| SELENOF | |||||||||||||||||||||||||||||||||||||||||||||||||||
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| Identifiers | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Aliases | SELENOF , selenoprotein F, SEP15 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 606254 MGI: 1927947 HomoloGene: 3145 GeneCards: SELENOF | ||||||||||||||||||||||||||||||||||||||||||||||||||
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| Wikidata | |||||||||||||||||||||||||||||||||||||||||||||||||||
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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.
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]
This gene is localized on chromosome 1p31, a genetic locus commonly mutated or deleted in human cancers. [5]
| Sep15 | |||||||||
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 Solution structure of SelM from Mus musculus | |||||||||
| Identifiers | |||||||||
| Symbol | Sep15_SelM | ||||||||
| Pfam | PF08806 | ||||||||
| InterPro | IPR014912 | ||||||||
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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]
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]
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]
Selenocysteine is the 21st proteinogenic amino acid. Selenoproteins contain selenocysteine residues. Selenocysteine is an analogue of the more common cysteine with selenium in place of the sulfur.
In molecular biology a selenoprotein is any protein that includes a selenocysteine amino acid residue. Among functionally characterized selenoproteins are five glutathione peroxidases (GPX) and three thioredoxin reductases, (TrxR/TXNRD) which both contain only one Sec. Selenoprotein P is the most common selenoprotein found in the plasma. It is unusual because in humans it contains 10 Sec residues, which are split into two domains, a longer N-terminal domain that contains 1 Sec, and a shorter C-terminal domain that contains 9 Sec. The longer N-terminal domain is likely an enzymatic domain, and the shorter C-terminal domain is likely a means of safely transporting the very reactive selenium atom throughout the body.
Glutathione peroxidase 1, also known as GPx1, is an enzyme that in humans is encoded by the GPX1 gene on chromosome 3. This gene encodes a member of the glutathione peroxidase family. Glutathione peroxidase functions in the detoxification of hydrogen peroxide, and is one of the most important antioxidant enzymes in humans.
The enzyme selenocysteine lyase (SCL) (EC 4.4.1.16) catalyzes the chemical reaction
Peroxiredoxin-1 is a protein that in humans is encoded by the PRDX1 gene.
Kv channel-interacting protein 2 also known as KChIP2 is a protein that in humans is encoded by the KCNIP2 gene.
Thioredoxin-interacting protein is a protein that in humans is encoded by the TXNIP gene.
Selenoprotein S, also known as SELS, is a human gene.
Endoplasmic reticulum protein 29 (ERp29) is a chaperone protein that in humans is encoded by the ERP29 gene.
Selenide, water dikinase 1 is an enzyme that in humans is encoded by the SEPHS1 gene.
ERO1-like protein alpha is a protein that in humans is encoded by the ERO1L gene.
Voltage-gated potassium channel subunit beta-1 is a protein that in humans is encoded by the KCNAB1 gene.
Glutaredoxin 2 (GLRX2) is an enzyme that in humans encoded by the GLRX2 gene. GLRX2, also known as GRX2, is a glutaredoxin family protein and a thiol-disulfide oxidoreductase that maintains cellular thiol homeostasis. This gene consists of four exons and three introns, spanned 10 kilobase pairs, and localized to chromosome 1q31.2–31.3.
Thioredoxin domain-containing protein 5 is a protein that in humans is encoded by the TXNDC5 gene.
Methionine-R-sulfoxide reductase B1 is an enzyme that in humans is encoded by the SEPX1 gene.
Thioredoxin, mitochondrial also known as thioredoxin-2 is a protein that in humans is encoded by the TXN2 gene on chromosome 22. This nuclear gene encodes a mitochondrial member of the thioredoxin family, a group of small multifunctional redox-active proteins. The encoded protein may play important roles in the regulation of the mitochondrial membrane potential and in protection against oxidant-induced apoptosis.
O-phosphoseryl-tRNA(Sec) selenium transferase is an enzyme that in humans is encoded by the SEPSECS gene.
Selenoprotein T, also known as SELT, is a protein that in humans is encoded by the SELT gene.
In molecular biology, the protein domain selenoprotein P (SelP) is the only known eukaryotic selenoprotein that contains multiple selenocysteine (Sec) residues. It is a secreted glycoprotein, often found in the plasma. Its precise function remains to be elucidated; however, it is thought to have antioxidant properties. This particular protein contains two domains: the C terminal and N terminal domain. The N-terminal domain is larger than the C terminal and the N-terminal is thought to be glycosylated.
Protein disulfide isomerase family A member 2 is a protein that in humans is encoded by the PDIA2 gene.
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