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SEP15

From Wikipedia, the free encyclopedia
Protein-coding gene in the species Homo sapiens
SELENOF
Identifiers
AliasesSELENOF, selenoprotein F, SEP15
External IDsOMIM:606254;MGI:1927947;HomoloGene:3145;GeneCards:SELENOF;OMA:SELENOF - orthologs
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for SELENOF
Genomic location for SELENOF
Band1p22.3Start86,862,445bp[1]
End86,914,424bp[1]
Gene location (Mouse)
Chromosome 3 (mouse)
Chr.Chromosome 3 (mouse)[2]
Chromosome 3 (mouse)
Genomic location for SELENOF
Genomic location for SELENOF
Band3|3 H2Start144,276,065bp[2]
End144,303,441bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • islet of Langerhans

  • retinal pigment epithelium

  • corpus epididymis

  • seminal vesicula

  • monocyte

  • stromal cell of endometrium

  • caput epididymis

  • gallbladder

  • epithelium of nasopharynx

  • mucosa of paranasal sinus
Top expressed in
  • seminal vesicula

  • parotid gland

  • optic nerve

  • right lung lobe

  • molar

  • olfactory epithelium

  • stroma of bone marrow

  • lobe of prostate

  • right kidney

  • median eminence
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo /QuickGO
Orthologs
SpeciesHumanMouse
Entrez

9403

93684

Ensembl

ENSG00000183291

ENSMUSG00000037072

UniProt

O60613

Q9ERR7

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 aprotein that in humans is encoded by theSEP15gene.[5] Two alternatively spliced transcript variants encoding distinctisoforms have been found for this gene.

Function

[edit]

This gene encodes aselenoprotein, which contains aselenocysteine (Sec) residue at its active site. The selenocysteine is encoded by theUGAcodon that normally signals translation termination. The 3' UTR of selenoprotein genes have a commonstem-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 haveredox function and may be involved in the quality control ofprotein 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]
Protein family
Sep15
Solution structure of SelM fromMus 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 calledSep15 however in the case ofmice, it is namedSelM. This protein is aselenoprotein only found ineukaryotes. This domain has athioredoxin-likedomain and a surface accessibleactive siteredoxmotif.[6] This suggests that they function as thiol-disulfideisomerases involved in disulfidebond formation in theendoplasmic reticulum.[6]

Function

[edit]

Recent studies have shown in mice, where the SEP15 gene has beensilenced 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 threealpha helices and a mixed parallel/anti-parallel four-strandedbeta-sheet.[6]

References

[edit]
  1. ^abcGRCh38: Ensembl release 89: ENSG00000183291Ensembl, May 2017
  2. ^abcGRCm38: 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. ^abc"Entrez Gene: SEP15 15 kDa selenoprotein".
  6. ^abcFerguson 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]


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