Roxan

ZC3H7B
Identifiers
Aliases	ZC3H7B , RoXaN, zinc finger CCCH-type containing 7B, ROXAN1
External IDs	OMIM: 618206; MGI: 1328310; HomoloGene: 9735; GeneCards: ZC3H7B; OMA:ZC3H7B - orthologs
Gene location (Human)
Chr.	Chromosome 22 (human)
End	41,360,147 bp
Gene location (Mouse)
Chr.	Chromosome 15 (mouse)
End	81,680,461 bp
RNA expression pattern
	Top expressed in
	endothelial cell; ; buccal mucosa cell; ; nipple; ; renal medulla; ; cardia; ; pylorus; ; superior surface of tongue; ; ventral tegmental area; ; sperm; ; trigeminal ganglion;
	Top expressed in
	otolith organ; ; hand; ; utricle; ; dentate gyrus of hippocampal formation granule cell; ; Gonadal ridge; ; decidua; ; visual cortex; ; ventricular zone; ; suprachiasmatic nucleus; ; primary visual cortex;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	metal ion binding ; protein binding ; RNA binding ; miRNA binding ;
Cellular component	nucleus ;
Biological process	viral process ; posttranscriptional regulation of gene expression ; production of miRNAs involved in gene silencing by miRNA ;
	Sources:Amigo / QuickGO
Orthologs
	23264
	20286
	ENSG00000100403
	ENSMUSG00000022390
	Q9UGR2
	F8VPP8
	NM_017590
	NM_001081016
	NP_060060
	NP_001074485
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated November 19, 2024

RoXaN (Rotavirus 'X'-associated non-structural protein) also known as ZC3H7B (zinc finger CCCH-type containing 7B), is a protein that in humans is encoded by the ZC3H7B gene.^[5] RoXaN is a protein that contains tetratricopeptide repeat and leucine-aspartate repeat as well as zinc finger domains. This protein also interacts with the rotavirus non-structural protein NSP3.^[5]

Function

Rotavirus mRNAs are capped but not polyadenylated, and viral proteins are translated by the cellular translation machinery. This is accomplished through the action of the viral Nonstructural Protein NSP3 which specifically binds the 3' consensus sequence of viral mRNAs and interacts with the eukaryotic translation initiation factor eIF4G I.^[6]

RoXaN (rotavirus X protein associated with NSP3) is 110-kDa cellular protein that contains a minimum of three regions predicted to be involved in protein–protein or nucleic acid–protein interactions. A tetratricopeptide repeat region, a protein–protein interaction domain most often found in multiprotein complexes, is present in the amino-terminal region. In the carboxy terminus, at least five zinc finger motifs are observed, further suggesting the capacity of RoXaN to bind other proteins or nucleic acids. Between these two regions exists a paxillin leucine-aspartate repeat (LD) motif which is involved in protein–protein interactions.^[6]

Clinical significance

RoXaN is capable of interacting with NSP3 in vivo and during rotavirus infection. Domains of interaction correspond to the dimerization domain of NSP3 (amino acids 163 to 237) and the LD domain of RoXaN (amino acids 244 to 341). The interaction between NSP3 and RoXaN does not impair the interaction between NSP3 and eIF4G I, and a ternary complex made of NSP3, RoXaN, and eIF4G I can be detected in rotavirus-infected cells, implicating RoXaN in translation regulation.^[6]

Expression of RoXaN was found to be correlated with a higher tumor grad in GIST (gastrointestinal stromal tumors).^[7]

Related Research Articles

Poly(A)-binding protein is an RNA-binding protein which triggers the binding of eukaryotic initiation factor 4 complex (eIF4G) directly to the poly(A) tail of mRNA which is 200-250 nucleotides long. The poly(A) tail is located on the 3' end of mRNA and was discovered by Mary Edmonds, who also characterized the poly-A polymerase enzyme that generates the poly(a) tail. The binding protein is also involved in mRNA precursors by helping polyadenylate polymerase add the poly(A) nucleotide tail to the pre-mRNA before translation. The nuclear isoform selectively binds to around 50 nucleotides and stimulates the activity of polyadenylate polymerase by increasing its affinity towards RNA. Poly(A)-binding protein is also present during stages of mRNA metabolism including nonsense-mediated decay and nucleocytoplasmic trafficking. The poly(A)-binding protein may also protect the tail from degradation and regulate mRNA production. Without these two proteins in-tandem, then the poly(A) tail would not be added and the RNA would degrade quickly.

Rotavirus translation, the process of translating mRNA into proteins, occurs in a different way in Rotaviruses. Unlike the vast majority of cellular proteins in other organisms, in Rotaviruses the proteins are translated from capped but nonpolyadenylated mRNAs. The viral nonstructural protein NSP3 specifically binds the 3'-end consensus sequence of viral mRNAs and interacts with the eukaryotic translation initiation factor eIF4G. The Rotavirus replication cycle occurs entirely in the cytoplasm. Upon virus entry, the viral transcriptase synthesizes capped but nonpolyadenylated mRNA The viral mRNAs bear 5' and 3' untranslated regions (UTR) of variable length and are flanked by two different sequences common to all genes.

Rotavirus protein NSP3 (NS34) is bound to the 3' end consensus sequence of viral mRNAs in infected cells.

Tristetraprolin (TTP), also known as zinc finger protein 36 homolog (ZFP36), is a protein that in humans, mice and rats is encoded by the ZFP36 gene. It is a member of the TIS11 family, along with butyrate response factors 1 and 2.

Required for meiotic nuclear division 5 homolog B , also known as RMND5B, is a protein which in humans is encoded by the RMND5B gene. It has a zinc finger domain and is highly conserved throughout many eukaryotic organisms.

Zinc finger protein 40 is a protein that in humans is encoded by the HIVEP1 gene.

Mitochondrial import receptor subunit TOM34 is a protein that in humans is encoded by the TOMM34 gene.

Zinc finger protein 655 is a protein that in humans is encoded by the ZNF655 gene.

SH3 domain and tetratricopeptide repeats-containing protein 2 is a protein that in humans is encoded by the SH3TC2 gene. It is believed to be expressed in the Schwann cells that wrap the myelin sheath around nerves.

Zinc finger CCCH domain-containing protein 13 is a protein that in humans is encoded by the ZC3H13 gene.

Zinc finger CCCH-type antiviral protein 1 is a protein that in humans is encoded by the ZC3HAV1 gene.

Zinc finger protein 161 homolog is a protein that in humans is encoded by the ZBTB14 gene.

Zinc finger protein 330 is a protein that in humans is encoded by the ZNF330 gene.

Tetratricopeptide repeat protein 1 is a protein that in humans is encoded by the TTC1 gene.

Zinc finger protein 19 is a protein that in humans is encoded by the ZNF19 gene.

Tetratricopeptide repeat protein 35 is a protein that in humans is encoded by the TTC35 gene.

PHD finger protein 1 is a protein that in humans is encoded by the PHF1 gene.

Zinc finger protein 193 is a protein that in humans is encoded by the ZNF193 gene.

Zinc finger CCCH-type with G patch domain-containing protein is a protein that in humans is encoded by the ZGPAT gene.

ZC3H12B, also known as CXorf32 or MCPIP2, is a protein encoded by gene ZC3H12B located on chromosome Xq12 in humans.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000100403 – Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000022390 – 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.
1 2 "Entrez Gene: ZC3H7B zinc finger CCCH-type containing 7B".
1 2 3 Vitour D, Lindenbaum P, Vende P, Becker MM, Poncet D (April 2004). "RoXaN, a novel cellular protein containing TPR, LD, and zinc finger motifs, forms a ternary complex with eukaryotic initiation factor 4G and rotavirus NSP3". J. Virol. 78 (8): 3851–62. doi:10.1128/JVI.78.8.3851-3862.2004. PMC 374268 . PMID 15047801.
↑ Kang HJ, Koh KH, Yang E, You KT, Kim HJ, Paik YK, Kim H (February 2006). "Differentially expressed proteins in gastrointestinal stromal tumors with KIT and PDGFRA mutations". Proteomics. 6 (4): 1151–7. doi:10.1002/pmic.200500372. PMID 16402362. S2CID 2780778.

Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Kikuno R, Nagase T, Ishikawa K, et al. (June 1999). "Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Research. 6 (3): 197–205. doi: 10.1093/dnares/6.3.197 . PMID 10470851.
Dunham I, Shimizu N, Roe BA, et al. (December 1999). "The DNA sequence of human chromosome 22". Nature. 402 (6761): 489–95. Bibcode:1999Natur.402..489D. doi: 10.1038/990031 . PMID 10591208.
Wiemann S, Weil B, Wellenreuther R, et al. (March 2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome Research. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072 . PMID 11230166.
Strausberg RL, Feingold EA, Grouse LH, et al. (December 2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proceedings of the National Academy of Sciences of the United States of America. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC 139241 . PMID 12477932.
Gerhard DS, Wagner L, Feingold EA, et al. (October 2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Research. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928 . PMID 15489334.
Rush J, Moritz A, Lee KA, et al. (January 2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nature Biotechnology. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455. S2CID 7200157.
Lim J, Hao T, Shaw C, et al. (May 2006). "A protein–protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell. 125 (4): 801–14. doi: 10.1016/j.cell.2006.03.032 . PMID 16713569.

This article on a gene on human chromosome 22 is a stub. You can help Wikipedia by expanding it.

This page is based on this Wikipedia article
Text is available under the CC BY-SA 4.0 license; additional terms may apply.
Images, videos and audio are available under their respective licenses.

[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000100403 – Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000022390 – 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.

[entrez-5] 1 2 "Entrez Gene: ZC3H7B zinc finger CCCH-type containing 7B".

[pmid15047801-6] 1 2 3 Vitour D, Lindenbaum P, Vende P, Becker MM, Poncet D (April 2004). "RoXaN, a novel cellular protein containing TPR, LD, and zinc finger motifs, forms a ternary complex with eukaryotic initiation factor 4G and rotavirus NSP3". J. Virol. 78 (8): 3851–62. doi:10.1128/JVI.78.8.3851-3862.2004. PMC 374268 . PMID 15047801.

[pmid16402362-7] Kang HJ, Koh KH, Yang E, You KT, Kim HJ, Paik YK, Kim H (February 2006). "Differentially expressed proteins in gastrointestinal stromal tumors with KIT and PDGFRA mutations". Proteomics. 6 (4): 1151–7. doi:10.1002/pmic.200500372. PMID 16402362. S2CID 2780778.

[1]

[2]

[3]

[4]

[5]

[6]

[7]

Roxan

Contents

Function

Clinical significance

Related Research Articles

References

Further reading