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Cntn1  -  contactin 1

Rattus norvegicus

Synonyms: Contactin-1, Neural cell surface protein F3
 
 
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High impact information on Cntn1

 

Biological context of Cntn1

  • The F3/contactin rat gene differs from the mouse gene for two reasons: (1) it contains two additional untranslated exons that are alternatively spliced and (2) it lacks the homologue mouse untranslated exon 0 [3].
  • The formation of these specialized axoglial contacts depends on the presence of three cell adhesion molecules: neurofascin 155 on the glial membrane and a complex of Caspr and contactin on the axon [4].
  • Fluorescence in situ hybridization maps the gene for human contactin to human chromosome 12q11-q12 [5].
  • The h-contactin gene locus is thus in close proximity to homeobox 3, integrin subunit alpha 5, several proto-oncogene genes, a chromosomal breakpoint associated with various tumors, and the gene locus for Stickler syndrome [5].
  • NB-2 shared 46, 43, 55 and 55% identities with Contactin/F3, Tag-1, Big-1 and Big-2, respectively, at the amino acid sequence level [6].
 

Anatomical context of Cntn1

 

Associations of Cntn1 with chemical compounds

  • Independent cDNAs encoding two putative contactin isoforms were isolated and sequenced: h-contactin 1 cDNA encodes a protein with the amino-terminal sequence of purified Gp135, while the putative h-contactin 2 gene has a deletion of 33 nucleotides that predicts a protein with a shortened amino terminus [5].
 

Co-localisations of Cntn1

  • We now report that contactin colocalizes and forms a cis complex with Caspr in the paranodes and juxtamesaxon [9].
 

Other interactions of Cntn1

References

  1. The axonal membrane protein Caspr, a homologue of neurexin IV, is a component of the septate-like paranodal junctions that assemble during myelination. Einheber, S., Zanazzi, G., Ching, W., Scherer, S., Milner, T.A., Peles, E., Salzer, J.L. J. Cell Biol. (1997) [Pubmed]
  2. Identification of a novel contactin-associated transmembrane receptor with multiple domains implicated in protein-protein interactions. Peles, E., Nativ, M., Lustig, M., Grumet, M., Schilling, J., Martinez, R., Plowman, G.D., Schlessinger, J. EMBO J. (1997) [Pubmed]
  3. Polymorphism of the untranslated regions of the F3/contactin mRNA in the rat nervous system. Rome, C., Roullot, V., Couillaud, F. Brain Res. Mol. Brain Res. (2005) [Pubmed]
  4. Spectrins and ankyrinB constitute a specialized paranodal cytoskeleton. Ogawa, Y., Schafer, D.P., Horresh, I., Bar, V., Hales, K., Yang, Y., Susuki, K., Peles, E., Stankewich, M.C., Rasband, M.N. J. Neurosci. (2006) [Pubmed]
  5. Molecular cloning and in situ localization of the human contactin gene (CNTN1) on chromosome 12q11-q12. Berglund, E.O., Ranscht, B. Genomics (1994) [Pubmed]
  6. Novel neural adhesion molecules in the Contactin/F3 subgroup of the immunoglobulin superfamily: isolation and characterization of cDNAs from rat brain. Ogawa, J., Kaneko, H., Masuda, T., Nagata, S., Hosoya, H., Watanabe, K. Neurosci. Lett. (1996) [Pubmed]
  7. Direct interaction with contactin targets voltage-gated sodium channel Na(v)1.9/NaN to the cell membrane. Liu, C.J., Dib-Hajj, S.D., Black, J.A., Greenwood, J., Lian, Z., Waxman, S.G. J. Biol. Chem. (2001) [Pubmed]
  8. Age-related decline of F3/contactin in rat hippocampus. Shimazaki, K., Hosoya, H., Takeda, Y., Kobayashi, S., Watanabe, K. Neurosci. Lett. (1998) [Pubmed]
  9. Contactin-associated protein (Caspr) and contactin form a complex that is targeted to the paranodal junctions during myelination. Rios, J.C., Melendez-Vasquez, C.V., Einheber, S., Lustig, M., Grumet, M., Hemperly, J., Peles, E., Salzer, J.L. J. Neurosci. (2000) [Pubmed]
  10. Neural recognition molecule NB-2 of the contactin/F3 subgroup in rat: Specificity in neurite outgrowth-promoting activity and restricted expression in the brain regions. Ogawa, J., Lee, S., Itoh, K., Nagata, S., Machida, T., Takeda, Y., Watanabe, K. J. Neurosci. Res. (2001) [Pubmed]
 
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