Jump to content

SEP15

From Wikipedia, the free encyclopedia

This is an old revision of this page, as edited by OAbot (talk | contribs) at 07:46, 16 April 2020 (Open access bot: doi added to citation with #oabot.). The present address (URL) is a permanent link to this revision, which may differ significantly from the current revision.

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

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

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

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 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

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

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

  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.{{cite journal}}: CS1 maint: unflagged free DOI (link)

Further reading