Tenascin-R

Tenascin R (restrictin, janusin)

PDB rendering based on 1tdq.

Available structures
PDB	1tdq

Identifiers

Symbols

TNR; MGC149328; TN-R

External IDs

OMIM: 601995 MGI: 99516 HomoloGene: 124416 GeneCards: TNR Gene

Gene Ontology
Molecular function	• integrin binding
Cellular component	• extracellular region • proteinaceous extracellular matrix • cell surface • membrane raft
Biological process	• cell adhesion • negative regulation of cell adhesion • signal transduction • axon guidance • extracellular matrix organization
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 1:
175.29 – 175.71 Mb

Chr 1:
161.67 – 161.86 Mb

PubMed search

[1]

[2]

Tenascin-R is a protein that in humans is encoded by the TNR gene.^[1]^[2]^[3]

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.^[4] The genes are expressed in distinct tissues at different times during embryonic development and are present in adult tissues.[supplied by OMIM]^[3]

References

^ Carnemolla B, Leprini A, Borsi L, Querze G, Urbini S, Zardi L (Jun 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. doi:10.1074/jbc.271.14.8157. PMID 8626505.
^ Leprini A, Gherzi R, Siri A, Querze G, Viti F, Zardi L (Jan 1997). "The human tenascin-R gene". J Biol Chem 271 (49): 31251–4. doi:10.1074/jbc.271.49.31251. PMID 8940128.
^ ^a ^b "Entrez Gene: TNR tenascin R (restrictin, janusin)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7143.
^ Erickson HP (October 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. doi:10.1016/0955-0674(93)90037-Q. PMID 7694605.

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. doi:10.1016/0955-0674(93)90037-Q. PMID 7694605.
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. doi:10.1111/j.1460-9568.1996.tb01262.x. 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. doi:10.1073/pnas.94.19.10116. PMC 23322. PMID 9294172. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=23322.
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. 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, 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. doi:10.1159/000134650. 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. doi:10.1083/jcb.142.4.1083. PMC 2132869. PMID 9722619. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2132869.
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. doi:10.1093/glycob/9.8.823. 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. PMC 64988. PMID 11752456. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=64988.
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. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
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. PMC 1356129. PMID 16344560. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1356129.
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.

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) · type VII (COL7A1) · type VIII (COL8A1, COL8A2) · type X (COL10A1) · type XI (COL11A1, COL11A2) · COL27A1 · COL28A1 · COL29A1

Enzymes	Prolyl hydroxylase/Lysyl hydroxylase · Cartilage associated protein/Leprecan · ADAMTS2 · Procollagen peptidase · Lysyl oxidase

Tenascin

Tenascin C · Tenascin X

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
B proteins: BY STRUCTURE: membrane, globular (en, ca, an), fibrous

Tenascin-R

Function

References

Further reading