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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''15 kDa selenoprotein''' is a [[protein]] that in humans is encoded by the ''SEP15'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SEP15 15 kDa selenoprotein| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9403| accessdate = }}</ref> Two alternatively spliced transcript variants encoding distinct [[isoforms]] have been found for this gene.
| update_page = yes
 
| require_manual_inspection = no
== Function ==
| update_protein_box = yes
 
| update_summary = yes
This gene encodes a [[selenoprotein]], which contains a [[selenocysteine]] (Sec) residue at its active site. The selenocysteine is encoded by the [[Stop-codon|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]].<ref name="entrez" />
| update_citations = yes
 
== Clinical significance ==
 
This gene is localized on chromosome 1p31, a genetic locus commonly mutated or deleted in human cancers.<ref name="entrez" />
 
==Protein domain==
{{Infobox protein family
| Symbol = Sep15_SelM
| Name = Sep15
| image = PDB 2a2p EBI.jpg
| width =
| caption = Solution structure of SelM from ''Mus musculus''
| Pfam = PF08806
| Pfam_clan = 
| InterPro = IPR014912
| SMART =
| PROSITE =
| MEROPS =
| SCOP =
| TCDB =  
| OPM family =  
| OPM protein =  
| CAZy =  
| CDD =  
}}
}}
The protein this gene encodes for is often called '''Sep15''' however in the case of [[Mus musculus|mice]], it is named '''SelM'''. This protein is an [[selenoprotein]] only found in [[eukaryotes]]. This domain has a  [[thioredoxin]]-like [[Domain (biology)|domain]] and a surface accessible [[active site]] [[redox]] [[protein motif|motif]].<ref name="pmid16319061">{{cite journal | vauthors = Ferguson AD, Labunskyy VM, Fomenko DE, Araç D, Chelliah Y, Amezcua CA, Rizo J, Gladyshev VN, Deisenhofer J | title = NMR structures of the selenoproteins Sep15 and SelM reveal redox activity of a new thioredoxin-like family | journal = The Journal of Biological Chemistry | volume = 281 | issue = 6 | pages = 3536–43 | date = February 2006 | pmid = 16319061 | doi = 10.1074/jbc.M511386200 }}</ref> This suggests that they function as thiol-[[disulfide]] [[isomerase]]s involved in disulfide [[Chemical bond|bond]] formation in the [[endoplasmic reticulum]].<ref name="pmid16319061"/>
=== Function ===
Recent studies have shown in mice, where the SEP15 gene has been [[gene silencing|silenced]] the mice subsequently became deficient in SEP15 and were able to inhibit the development of colorectal cancer.<ref name="pmid22254125">{{cite journal | vauthors = Tsuji PA, Naranjo-Suarez S, Carlson BA, Tobe R, Yoo MH, Davis CD | title = Deficiency in the 15 kDa selenoprotein inhibits human colon cancer cell growth | journal = Nutrients | volume = 3 | issue = 9 | pages = 805–17 | date = September 2011 | pmid = 22254125 | pmc = 3257736 | doi = 10.3390/nu3090805 }}</ref>


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
===Structure===
{{GNF_Protein_box
The particular structure has an alpha/beta central domain which is actually made up of three [[alpha helix|alpha helices]] and a mixed parallel/anti-parallel four-stranded [[beta-sheet]].<ref name="pmid16319061" />
| image =
| image_source =
| PDB =  
| Name = 15 kDa selenoprotein
| HGNCid =
| Symbol = SEP15
| AltSymbols =;
| OMIM = 606254
| ECnumber = 
| Homologene = 3145
| MGIid = 1927947
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008430 |text = selenium binding}}
| Component = {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005788 |text = endoplasmic reticulum lumen}}
| Process = {{GNF_GO|id=GO:0051084 |text = posttranslational protein folding}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 9403
    | Hs_Ensembl = 
    | Hs_RefseqProtein = NP_004252
    | Hs_RefseqmRNA = NM_004261
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 
    | Hs_GenLoc_start = 
    | Hs_GenLoc_end = 
    | Hs_Uniprot = 
    | Mm_EntrezGene = 93684
    | Mm_Ensembl = ENSMUSG00000037072
    | Mm_RefseqmRNA = NM_053102
    | Mm_RefseqProtein = NP_444332
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 3
    | Mm_GenLoc_start = 144508111
    | Mm_GenLoc_end = 144534340
    | Mm_Uniprot = Q3TXW1
  }}
}}
'''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. -->
== References ==
{{PBB_Summary
{{reflist}}
| 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">{{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>
}}


==References==
== Further reading ==
{{reflist|2}}
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = 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 = 171–4 | date = January 1994 | pmid = 8125298 | doi = 10.1016/0378-1119(94)90802-8 }}
| citations =
* {{cite journal | vauthors = Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S | title = Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library | journal = Gene | volume = 200 | issue = 1-2 | pages = 149–56 | date = October 1997 | pmid = 9373149 | doi = 10.1016/S0378-1119(97)00411-3 }}
*{{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= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
* {{cite journal | vauthors = Gladyshev VN, Jeang KT, Wootton JC, Hatfield DL | title = A new human selenium-containing protein. Purification, characterization, and cDNA sequence | journal = The Journal of Biological Chemistry | volume = 273 | issue = 15 | pages = 8910–5 | date = April 1998 | pmid = 9535873 | doi = 10.1074/jbc.273.15.8910 }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
* {{cite journal | vauthors = Kumaraswamy E, Malykh A, Korotkov KV, Kozyavkin S, Hu Y, Kwon SY, Moustafa ME, Carlson BA, Berry MJ, Lee BJ, Hatfield DL, Diamond AM, Gladyshev VN | title = Structure-expression relationships of the 15-kDa selenoprotein gene. Possible role of the protein in cancer etiology | journal = The Journal of Biological Chemistry | volume = 275 | issue = 45 | pages = 35540–7 | date = November 2000 | pmid = 10945981 | doi = 10.1074/jbc.M004014200 }}
*{{cite journal | author=Gladyshev VN, Jeang KT, Wootton JC, Hatfield DL |title=A new human selenium-containing protein. Purification, characterization, and cDNA sequence. |journal=J. Biol. Chem. |volume=273 |issue= 15 |pages= 8910-5 |year= 1998 |pmid= 9535873 |doi= }}
* {{cite journal | vauthors = Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Böcher M, Blöcker H, Bauersachs S, Blum H, Lauber J, Düsterhöft A, Beyer A, Köhrer K, Strack N, Mewes HW, Ottenwälder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A | title = Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs | journal = Genome Research | volume = 11 | issue = 3 | pages = 422–35 | date = March 2001 | pmid = 11230166 | pmc = 311072 | doi = 10.1101/gr.GR1547R }}
*{{cite journal | author=Kumaraswamy E, Malykh A, Korotkov KV, ''et al.'' |title=Structure-expression relationships of the 15-kDa selenoprotein gene. Possible role of the protein in cancer etiology. |journal=J. Biol. Chem. |volume=275 |issue= 45 |pages= 35540-7 |year= 2001 |pmid= 10945981 |doi= 10.1074/jbc.M004014200 }}
* {{cite journal | vauthors = Korotkov KV, Kumaraswamy E, Zhou Y, Hatfield DL, Gladyshev VN | title = Association between the 15-kDa selenoprotein and UDP-glucose:glycoprotein glucosyltransferase in the endoplasmic reticulum of mammalian cells | journal = The Journal of Biological Chemistry | volume = 276 | issue = 18 | pages = 15330–6 | date = May 2001 | pmid = 11278576 | doi = 10.1074/jbc.M009861200 }}
*{{cite journal | author=Wiemann S, Weil B, Wellenreuther R, ''et al.'' |title=Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. |journal=Genome Res. |volume=11 |issue= 3 |pages= 422-35 |year= 2001 |pmid= 11230166 |doi= 10.1101/gr.154701 }}
* {{cite journal | vauthors = Kumaraswamy E, Korotkov KV, Diamond AM, Gladyshev VN, Hatfield DL | title = Genetic and functional analysis of mammalian Sep15 selenoprotein | journal = Methods in Enzymology | volume = 347 | issue =  | pages = 187–97 | year = 2002 | pmid = 11898406 | doi = 10.1016/S0076-6879(02)47017-6 | isbn = 978-0-12-182248-4 | series = Methods in Enzymology }}
*{{cite journal | author=Korotkov KV, Kumaraswamy E, Zhou Y, ''et al.'' |title=Association between the 15-kDa selenoprotein and UDP-glucose:glycoprotein glucosyltransferase in the endoplasmic reticulum of mammalian cells. |journal=J. Biol. Chem. |volume=276 |issue= 18 |pages= 15330-6 |year= 2001 |pmid= 11278576 |doi= 10.1074/jbc.M009861200 }}
* {{cite journal | vauthors = Wu HJ, Lin C, Zha YY, Yang JG, Zhang MC, Zhang XY, Liang X, Fu M, Wu M | title = [Redox reactions of Sep15 and its relationship with tumor development] | journal = Ai Zheng = Aizheng = Chinese Journal of Cancer | volume = 22 | issue = 2 | pages = 119–22 | date = February 2003 | pmid = 12600282 | doi =  }}
*{{cite journal | author=Kumaraswamy E, Korotkov KV, Diamond AM, ''et al.'' |title=Genetic and functional analysis of mammalian Sep15 selenoprotein. |journal=Meth. Enzymol. |volume=347 |issue=  |pages= 187-97 |year= 2002 |pmid= 11898406 |doi= }}
* {{cite journal | vauthors = Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J | title = Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides | journal = Nature Biotechnology | volume = 21 | issue = 5 | pages = 566–9 | date = May 2003 | pmid = 12665801 | doi = 10.1038/nbt810 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
* {{cite journal | vauthors = Apostolou S, Klein JO, Mitsuuchi Y, Shetler JN, Poulikakos PI, Jhanwar SC, Kruger WD, Testa JR | title = Growth inhibition and induction of apoptosis in mesothelioma cells by selenium and dependence on selenoprotein SEP15 genotype | journal = Oncogene | volume = 23 | issue = 29 | pages = 5032–40 | date = June 2004 | pmid = 15107826 | doi = 10.1038/sj.onc.1207683 }}
*{{cite journal | author=Wu HJ, Lin C, Zha YY, ''et al.'' |title=[Redox reactions of Sep15 and its relationship with tumor development] |journal=Ai Zheng |volume=22 |issue= 2 |pages= 119-22 |year= 2003 |pmid= 12600282 |doi=  }}
* {{cite journal | vauthors = Wellenreuther R, Schupp I, Poustka A, Wiemann S | title = SMART amplification combined with cDNA size fractionation in order to obtain large full-length clones | journal = BMC Genomics | volume = 5 | issue = 1 | pages = 36 | date = June 2004 | pmid = 15198809 | pmc = 436056 | doi = 10.1186/1471-2164-5-36 }}
*{{cite journal | author=Gevaert K, Goethals M, Martens L, ''et al.'' |title=Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. |journal=Nat. Biotechnol. |volume=21 |issue= 5 |pages= 566-9 |year= 2004 |pmid= 12665801 |doi= 10.1038/nbt810 }}
*{{cite journal | author=Apostolou S, Klein JO, Mitsuuchi Y, ''et al.'' |title=Growth inhibition and induction of apoptosis in mesothelioma cells by selenium and dependence on selenoprotein SEP15 genotype. |journal=Oncogene |volume=23 |issue= 29 |pages= 5032-40 |year= 2004 |pmid= 15107826 |doi= 10.1038/sj.onc.1207683 }}
*{{cite journal | author=Wellenreuther R, Schupp I, Poustka A, ''et al.'' |title=SMART amplification combined with cDNA size fractionation in order to obtain large full-length clones. |journal=BMC Genomics |volume=5 |issue= 1 |pages= 36 |year= 2004 |pmid= 15198809 |doi= 10.1186/1471-2164-5-36 }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | author=Gregory SG, Barlow KF, McLay KE, ''et al.'' |title=The DNA sequence and biological annotation of human chromosome 1. |journal=Nature |volume=441 |issue= 7091 |pages= 315-21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727 }}
}}
{{refend}}
{{refend}}
[[Category:Selenoproteins]]


{{protein-stub}}
{{protein-stub}}
{{WikiDoc Sources}}

Latest revision as of 02:31, 27 October 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

15 kDa selenoprotein is a protein that in humans is encoded by the SEP15 gene.[1] Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.

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. Studies in mouse suggest that this selenoprotein may have redox function and may be involved in the quality control of protein folding.[1]

Clinical significance

This gene is localized on chromosome 1p31, a genetic locus commonly mutated or deleted in human cancers.[1]

Protein domain

Sep15
File:PDB 2a2p EBI.jpg
Solution structure of SelM from Mus musculus
Identifiers
SymbolSep15_SelM
PfamPF08806
InterProIPR014912

The protein this gene encodes for is often called Sep15 however in the case of mice, it is named SelM. This protein is an selenoprotein only found in eukaryotes. This domain has a thioredoxin-like domain and a surface accessible active site redox motif.[2] This suggests that they function as thiol-disulfide isomerases involved in disulfide bond formation in the endoplasmic reticulum.[2]

Function

Recent studies have shown in mice, where the SEP15 gene has been silenced the mice subsequently became deficient in SEP15 and were able to inhibit the development of colorectal cancer.[3]

Structure

The particular structure has an alpha/beta central domain which is actually made up of three alpha helices and a mixed parallel/anti-parallel four-stranded beta-sheet.[2]

References

  1. ↑ 1.0 1.1 1.2 "Entrez Gene: SEP15 15 kDa selenoprotein".
  2. ↑ 2.0 2.1 2.2 Ferguson AD, Labunskyy VM, Fomenko DE, Araç D, Chelliah Y, Amezcua CA, Rizo J, Gladyshev VN, Deisenhofer J (February 2006). "NMR structures of the selenoproteins Sep15 and SelM reveal redox activity of a new thioredoxin-like family". The Journal of Biological Chemistry. 281 (6): 3536–43. doi:10.1074/jbc.M511386200. PMID 16319061.
  3. ↑ Tsuji PA, Naranjo-Suarez S, Carlson BA, Tobe R, Yoo MH, Davis CD (September 2011). "Deficiency in the 15 kDa selenoprotein inhibits human colon cancer cell growth". Nutrients. 3 (9): 805–17. doi:10.3390/nu3090805. PMC 3257736. PMID 22254125.

Further reading

  • Maruyama K, Sugano S (January 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.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 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.
  • Gladyshev VN, Jeang KT, Wootton JC, Hatfield DL (April 1998). "A new human selenium-containing protein. Purification, characterization, and cDNA sequence". The Journal of Biological Chemistry. 273 (15): 8910–5. doi:10.1074/jbc.273.15.8910. PMID 9535873.
  • Kumaraswamy E, Malykh A, Korotkov KV, Kozyavkin S, Hu Y, Kwon SY, Moustafa ME, Carlson BA, Berry MJ, Lee BJ, Hatfield DL, Diamond AM, Gladyshev VN (November 2000). "Structure-expression relationships of the 15-kDa selenoprotein gene. Possible role of the protein in cancer etiology". The Journal of Biological Chemistry. 275 (45): 35540–7. doi:10.1074/jbc.M004014200. PMID 10945981.
  • Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Böcher M, Blöcker H, Bauersachs S, Blum H, Lauber J, Düsterhöft A, Beyer A, Köhrer K, Strack N, Mewes HW, Ottenwälder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A (March 2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome Research. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
  • Korotkov KV, Kumaraswamy E, Zhou Y, Hatfield DL, Gladyshev VN (May 2001). "Association between the 15-kDa selenoprotein and UDP-glucose:glycoprotein glucosyltransferase in the endoplasmic reticulum of mammalian cells". The Journal of Biological Chemistry. 276 (18): 15330–6. doi:10.1074/jbc.M009861200. PMID 11278576.
  • Kumaraswamy E, Korotkov KV, Diamond AM, Gladyshev VN, Hatfield DL (2002). "Genetic and functional analysis of mammalian Sep15 selenoprotein". Methods in Enzymology. Methods in Enzymology. 347: 187–97. doi:10.1016/S0076-6879(02)47017-6. ISBN 978-0-12-182248-4. PMID 11898406.
  • Wu HJ, Lin C, Zha YY, Yang JG, Zhang MC, Zhang XY, Liang X, Fu M, Wu M (February 2003). "[Redox reactions of Sep15 and its relationship with tumor development]". Ai Zheng = Aizheng = Chinese Journal of Cancer. 22 (2): 119–22. PMID 12600282.
  • Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J (May 2003). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nature Biotechnology. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801.
  • Apostolou S, Klein JO, Mitsuuchi Y, Shetler JN, Poulikakos PI, Jhanwar SC, Kruger WD, Testa JR (June 2004). "Growth inhibition and induction of apoptosis in mesothelioma cells by selenium and dependence on selenoprotein SEP15 genotype". Oncogene. 23 (29): 5032–40. doi:10.1038/sj.onc.1207683. PMID 15107826.
  • Wellenreuther R, Schupp I, Poustka A, Wiemann S (June 2004). "SMART amplification combined with cDNA size fractionation in order to obtain large full-length clones". BMC Genomics. 5 (1): 36. doi:10.1186/1471-2164-5-36. PMC 436056. PMID 15198809.
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