TNR (gene)

From Wikipedia, the free encyclopedia

Tenascin R (restrictin, janusin)

PDB rendering based on 1tdq.

Available structures: 1tdq

Identifiers

Symbol(s)

TNR; MGC149328

External IDs

OMIM: 601995 MGI: 99516 HomoloGene: 2466

Gene ontology
Molecular Function:	• receptor binding • extracellular matrix structural constituent
Cellular Component:	• proteinaceous extracellular matrix • extracellular space • cell surface • lipid raft
Biological Process:	• cell adhesion • signal transduction • axon guidance • extracellular matrix organization and biogenesis

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_003285 (mRNA)
NP_003276 (protein)

NM_022312 (mRNA)
NP_071707 (protein)

Location

Chr 1: 173.56 - 173.98 Mb

Chr 1: 161.57 - 161.76 Mb

Pubmed search

[1]

[2]

Tenascin R (restrictin, janusin), also known as TNR, is a human gene.^[1]

Tenascin-R (TNR) is an extracellular matix 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; MIM 187380), TNX (TNXB; MIM 600985), and TNR (Erickson, 1993). The genes are expressed in distinct tissues at different times during embryonic development and are present in adult tissues.[supplied by OMIM]^[1]

[edit] References

^ ^a ^b Entrez Gene: TNR tenascin R (restrictin, janusin).

[edit] Further reading

Erickson HP (1993). "Tenascin-C, tenascin-R and tenascin-X: a family of talented proteins in search of functions.". Curr. Opin. Cell Biol. 5 (5): 869-76. PMID 7694605.
Carnemolla B, Leprini A, Borsi L, et al. (1996). "Human tenascin-R. Complete primary structure, pre-mRNA alternative splicing and gene localization on chromosome 1q23-q24.". J. Biol. Chem. 271 (14): 8157-60. PMID 8626505.
Leprini A, Gherzi R, Siri A, et al. (1997). "The human tenascin-R gene.". J. Biol. Chem. 271 (49): 31251-4. PMID 8940128.
Xiao ZC, Taylor J, Montag D, et al. (1997). "Distinct effects of recombinant tenascin-R domains in neuronal cell functions and identification of the domain interacting with the neuronal recognition molecule F3/11.". Eur. J. Neurosci. 8 (4): 766-82. PMID 9081628.
Aspberg A, Miura R, Bourdoulous S, et al. (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.". Proc. Natl. Acad. Sci. U.S.A. 94 (19): 10116-21. PMID 9294172.
Xiao ZC, Hillenbrand R, Schachner M, et al. (1997). "Signaling events following the interaction of the neuronal adhesion molecule F3 with the N-terminal domain of tenascin-R.". J. Neurosci. Res. 49 (6): 698-709. PMID 9335257.
Arrigo G, Gherzi R, Bonaglia MC, et al. (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.". Cytogenet. Cell Genet. 78 (2): 145-6. PMID 9371410.
Volkmer H, Zacharias U, Nörenberg U, Rathjen FG (1998). "Dissection of complex molecular interactions of neurofascin with axonin-1, F11, and tenascin-R, which promote attachment and neurite formation of tectal cells.". J. Cell Biol. 142 (4): 1083-93. PMID 9722619.
Zamze S, Harvey DJ, Pesheva P, et al. (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. PMID 10406848.
Olin AI, Mörgelin M, Sasaki T, et al. (2001). "The proteoglycans aggrecan and Versican form networks with fibulin-2 through their lectin domain binding.". J. Biol. Chem. 276 (2): 1253-61. doi:10.1074/jbc.M006783200. PMID 11038354.
Xu XR, Huang J, Xu ZG, et al. (2002). "Insight into hepatocellular carcinogenesis at transcriptome level by comparing gene expression profiles of hepatocellular carcinoma with those of corresponding noncancerous liver.". Proc. Natl. Acad. Sci. U.S.A. 98 (26): 15089-94. doi:10.1073/pnas.241522398. PMID 11752456.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899-903. doi:10.1073/pnas.242603899. PMID 12477932.
Woodworth A, Pesheva P, Fiete D, Baenziger JU (2004). "Neuronal-specific synthesis and glycosylation of tenascin-R.". J. Biol. Chem. 279 (11): 10413-21. doi:10.1074/jbc.M312466200. PMID 14681222.
Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.". Genome Res. 16 (1): 55-65. doi:10.1101/gr.4039406. PMID 16344560.
Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1.". Nature 441 (7091): 315-21. doi:10.1038/nature04727. PMID 16710414.
Bukalo O, Schachner M, Dityatev A (2007). "Hippocampal metaplasticity induced by deficiency in the extracellular matrix glycoprotein tenascin-R.". J. Neurosci. 27 (22): 6019-28. doi:10.1523/JNEUROSCI.1022-07.2007. PMID 17537973.