain a heme cofactor biochemistry cofactor in their active sites, or alternately redox redox active cysteine or selenocysteine residues. The nature of the nucleophile electron donor is very dependent on the structure of the enzyme. For example, horseradish peroxidase can use a variety of organic compounds as electron donors and acceptors. Horseradish peroxidase has an accessible active site , and many compounds can reach the site of the reaction. Because there is a very closed active site, for an enzyme such as cytochrome c peroxidase , the compounds that donate electrons are very specific, . While the exact mechanisms have yet to be elucidated, peroxidases are known to play a part in increasing a plant s defenses against pathogens. ref Cite journal author Karthikeyan M et al. title Induction of resistance in host against the infection of leaf blight pathogen Alternaria palandui in onion Allium cepa var aggregatum journal Indian J Biochem Biophys volume 42 issue 6 pages 371 7 year 2005 month December pmid 16955738 format ref Peroxidases are sometimes used as histology histological marker. Cytochrome c peroxidase is used as a soluble, easily purified model for cytochrome c oxidase . The glutathione peroxidase family consists of 8 known human isoforms. Glutathione peroxidases use glutathione as an electron donor and are active with both hydroge ... more details
reductase have evolved independently A high molecular weight MW 55,000 type containing a selenocysteine ... thioredoxin reductase Implications for mechanism and evolution of a selenocysteine dependent ... cysteine selenocysteine sequence journal PNAS year 2000 month May volume 97 issue 11 pages ... more details
Image MRNA structure.svg thumb 400px mRNA structure, approximately to scale for a human mRNA, where the median length of 3 UTR is 700 nucleotides In molecular genetics , the three prime untranslated region 3 UTR is a particular section of messenger RNA mRNA . It starts with the nucleotide immediately following the stop codon of the coding region . An mRNA molecule codes for a protein through Translation genetics translation . The mRNA also contains regions that are not translated. In eukaryotes these regions are the 5 cap cap , 5 untranslated region , 3 untranslated region , and Polyadenylation polyA tail see diagram . In prokaryotes mRNA structures have some differences see mRNA as do histone mRNAs. However, both have 3 UTRs. Several regulatory sequence s are found in the 3 UTR A polyadenylation signal, usually AAUAAA , or a slight variant. This marks the site of cleavage of the transcript approximately 30 base pair s past the signal, followed by the addition of several hundred adenine residues poly A tail . ref name pmid20211174 cite journal author Neilson JR, Sandberg R. title Heterogeneity in mammalian RNA 3 end formation. journal Exp Cell Res. volume 316 issue 8 pages 1357 64 year 2010 month May pmid 20211174 pmc 2866830 doi 10.1016 j.yexcr.2010.02.040 ref ref name pmid18468939 cite journal author Ryan K, Bauer DL. title Finishing touches post translational modification of protein factors involved in mammalian pre mRNA 3 end formation. journal Int J Biochem Cell Biol. volume 40 issue 11 pages 2384 96 year 2008 month pmid 18468939 pmc 2548416 doi 10.1016 j.biocel.2008.03.016 ref Binding sites for proteins, that may affect the mRNA s stability or location in the cell, like SECIS element s which direct the ribosome to translate the codon UGA as selenocysteine s rather than as a stop codon , or AU rich element s AREs , stretches consisting of mainly adenine and uracil nucleotides which can either stabilize or destabilize the mRNA depending on the protein bound to i ... more details
PBB geneid 2882 Glutathione peroxidase 7 is an enzyme that in humans is encoded by the GPX7 gene . ref name pmid15294905 cite journal author Utomo A, Jiang X, Furuta S, Yun J, Levin DS, Wang YC, Desai KV, Green JE, Chen PL, Lee WH title Identification of a novel putative non selenocysteine containing phospholipid hydroperoxide glutathione peroxidase NPGPx essential for alleviating oxidative stress generated from polyunsaturated fatty acids in breast cancer cells journal J Biol Chem volume 279 issue 42 pages 43522 9 year 2004 month Oct pmid 15294905 pmc doi 10.1074 jbc.M407141200 ref ref name entrez cite web title Entrez Gene GPX7 glutathione peroxidase 7 url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 2882 accessdate ref The PBB Summary template is automatically maintained by Protein Box Bot. See Template PBB Controls to Stop updates. PBB Summary section title summary text References reflist Further reading refbegin 2 PBB Further reading citations cite journal author Opalenik SR, Ding Q, Mallery SR, Thompson JA title Glutathione depletion associated with the HIV 1 TAT protein mediates the extracellular appearance of acidic fibroblast growth factor. journal Arch. Biochem. Biophys. volume 351 issue 1 pages 17 26 year 1998 pmid 9501919 doi 10.1006 abbi.1997.0566 cite journal author Choi J, Liu RM, Kundu RK, et al. title Molecular mechanism of decreased glutathione content in human immunodeficiency virus type 1 Tat transgenic mice. journal J. Biol. Chem. volume 275 issue 5 pages 3693 8 year 2000 pmid 10652368 doi 10.1074 jbc.275.5.3693 cite journal author Richard MJ, Guiraud P, Didier C, et al. title Human immunodeficiency virus type 1 Tat protein impairs selenoglutathione peroxidase expression and activity by a mechanism independent of cellular selenium uptake consequences on cellular resistance to UV A radiation. journal Arch. Biochem. Biophys. volume 386 issue 2 pages 213 20 year 2001 pmid 11368344 doi 10.1006 abbi.2000.2197 cite jo ... more details
acids selenomethionine , selenocysteine , and methylselenocysteine . In these compounds, selenium ... to be present in two independent sets of enzyme s. This was followed by the discovery of selenocysteine in proteins. During the 1980s, it was shown that selenocysteine is encoded by the Genetic ... acid s selenocysteine and selenomethionine . In humans, selenium is a dietary mineral trace element ..., such as dimethyl selenide, selenomethionine , selenocysteine and methylselenocysteine , all of which ... the evolution of selenocysteine. Selenium is incorporated into several prokaryotic selenoprotein families in bacteria, archaea and eukaryotes as selenocysteine, ref name glady cite journal author Gladyshev VN, Hatfield DL title Selenocysteine containing proteins in mammals journal Journal of Biomedical ... phylogenetic origin. The selenocysteine containing form occurs in species as diverse as green ... name Stadtman cite journal author Stadtman TC title Selenocysteine journal Annual Review of Biochemistry ... more details
of the protein, in particular if unconventional amino acid s such as selenocysteine are incorporated ... hairpin SElenoCysteine Insertion Sequence, or SECIS . There are many computer programs capable ... more details
Orphan date February 2009 PBB geneid 55829 Selenoprotein S , also known as SELS , is a human gene . ref name entrez cite web title Entrez Gene SELS selenoprotein S url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 55829 accessdate ref The PBB Summary template is automatically maintained by Protein Box Bot. See Template PBB Controls to Stop updates. PBB Summary section title summary text 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. ref name entrez Interactions SELS gene has been shown to Protein protein interaction interact with Valosin containing protein . ref name pmid15215856 cite journal last Ye first Yihong authorlink coauthors Shibata Yoko, Yun Chi, Ron David, Rapoport Tom A year 2004 month Jun. title A membrane protein complex mediates retro translocation from the ER lumen into the cytosol journal Nature journal Nature volume 429 issue 6994 pages 841 7 publisher location England pmid 15215856 doi 10.1038 nature02656 bibcode oclc id url language format accessdate laysummary laysource laydate quote unused data DUPLICATE DATA pmid 15215847 ref ref name pmid18199748 cite journal last Wang first Qiuyan authorlink coauthors Li Lianyun, Ye Yihong year 2008 month Mar. title Inhibition of p97 dependent Protein Degradation by Eeyarestatin I journal J. Biol. Chem. volume 283 issue 12 pages 7445 54 publisher location United States issn 0021 9258 pmid 18199748 doi 10.10 ... more details
PBB geneid 57190 Selenoprotein N is a protein that in humans is encoded by the SEPN1 gene . ref name pmid10608886 cite journal author Lescure A, Gautheret D, Carbon P, Krol A title Novel selenoproteins identified in silico and in vivo by using a conserved RNA structural motif journal J Biol Chem volume 274 issue 53 pages 38147 54 year 2000 month Feb pmid 10608886 pmc doi 10.1074 jbc.274.53.38147 ref ref name entrez cite web title Entrez Gene SEPN1 selenoprotein N, 1 url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 57190 accessdate ref Function 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. Mutations in this gene cause the classical phenotype of multiminicore disease and congenital muscular dystrophy with spinal rigidity and restrictive respiratory syndrome. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene. ref name entrez Model organisms class wikitable sortable collapsible collapsed border 1 cellpadding 2 style float right Sepn1 knockout mouse phenotype Characteristic Phenotype Homozygote viability bgcolor 488ED3 Normal Fertility bgcolor 488ED3 Normal Body weight bgcolor 488ED3 Normal Open Field animal test Anxiety bgcolor 488ED3 Normal Neurological assessment bgcolor 488ED3 Normal Grip strength bgcolor 488ED3 Normal Hot plate test Hot plate bgcolor 488ED3 Normal Dysmorphology bgcolor 488ED3 Normal Indirect calorimetry bgcolor 488ED3 Normal Glucose tolerance test bgcolor 488ED3 Normal Auditory brainstem response bgcolor 488ED3 Normal Dual energy X ray absorptiometry DEXA bgcolor 488ED3 Normal Radiography bgcolor C40000 Abnormal ref name Radiograp ... more details
PBB geneid 6414 Selenoprotein P is a protein that in humans is encoded by the SEPP1 gene . ref name pmid8421687 cite journal author Hill KE, Lloyd RS, Burk RF title Conserved nucleotide sequences in the open reading frame and 3 untranslated region of selenoprotein P mRNA journal Proc Natl Acad Sci U S A volume 90 issue 2 pages 537 41 year 1993 month Feb pmid 8421687 pmc 45698 doi 10.1073 pnas.90.2.537 ref ref name entrez cite web title Entrez Gene SEPP1 selenoprotein P, plasma, 1 url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 6414 accessdate ref The PBB Summary template is automatically maintained by Protein Box Bot. See Template PBB Controls to Stop updates. PBB Summary section title summary text This gene encodes a selenoprotein containing multiple selenocysteine Sec residues, which are 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 , which is necessary for the recognition of UGA as a Sec codon rather than as a stop signal. This selenoprotein is an extracellular glycoprotein , and is unusual in that it contains 10 Sec residues per polypeptide. It is a heparin binding protein that appears to be associated with endothelial cells, and has been implicated to function as an antioxidant in the extracellular space. Several transcript variants, encoding either the same or different isoform, have been found for this gene. ref name entrez References reflist Further reading refbegin 2 PBB Further reading citations cite journal author Burk RF, Hill KE title Selenoprotein P. A selenium rich extracellular glycoprotein journal J. Nutr. volume 124 issue 10 pages 1891 7 year 1994 pmid 7931697 doi cite journal author Mostert V title Selenoprotein P properties, functions, and regulation journal Arch. Biochem. Biophys. volume 376 issue 2 pages 433 8 year 2000 pmid 10775431 doi 10.1006 abbi.2000.1735 cite journal author Hill ... more details
aging and cancer. Most known selenium dependent enzymes contain selenocysteine , a cysteine analog in which selenium replaces sulfur and which is encoded in a special manner by DNA. Selenocysteine ... more details
Creighton Of these, 20 are encoded by the universal genetic code . The remaining 2, selenocysteine and pyrrolysine , are incorporated into proteins by unique synthetic mechanisms. Selenocysteine is incorporated ... to encode selenocysteine instead of a stop codon . ref Cite journal author Driscoll DM, Copeland PR ... ref Image L selenocysteine 2D skeletal.png thumb 165px left alt The structure of selenocysteine, this differs ... hydrogen and a selenium attached. The amino acid selenocysteine Non standard amino acids Aside from ... Glutamine Tryptophan Glycine Valine Ornithine Proline Selenocysteine Serine Taurine Tyrosine Essential ... more details
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