RC3H1

RC3H1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3X1O, 4QIK, 4QIL, 4ULW, 4YWQ
Identifiers
Aliases	RC3H1, RNF198, ROQUIN, ring finger and CCCH-type domains 1
External IDs	MGI: 2685397 HomoloGene: 19036 GeneCards: RC3H1
Gene ontology Molecular function • ubiquitin protein ligase activity • zinc ion binding • metal ion binding • RNA binding • poly(A) RNA binding • mRNA binding • RNA stem-loop binding • mRNA 3'-UTR binding Cellular component • cytoplasm • P-body • cytoplasmic stress granule Biological process • regulation of T cell proliferation • regulation of T cell activation • B cell homeostasis • spleen development • positive regulation of NIK/NF-kappaB signaling • T cell homeostasis • T cell proliferation • regulation of gene expression • lymph node development • T follicular helper cell differentiation • negative regulation of T-helper cell differentiation • regulation of mRNA stability • positive regulation of mRNA catabolic process • regulation of germinal center formation • posttranscriptional regulation of gene expression • negative regulation of germinal center formation • negative regulation of B cell proliferation • cellular response to interleukin-1 • protein ubiquitination • nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay • cytoplasmic mRNA processing body assembly • regulation of T cell receptor signaling pathway • nuclear-transcribed mRNA catabolic process • negative regulation of activated T cell proliferation • 3'-UTR-mediated mRNA destabilization Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	149041	381305
Ensembl	ENSG00000135870	ENSMUSG00000040423
UniProt	Q5TC82	Q4VGL6
RefSeq (mRNA)	NM_001300850 NM_001300851 NM_001300852 NM_172071	NM_001024952
RefSeq (protein)	NP_001287779.1 NP_001287780.1 NP_001287781.1 NP_742068.1 NP_001287779.1	NP_001020123.1
Location (UCSC)	Chr 1: 173.93 – 174.02 Mb	Chr 1: 160.91 – 160.97 Mb
PubMed search	[1]	[2]
Wikidata

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Ring finger and CCCH-type domains 1, also known as Roquin-1, is a protein that in humans is encoded by the RC3H1 gene. ^[3]

Function

The consensus primary sequence and secondary structure for the Roquin-1 (RC3H1) binding site (also called constitutive decay element (CDE)).

This gene encodes a protein containing RING-type and C3H1-type zinc finger motifs. The encoded protein recognizes and binds to a constitutive decay element (CDE) in the 3' UTR of mRNAs, leading to mRNA deadenylation and degradation. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jul 2014].

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. "Entrez Gene: Ring finger and CCCH-type domains 1". Retrieved 2014-10-08.

Further reading

• Bertossi, A; Aichinger, M; Sansonetti, P; Lech, M; Neff, F; Pal, M; Wunderlich, F. T.; Anders, H. J.; Klein, L; Schmidt-Supprian, M (2011). "Loss of Roquin induces early death and immune deregulation but not autoimmunity". Journal of Experimental Medicine. 208 (9): 1749–56. doi:10.1084/jem.20110578. PMC 3171092. PMID 21844204.
• Leppek, K; Schott, J; Reitter, S; Poetz, F; Hammond, M. C.; Stoecklin, G (2013). "Roquin promotes constitutive mRNA decay via a conserved class of stem-loop recognition motifs". Cell. 153 (4): 869–81. doi:10.1016/j.cell.2013.04.016. PMID 23663784.
• Heissmeyer, V; Vogel, K. U. (2013). "Molecular control of Tfh-cell differentiation by Roquin family proteins". Immunological Reviews. 253 (1): 273–89. doi:10.1111/imr.12056. PMID 23550652.
• Chang, P. P.; Lee, S. K.; Hu, X; Davey, G; Duan, G; Cho, J. H.; Karupiah, G; Sprent, J; Heath, W. R.; Bertram, E. M.; Vinuesa, C. G. (2012). "Breakdown in repression of IFN-γ mRNA leads to accumulation of self-reactive effector CD8+ T cells". The Journal of Immunology. 189 (2): 701–10. doi:10.4049/jimmunol.1102432. PMID 22685317.
• Athanasopoulos, V; Barker, A; Yu, D; Tan, A. H.; Srivastava, M; Contreras, N; Wang, J; Lam, K. P.; Brown, S. H.; Goodnow, C. C.; Dixon, N. E.; Leedman, P. J.; Saint, R; Vinuesa, C. G. (2010). "The ROQUIN family of proteins localizes to stress granules via the ROQ domain and binds target mRNAs". FEBS Journal. 277 (9): 2109–27. doi:10.1111/j.1742-4658.2010.07628.x. PMID 20412057.
• Yu, D; Tan, A. H.; Hu, X; Athanasopoulos, V; Simpson, N; Silva, D. G.; Hutloff, A; Giles, K. M.; Leedman, P. J.; Lam, K. P.; Goodnow, C. C.; Vinuesa, C. G. (2007). "Roquin represses autoimmunity by limiting inducible T-cell co-stimulator messenger RNA". Nature. 450 (7167): 299–303. doi:10.1038/nature06253. PMID 18172933.
• Pratama, A; Ramiscal, R. R.; Silva, D. G.; Das, S. K.; Athanasopoulos, V; Fitch, J; Botelho, N. K.; Chang, P. P.; Hu, X; Hogan, J. J.; Maña, P; Bernal, D; Korner, H; Yu, D; Goodnow, C. C.; Cook, M. C.; Vinuesa, C. G. (2013). "Roquin-2 shares functions with its paralog Roquin-1 in the repression of mRNAs controlling T follicular helper cells and systemic inflammation". Immunity. 38 (4): 669–80. doi:10.1016/j.immuni.2013.01.011. PMID 23583642.
• Vinuesa, C. G.; Cook, M. C.; Angelucci, C; Athanasopoulos, V; Rui, L; Hill, K. M.; Yu, D; Domaschenz, H; Whittle, B; Lambe, T; Roberts, I. S.; Copley, R. R.; Bell, J. I.; Cornall, R. J.; Goodnow, C. C. (2005). "A RING-type ubiquitin ligase family member required to repress follicular helper T cells and autoimmunity". Nature. 435 (7041): 452–8. doi:10.1038/nature03555. PMID 15917799.
• Linterman, M. A.; Rigby, R. J.; Wong, R; Silva, D; Withers, D; Anderson, G; Verma, N. K.; Brink, R; Hutloff, A; Goodnow, C. C.; Vinuesa, C. G. (2009). "Roquin differentiates the specialized functions of duplicated T cell costimulatory receptor genes CD28 and ICOS". Immunity. 30 (2): 228–41. doi:10.1016/j.immuni.2008.12.015. PMID 19217324.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.