Jump to content

SEP15

From Wikipedia, the free encyclopedia
SELENOF
Identifiers
AliasesSELENOF, selenoprotein F, SEP15
External IDsOMIM: 606254; MGI: 1927947; HomoloGene: 3145; GeneCards: SELENOF; OMA:SELENOF - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_004261
NM_203341

NM_053102

RefSeq (protein)

NP_004252
NP_976086

NP_444332

Location (UCSC)Chr 1: 86.86 – 86.91 MbChr 3: 144.28 – 144.3 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

15 kDa selenoprotein is a protein that in humans is encoded by the SEP15 gene.[5] Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.

Function

[edit]

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.[5]

Clinical significance

[edit]

This gene is localized on chromosome 1p31, a genetic locus commonly mutated or deleted in human cancers.[5]

Protein domain

[edit]
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 a selenoprotein only found in eukaryotes. This domain has a thioredoxin-like domain and a surface accessible active site redox motif.[6] This suggests that they function as thiol-disulfide isomerases involved in disulfide bond formation in the endoplasmic reticulum.[6]

Function

[edit]

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.[7]

Structure

[edit]

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.[6]

References

[edit]
  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000183291Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000037072Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b c "Entrez Gene: SEP15 15 kDa selenoprotein".
  6. ^ 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". The Journal of Biological Chemistry. 281 (6): 3536–43. doi:10.1074/jbc.M511386200. PMID 16319061.
  7. ^ 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

[edit]