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SEP15

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Template:PBB 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
Solution structure of SelM from Mus musculus
Identifiers
SymbolSep15_SelM
PfamPF08806
InterProIPR014912
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

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. ^ a b c "Entrez Gene: SEP15 15 kDa selenoprotein".
  2. ^ a b c 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". J. Biol. Chem. 281 (6): 3536–43. doi:10.1074/jbc.M511386200. PMID 16319061.{{cite journal}}: CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link)
  3. ^ Tsuji PA, Naranjo-Suarez S, Carlson BA, Tobe R, Yoo MH, Davis CD (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.{{cite journal}}: CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link)

Further reading


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