Tenascin-R

Tenascin-R is a protein that in humans is encoded by the TNR gene.[5][6][7]

TNR
Identifiers
Aliases	TNR, TN-R, tenascin R
External IDs	OMIM: 601995 MGI: 99516 HomoloGene: 124416 GeneCards: TNR
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 159,523,769 bp[2] End 159,931,729 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • GO:0001948 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 synaptic 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: 159.52 – 159.93 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

Tenascin-R (TNR) is an extracellular matrix protein expressed primarily in the central nervous system. It is a member of the tenascin (TN) gene family, which includes at least 3 genes in mammals: TNC (or hexabrachion), TNX (TNXB), and TNR.[8] 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. GRCh38: Ensembl release 89: ENSG00000116147 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000015829 - 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. 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". The Journal of Biological Chemistry. 271 (14): 8157–60. doi:10.1074/jbc.271.14.8157. PMID 8626505.
6. Leprini A, Gherzi R, Siri A, Querzé G, Viti F, Zardi L (December 1996). "The human tenascin-R gene". The Journal of Biological Chemistry. 271 (49): 31251–4. doi:10.1074/jbc.271.49.31251. PMID 8940128.
7. "Entrez Gene: TNR tenascin R (restrictin, janusin)".
8. 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:10.1016/0955-0674(93)90037-Q. PMID 7694605.

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:10.1016/0955-0674(93)90037-Q. PMID 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:10.1111/j.1460-9568.1996.tb01262.x. PMID 9081628. S2CID 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". Proceedings of the National Academy of Sciences of the United States of America. 94 (19): 10116–21. Bibcode:1997PNAS...9410116A. doi:10.1073/pnas.94.19.10116. PMC 23322. PMID 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:10.1002/(SICI)1097-4547(19970915)49:6<698::AID-JNR4>3.0.CO;2-2. PMID 9335257.
• 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:10.1159/000134650. PMID 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". The Journal of Cell Biology. 142 (4): 1083–93. doi:10.1083/jcb.142.4.1083. PMC 2132869. PMID 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". Glycobiology. 9 (8): 823–31. doi:10.1093/glycob/9.8.823. PMID 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". The Journal of Biological Chemistry. 276 (2): 1253–61. doi:10.1074/jbc.M006783200. PMID 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". Proceedings of the National Academy of Sciences of the United States of America. 98 (26): 15089–94. Bibcode:2001PNAS...9815089X. doi:10.1073/pnas.241522398. PMC 64988. PMID 11752456.
• Woodworth A, Pesheva P, Fiete D, Baenziger JU (March 2004). "Neuronal-specific synthesis and glycosylation of tenascin-R". The Journal of Biological Chemistry. 279 (11): 10413–21. doi:10.1074/jbc.M312466200. PMID 14681222.
• Bukalo O, Schachner M, Dityatev A (May 2007). "Hippocampal metaplasticity induced by deficiency in the extracellular matrix glycoprotein tenascin-R". The Journal of Neuroscience. 27 (22): 6019–28. doi:10.1523/JNEUROSCI.1022-07.2007. PMC 6672247. PMID 17537973.