Viperin

RSAD2
Identifiers
Aliases	RSAD2, 2510004L01Rik, cig33, cig5, vig1, radical S-adenosyl methionine domain containing 2, Viperin Protein, Viperin
External IDs	OMIM: 607810; MGI: 1929628; HomoloGene: 10969; GeneCards: RSAD2; OMA:RSAD2 - orthologs
Gene location (Human)
Chr.	Chromosome 2 (human)
End	6,898,239 bp
Gene location (Mouse)
Chr.	Chromosome 12 (mouse)
End	26,506,451 bp
RNA expression pattern
	Top expressed in
	buccal mucosa cell; ; decidua; ; monocyte; ; bronchial epithelial cell; ; palpebral conjunctiva; ; Achilles tendon; ; retinal pigment epithelium; ; trabecular bone; ; amniotic fluid; ; right uterine tube;
	Top expressed in
	blood; ; tibiofemoral joint; ; body of femur; ; spleen; ; mucous cell of stomach; ; bone marrow; ; endothelial cell of lymphatic vessel; ; lumbar spinal ganglion; ; right ventricle; ; ciliary body;
	More reference expression data
	n/a
Gene ontology
Molecular function	4 iron, 4 sulfur cluster binding; iron-sulfur cluster binding; metal ion binding; protein self-association; catalytic activity; protein binding;
Cellular component	Golgi apparatus; endoplasmic reticulum membrane; membrane; lipid droplet; mitochondrial outer membrane; endoplasmic reticulum; mitochondrion; mitochondrial inner membrane; fibrillar center;
Biological process	CD4-positive, alpha-beta T cell differentiation; CD4-positive, alpha-beta T cell activation; immune system process; response to virus; positive regulation of toll-like receptor 7 signaling pathway; negative regulation of viral genome replication; defense response to virus; type I interferon signaling pathway; positive regulation of toll-like receptor 9 signaling pathway; innate immune response; viral process; positive regulation of T-helper 2 cell cytokine production; negative regulation of protein secretion;
	Sources:Amigo / QuickGO
Orthologs
	91543
	58185
	ENSG00000134321
	ENSMUSG00000020641
	Q8WXG1
	Q8CBB9
	NM_080657
	NM_021384
	NP_542388
	NP_067359
	Wikidata
View/Edit Human	View/Edit Mouse

Radical S-adenosyl methionine domain-containing protein 2 is a protein that in humans is encoded by the RSAD2 gene. RSAD2 is a multifunctional protein in viral processes that is an interferon stimulated gene.^[5] It has been reported that viperin could be induced by either IFN-dependent or IFN-independent pathways and certain viruses may use viperin to increase their infectivity.^[6]^[7]

The protein was previously called Virus inhibitory protein, endoplasmic reticulum-associated, interferon-inducible (Viperin). The name viperin has been rectified due to inappropriate use of it to describe homologous prokaryotic enzymes producing nucleotide analogues.^[8] The enzymes across all domains of life are renamed SAM-dependent nucleotide dehydratase (SAND) using NC-IUBMB recommendations.^[8]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000134321 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000020641 – 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.
^ Seo JY, Yaneva R, Cresswell P (December 2011). "Viperin: a multifunctional, interferon-inducible protein that regulates virus replication". Cell Host & Microbe. 10 (6): 534–9. doi:10.1016/j.chom.2011.11.004. PMC 3246677. PMID 22177558.
^ Mattijssen S, Pruijn GJ (May 2012). "Viperin, a key player in the antiviral response". Microbes and Infection. 14 (5): 419–26. doi:10.1016/j.micinf.2011.11.015. hdl:2066/94161. PMID 22182524.
^ Helbig KJ, Beard MR (March 2014). "The role of viperin in the innate antiviral response". Journal of Molecular Biology. Antiviral Innate Immunity (Part II). 426 (6): 1210–9. doi:10.1016/j.jmb.2013.10.019. hdl:2440/94032. PMID 24157441.
^ ^a ^b Ji Y, Wei L, Da A, Stark H, Hagedoorn PL, Ciofi-Baffoni S, et al. (21 October 2022). "Radical-SAM dependent nucleotide dehydratase (SAND), rectification of the names of an ancient iron-sulfur enzyme using NC-IUBMB recommendations". Frontiers in Molecular Biosciences. 9: 1032220. doi:10.3389/fmolb.2022.1032220. PMC 9642334. PMID 36387278.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000134321 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000020641 – 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.

[5] Seo JY, Yaneva R, Cresswell P (December 2011). "Viperin: a multifunctional, interferon-inducible protein that regulates virus replication". Cell Host & Microbe. 10 (6): 534–9. doi:10.1016/j.chom.2011.11.004. PMC 3246677. PMID 22177558.

[Mattijssen_2012-6] Mattijssen S, Pruijn GJ (May 2012). "Viperin, a key player in the antiviral response". Microbes and Infection. 14 (5): 419–26. doi:10.1016/j.micinf.2011.11.015. hdl:2066/94161. PMID 22182524.

[Helbig_2014-7] Helbig KJ, Beard MR (March 2014). "The role of viperin in the innate antiviral response". Journal of Molecular Biology. Antiviral Innate Immunity (Part II). 426 (6): 1210–9. doi:10.1016/j.jmb.2013.10.019. hdl:2440/94032. PMID 24157441.

[Ji_2022-8] Ji Y, Wei L, Da A, Stark H, Hagedoorn PL, Ciofi-Baffoni S, et al. (21 October 2022). "Radical-SAM dependent nucleotide dehydratase (SAND), rectification of the names of an ancient iron-sulfur enzyme using NC-IUBMB recommendations". Frontiers in Molecular Biosciences. 9: 1032220. doi:10.3389/fmolb.2022.1032220. PMC 9642334. PMID 36387278.

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