SEPX1

MSRB1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	3MAO
Identifiers
Aliases	MSRB1 , SELR, SELX, SEPX1, SepR, HSPC270, methionine sulfoxide reductase B1, SELENOX, SELENOR
External IDs	OMIM: 606216 MGI: 1351642 HomoloGene: 8455 GeneCards: MSRB1
Gene location (Human)
Chr.	Chromosome 16 (human)
End	1,943,199 bp
Gene location (Mouse)
Chr.	Chromosome 17 (mouse)
End	24,961,752 bp
RNA expression pattern
	Top expressed in
	blood; ; right lobe of liver; ; body of pancreas; ; cancellous bone; ; thoracic diaphragm; ; monocyte; ; bone marrow; ; periodontal fiber; ; kidney; ; bone marrow cells;
	Top expressed in
	left lobe of liver; ; parotid gland; ; sternocleidomastoid muscle; ; temporal muscle; ; triceps brachii muscle; ; interventricular septum; ; digastric muscle; ; plantaris muscle; ; extensor digitorum longus muscle; ; myocardium of ventricle;
	More reference expression data
	n/a
Gene ontology
Molecular function	oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor ; oxidoreductase activity ; actin binding ; zinc ion binding ; metal ion binding ; methionine-R-sulfoxide reductase activity ; peptide-methionine (R)-S-oxide reductase activity ; L-methionine-(R)-S-oxide reductase activity ; protein binding ;
Cellular component	cytoplasm ; cytosol ; cytoskeleton ; nucleus ; actin cytoskeleton ; cellular component ;
Biological process	immune system process ; actin filament polymerization ; innate immune response ; response to oxidative stress ; protein repair ;
	Sources:Amigo / QuickGO
Orthologs
	51734
	27361
	ENSG00000198736
	ENSMUSG00000075705
	Q9NZV6
	Q9JLC3
	NM_016332 ; NM_001382264 ; NM_001382265
	NM_013759 ; NM_001346668
	NP_057416 ; NP_001369193 ; NP_001369194
	NP_001333597 ; NP_038787
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated October 29, 2022

Methionine-R-sulfoxide reductase B1 is an enzyme that in humans is encoded by the SEPX1 gene.^[5]^[6]

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. This protein belongs to the methionine sulfoxide reductase B (MsrB) family, and it is expressed in a variety of adult and fetal tissues.^[6]

Related Research Articles

<span class="mw-page-title-main">Selenocysteine</span> Chemical compound

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.

<span class="mw-page-title-main">SECIS element</span> RNA sequence directing the translation of UGA codons as selenocysteines

In biology, the SECIS element is an RNA element around 60 nucleotides in length that adopts a stem-loop structure. This structural motif directs the cell to translate UGA codons as selenocysteines. SECIS elements are thus a fundamental aspect of messenger RNAs encoding selenoproteins, proteins that include one or more selenocysteine residues.

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.

Selenoprotein S, also known as SELS, is a human gene.

Selenide, water dikinase 1 is an enzyme that in humans is encoded by the SEPHS1 gene.

Cytochrome b-c1 complex subunit 1, mitochondrial is a protein that in humans is encoded by the UQCRC1 gene.

Selenoprotein N is a protein that in humans is encoded by the SEPN1 gene.

SECIS-binding protein 2 is a protein that in humans is encoded by the SECISBP2 gene.

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

Peptide methionine sulfoxide reductase (Msr) is a family of enzymes that in humans is encoded by the MSRA gene.

40S ribosomal protein S11 is a protein that in humans is encoded by the RPS11 gene.

Methionine aminopeptidase 1 is an enzyme that in humans is encoded by the METAP1 gene.

Selenoprotein W is a protein that in humans is encoded by the SEPW1 gene.

Methionine-R-sulfoxide reductase B2, mitochondrial is an enzyme that in humans is encoded by the MSRB2 gene. The MRSB2 enzyme catalyzes the reduction of methionine sulfoxide to methionine.

Zinc finger protein 346 is a protein that in humans is encoded by the ZNF346 gene.

Type II iodothyronine deiodinase is an enzyme that in humans is encoded by the DIO2 gene.

Cob(I)yrinic acid a,c-diamide adenosyltransferase, mitochondrial is an enzyme that in humans is encoded by the MMAB gene.

Selenoprotein T, also known as SELT, is a protein that in humans is encoded by the SELT gene.

Glutathione peroxidase 5 (GPx-5), also known as epididymal secretory glutathione peroxidase is an enzyme that in humans is encoded by the GPX5 gene.

Glutathione peroxidase 6 (GPx-6) is an enzyme that in humans is encoded by the GPX6 gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000198736 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000075705 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Lescure A, Gautheret D, Carbon P, Krol A (Feb 2000). "Novel selenoproteins identified in silico and in vivo by using a conserved RNA structural motif". J Biol Chem. 274 (53): 38147–54. doi: 10.1074/jbc.274.53.38147 . PMID 10608886.
1 2 "Entrez Gene: SEPX1 selenoprotein X, 1".

Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi: 10.1101/gr.6.9.791 . PMID 8889548.
Kryukov GV, Kryukov VM, Gladyshev VN (1999). "New mammalian selenocysteine-containing proteins identified with an algorithm that searches for selenocysteine insertion sequence elements". J. Biol. Chem. 274 (48): 33888–97. doi: 10.1074/jbc.274.48.33888 . PMID 10567350.
Zhang QH, Ye M, Wu XY, et al. (2001). "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells". Genome Res. 10 (10): 1546–60. doi:10.1101/gr.140200. PMC 310934 . PMID 11042152.
Daniels RJ, Peden JF, Lloyd C, et al. (2001). "Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16". Hum. Mol. Genet. 10 (4): 339–52. doi: 10.1093/hmg/10.4.339 . PMID 11157797.
Moskovitz J, Singh VK, Requena J, et al. (2002). "Purification and characterization of methionine sulfoxide reductases from mouse and Staphylococcus aureus and their substrate stereospecificity". Biochem. Biophys. Res. Commun. 290 (1): 62–5. doi:10.1006/bbrc.2001.6171. PMID 11779133.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC 139241 . PMID 12477932.
Kim HY, Gladyshev VN (2004). "Methionine sulfoxide reduction in mammals: characterization of methionine-R-sulfoxide reductases". Mol. Biol. Cell. 15 (3): 1055–64. doi:10.1091/mbc.E03-08-0629. PMC 363075 . PMID 14699060.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928 . PMID 15489334.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000198736 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000075705 - Ensembl, 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.

[pmid10608886-5] Lescure A, Gautheret D, Carbon P, Krol A (Feb 2000). "Novel selenoproteins identified in silico and in vivo by using a conserved RNA structural motif". J Biol Chem. 274 (53): 38147–54. doi: 10.1074/jbc.274.53.38147 . PMID 10608886.

[entrez-6] 1 2 "Entrez Gene: SEPX1 selenoprotein X, 1".

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SEPX1

Contents

See also

Related Research Articles

References

Further reading