# Tenascin-R

> Mediated Wiki article. Canonical URL: https://mediated.wiki/source/Tenascin-R
> Markdown URL: https://mediated.wiki/source/Tenascin-R.md
> Source: https://en.wikipedia.org/wiki/Tenascin-R
> Source revision: 1301336841
> License: Creative Commons Attribution-ShareAlike 4.0 International (https://creativecommons.org/licenses/by-sa/4.0/)

Protein-coding gene in the species Homo sapiens

TNR Identifiers Aliases TNR, TN-R, tenascin R, NEDSTO External IDs OMIM: 601995; MGI: 99516; HomoloGene: 124416; GeneCards: TNR; OMA:TNR - orthologs Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1q25.1 Start 175,315,194 bp[1] End 175,743,616 bp[1] Gene location (Mouse) Chr. Chromosome 1 (mouse)[2] Band 1|1 H1 Start 159,351,339 bp[2] End 159,759,299 bp[2] RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Region I of hippocampus proper entorhinal cortex inferior ganglion of vagus nerve medulla oblongata subthalamic nucleus superior vestibular nucleus ventral tegmental area postcentral gyrus inferior olivary nucleus pars reticulata Top expressed in dentate gyrus of hippocampal formation granule cell lumbar subsegment of spinal cord primary visual cortex superior frontal gyrus ciliary body iris facial motor nucleus neural layer of retina hippocampus proper anterior horn of spinal cord More reference expression data BioGPS More reference expression data Gene ontology Molecular function protein binding Cellular component extracellular region cell surface membrane raft perineuronal net collagen-containing extracellular matrix extracellular matrix Schaffer collateral - CA1 synapse glutamatergic synapse Biological process negative regulation of neuron projection development positive regulation of synaptic transmission, glutamatergic extracellular matrix organization axon guidance synapse organization positive regulation of transmission of nerve impulse neuron cell-cell adhesion negative regulation of cell-cell adhesion telencephalon cell migration negative regulation of axon extension locomotory exploration behavior long-term potentiation neuromuscular process controlling balance regulation of neurogenesis negative regulation of axon extension involved in regeneration negative regulation of synaptic transmission modulation of chemical synaptic transmission associative learning cell adhesion Sources:Amigo / QuickGO Orthologs Species Human Mouse Entrez 7143 21960 Ensembl ENSG00000116147 ENSMUSG00000015829 UniProt Q92752 Q8BYI9 RefSeq (mRNA) NM_003285 NM_001328635 NM_022312 RefSeq (protein) NP_001315564 NP_003276 NP_003276.3 NP_071707 Location (UCSC) Chr 1: 175.32 – 175.74 Mb Chr 1: 159.35 – 159.76 Mb PubMed search [3] [4] Wikidata View/Edit Human View/Edit Mouse

**Tenascin-R** is a [protein](/source/Protein) that in humans is encoded by the *TNR* [gene](/source/Gene).[5][6][7]

## Function

Tenascin-R (TNR) is an [extracellular matrix](/source/Extracellular_matrix) protein expressed primarily in the central nervous system. It is a member of the [tenascin](/source/Tenascin) (TN) gene family, which includes 4 genes in mammals: [TNC](/source/Tenascin_C) (or hexabrachion), [TNX](/source/Tenascin_X) (TNXB), TNW (also known as TNN) and TNR.[8][9] The genes are expressed in distinct tissues at different times during embryonic development and are present in adult tissues.[supplied by OMIM][7]

## References

1. ^ [***a***](#cite_ref-refGRCh38Ensembl_1-0) [***b***](#cite_ref-refGRCh38Ensembl_1-1) [***c***](#cite_ref-refGRCh38Ensembl_1-2) [GRCh38: Ensembl release 89: ENSG00000116147](http://May2017.archive.ensembl.org/Homo_sapiens/Gene/Summary?db=core;g=ENSG00000116147) – [Ensembl](/source/Ensembl_genome_database_project), May 2017

1. ^ [***a***](#cite_ref-refGRCm38Ensembl_2-0) [***b***](#cite_ref-refGRCm38Ensembl_2-1) [***c***](#cite_ref-refGRCm38Ensembl_2-2) [GRCm38: Ensembl release 89: ENSMUSG00000015829](http://May2017.archive.ensembl.org/Mus_musculus/Gene/Summary?db=core;g=ENSMUSG00000015829) – [Ensembl](/source/Ensembl_genome_database_project), May 2017

1. **[^](#cite_ref-3)** ["Human PubMed Reference:"](https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Link&LinkName=gene_pubmed&from_uid=7143). *National Center for Biotechnology Information, U.S. National Library of Medicine*.

1. **[^](#cite_ref-4)** ["Mouse PubMed Reference:"](https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Link&LinkName=gene_pubmed&from_uid=21960). *National Center for Biotechnology Information, U.S. National Library of Medicine*.

1. **[^](#cite_ref-pmid8626505_5-0)** Carnemolla B, Leprini A, Borsi L, Querzé G, Urbini S, Zardi L (April 1996). ["Human tenascin-R. Complete primary structure, pre-mRNA alternative splicing and gene localization on chromosome 1q23-q24"](https://doi.org/10.1074%2Fjbc.271.14.8157). *The Journal of Biological Chemistry*. **271** (14): 8157–60. [doi](/source/Doi_(identifier)):[10.1074/jbc.271.14.8157](https://doi.org/10.1074%2Fjbc.271.14.8157). [PMID](/source/PMID_(identifier)) [8626505](https://pubmed.ncbi.nlm.nih.gov/8626505).

1. **[^](#cite_ref-pmid8940128_6-0)** Leprini A, Gherzi R, Siri A, Querzé G, Viti F, Zardi L (December 1996). ["The human tenascin-R gene"](https://doi.org/10.1074%2Fjbc.271.49.31251). *The Journal of Biological Chemistry*. **271** (49): 31251–4. [doi](/source/Doi_(identifier)):[10.1074/jbc.271.49.31251](https://doi.org/10.1074%2Fjbc.271.49.31251). [PMID](/source/PMID_(identifier)) [8940128](https://pubmed.ncbi.nlm.nih.gov/8940128).

1. ^ [***a***](#cite_ref-entrez_7-0) [***b***](#cite_ref-entrez_7-1) ["Entrez Gene: TNR tenascin R (restrictin, janusin)"](https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=7143).

1. **[^](#cite_ref-pmid7694605_8-0)** Erickson HP (October 1993). "Tenascin-C, tenascin-R and tenascin-X: a family of talented proteins in search of functions". *Current Opinion in Cell Biology*. **5** (5): 869–76. [doi](/source/Doi_(identifier)):[10.1016/0955-0674(93)90037-Q](https://doi.org/10.1016%2F0955-0674%2893%2990037-Q). [PMID](/source/PMID_(identifier)) [7694605](https://pubmed.ncbi.nlm.nih.gov/7694605).

1. **[^](#cite_ref-9)** Hsia, Henry C.; Schwarzbauer, Jean E. (July 2005). ["Meet the Tenascins: Multifunctional and Mysterious"](https://doi.org/10.1074%2Fjbc.R500005200). *Journal of Biological Chemistry*. **280** (29): 26641–26644. [doi](/source/Doi_(identifier)):[10.1074/jbc.R500005200](https://doi.org/10.1074%2Fjbc.R500005200). [PMID](/source/PMID_(identifier)) [15932878](https://pubmed.ncbi.nlm.nih.gov/15932878).

## Further reading

- Erickson HP (October 1993). "Tenascin-C, tenascin-R and tenascin-X: a family of talented proteins in search of functions". *Current Opinion in Cell Biology*. **5** (5): 869–76. [doi](/source/Doi_(identifier)):[10.1016/0955-0674(93)90037-Q](https://doi.org/10.1016%2F0955-0674%2893%2990037-Q). [PMID](/source/PMID_(identifier)) [7694605](https://pubmed.ncbi.nlm.nih.gov/7694605).

- Xiao ZC, Taylor J, Montag D, Rougon G, Schachner M (April 1996). "Distinct effects of recombinant tenascin-R domains in neuronal cell functions and identification of the domain interacting with the neuronal recognition molecule F3/11". *The European Journal of Neuroscience*. **8** (4): 766–82. [doi](/source/Doi_(identifier)):[10.1111/j.1460-9568.1996.tb01262.x](https://doi.org/10.1111%2Fj.1460-9568.1996.tb01262.x). [PMID](/source/PMID_(identifier)) [9081628](https://pubmed.ncbi.nlm.nih.gov/9081628). [S2CID](/source/S2CID_(identifier)) [30389358](https://api.semanticscholar.org/CorpusID:30389358).

- Aspberg A, Miura R, Bourdoulous S, Shimonaka M, Heinegârd D, Schachner M, Ruoslahti E, Yamaguchi Y (September 1997). ["The C-type lectin domains of lecticans, a family of aggregating chondroitin sulfate proteoglycans, bind tenascin-R by protein-protein interactions independent of carbohydrate moiety"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC23322). *Proceedings of the National Academy of Sciences of the United States of America*. **94** (19): 10116–21. [Bibcode](/source/Bibcode_(identifier)):[1997PNAS...9410116A](https://ui.adsabs.harvard.edu/abs/1997PNAS...9410116A). [doi](/source/Doi_(identifier)):[10.1073/pnas.94.19.10116](https://doi.org/10.1073%2Fpnas.94.19.10116). [PMC](/source/PMC_(identifier)) [23322](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC23322). [PMID](/source/PMID_(identifier)) [9294172](https://pubmed.ncbi.nlm.nih.gov/9294172).

- Xiao ZC, Hillenbrand R, Schachner M, Thermes S, Rougon G, Gomez S (September 1997). "Signaling events following the interaction of the neuronal adhesion molecule F3 with the N-terminal domain of tenascin-R". *Journal of Neuroscience Research*. **49** (6): 698–709. [doi](/source/Doi_(identifier)):[10.1002/(SICI)1097-4547(19970915)49:6<698::AID-JNR4>3.0.CO;2-2](https://doi.org/10.1002%2F%28SICI%291097-4547%2819970915%2949%3A6%3C698%3A%3AAID-JNR4%3E3.0.CO%3B2-2). [PMID](/source/PMID_(identifier)) [9335257](https://pubmed.ncbi.nlm.nih.gov/9335257). [S2CID](/source/S2CID_(identifier)) [10209383](https://api.semanticscholar.org/CorpusID:10209383).

- Arrigo G, Gherzi R, Bonaglia MC, Leprini A, Zuffardi O, Zardi L (1997). "Assignment of the tenascin-R gene (Tnr) to mouse chromosome 4 band E2 by fluorescence in situ hybridization; refinement of the human TNR location to chromosome 1q24". *Cytogenetics and Cell Genetics*. **78** (2): 145–6. [doi](/source/Doi_(identifier)):[10.1159/000134650](https://doi.org/10.1159%2F000134650). [PMID](/source/PMID_(identifier)) [9371410](https://pubmed.ncbi.nlm.nih.gov/9371410).

- Volkmer H, Zacharias U, Nörenberg U, Rathjen FG (August 1998). ["Dissection of complex molecular interactions of neurofascin with axonin-1, F11, and tenascin-R, which promote attachment and neurite formation of tectal cells"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2132869). *The Journal of Cell Biology*. **142** (4): 1083–93. [doi](/source/Doi_(identifier)):[10.1083/jcb.142.4.1083](https://doi.org/10.1083%2Fjcb.142.4.1083). [PMC](/source/PMC_(identifier)) [2132869](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2132869). [PMID](/source/PMID_(identifier)) [9722619](https://pubmed.ncbi.nlm.nih.gov/9722619).

- Zamze S, Harvey DJ, Pesheva P, Mattu TS, Schachner M, Dwek RA, Wing DR (August 1999). ["Glycosylation of a CNS-specific extracellular matrix glycoprotein, tenascin-R, is dominated by O-linked sialylated glycans and "brain-type" neutral N-glycans"](https://doi.org/10.1093%2Fglycob%2F9.8.823). *Glycobiology*. **9** (8): 823–31. [doi](/source/Doi_(identifier)):[10.1093/glycob/9.8.823](https://doi.org/10.1093%2Fglycob%2F9.8.823). [hdl](/source/Hdl_(identifier)):[20.500.11850/422721](https://hdl.handle.net/20.500.11850%2F422721). [PMID](/source/PMID_(identifier)) [10406848](https://pubmed.ncbi.nlm.nih.gov/10406848).

- Olin AI, Mörgelin M, Sasaki T, Timpl R, Heinegård D, Aspberg A (January 2001). ["The proteoglycans aggrecan and Versican form networks with fibulin-2 through their lectin domain binding"](https://doi.org/10.1074%2Fjbc.M006783200). *The Journal of Biological Chemistry*. **276** (2): 1253–61. [doi](/source/Doi_(identifier)):[10.1074/jbc.M006783200](https://doi.org/10.1074%2Fjbc.M006783200). [PMID](/source/PMID_(identifier)) [11038354](https://pubmed.ncbi.nlm.nih.gov/11038354).

- Xu XR, Huang J, Xu ZG, Qian BZ, Zhu ZD, Yan Q, Cai T, Zhang X, Xiao HS, Qu J, Liu F, Huang QH, Cheng ZH, Li NG, Du JJ, Hu W, Shen KT, Lu G, Fu G, Zhong M, Xu SH, Gu WY, Huang W, Zhao XT, Hu GX, Gu JR, Chen Z, Han ZG (December 2001). ["Insight into hepatocellular carcinogenesis at transcriptome level by comparing gene expression profiles of hepatocellular carcinoma with those of corresponding noncancerous liver"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC64988). *Proceedings of the National Academy of Sciences of the United States of America*. **98** (26): 15089–94. [Bibcode](/source/Bibcode_(identifier)):[2001PNAS...9815089X](https://ui.adsabs.harvard.edu/abs/2001PNAS...9815089X). [doi](/source/Doi_(identifier)):[10.1073/pnas.241522398](https://doi.org/10.1073%2Fpnas.241522398). [PMC](/source/PMC_(identifier)) [64988](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC64988). [PMID](/source/PMID_(identifier)) [11752456](https://pubmed.ncbi.nlm.nih.gov/11752456).

- Woodworth A, Pesheva P, Fiete D, Baenziger JU (March 2004). ["Neuronal-specific synthesis and glycosylation of tenascin-R"](https://doi.org/10.1074%2Fjbc.M312466200). *The Journal of Biological Chemistry*. **279** (11): 10413–21. [doi](/source/Doi_(identifier)):[10.1074/jbc.M312466200](https://doi.org/10.1074%2Fjbc.M312466200). [PMID](/source/PMID_(identifier)) [14681222](https://pubmed.ncbi.nlm.nih.gov/14681222).

- Bukalo O, Schachner M, Dityatev A (May 2007). ["Hippocampal metaplasticity induced by deficiency in the extracellular matrix glycoprotein tenascin-R"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6672247). *The Journal of Neuroscience*. **27** (22): 6019–28. [doi](/source/Doi_(identifier)):[10.1523/JNEUROSCI.1022-07.2007](https://doi.org/10.1523%2FJNEUROSCI.1022-07.2007). [PMC](/source/PMC_(identifier)) [6672247](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6672247). [PMID](/source/PMID_(identifier)) [17537973](https://pubmed.ncbi.nlm.nih.gov/17537973).

v t e Protein: scleroproteins Extracellular matrix Collagen Fibril forming type I COL1A1 COL1A2 type II (COL2A1) type III type V COL5A1 COL5A2 COL5A3 COL24A1 COL26A1 Other FACIT: type IX COL9A1 COL9A2 COL9A3 type XII (COL12A1) COL14A1 COL16A1 COL19A1 COL20A1 COL21A1 COL22A1 basement membrane: type IV COL4A1 COL4A2 COL4A3 COL4A4 COL4A5 COL4A6 multiplexin: COL15A1 type XVIII COL18A1 Endostatin transmembrane: COL13A1 COL17A1 COL23A1 COL25A1 other: type VI COL6A1 COL6A2 COL6A3 COL6A5 type VII (COL7A1) type VIII COL8A1 COL8A2 type X (COL10A1) type XI COL11A1 COL11A2 COL27A1 COL28A1 Enzymes Prolyl hydroxylase/Lysyl hydroxylase Cartilage associated protein/Leprecan ADAMTS2 Procollagen peptidase Lysyl oxidase Laminin alpha LAMA1 LAMA2 LAMA3 LAMA4 LAMA5 beta LAMB1 LAMB2 LAMB3 LAMB4 gamma LAMC1 LAMC2 LAMC3 Other ALCAM Elastin Tropoelastin Vitronectin FRAS1 FREM2 Decorin FAM20C ECM1 Matrix Gla protein Tectorin TECTA TECTB Other Keratin/Cytokeratin Gelatin Reticulin Cartilage oligomeric matrix protein See also diseases

This article on a gene on human chromosome 1 is a stub. You can help Wikipedia by adding missing information.

- [v](https://en.wikipedia.org/wiki/Template:Gene-1-stub)
- [t](/source/Template_talk%3AGene-1-stub)
- [e](https://en.wikipedia.org/wiki/Special:EditPage/Template:Gene-1-stub)

---
Adapted from the Wikipedia article [Tenascin-R](https://en.wikipedia.org/wiki/Tenascin-R) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/Tenascin-R?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.