Contactin 1

CNTN1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2EE2, 3S97
Identifiers
Aliases	CNTN1 , F3, GP135, MYPCN, contactin 1
External IDs	OMIM: 600016; MGI: 105980; HomoloGene: 7274; GeneCards: CNTN1; OMA:CNTN1 - orthologs
Gene location (Human)
Chr.	Chromosome 12 (human)
End	41,072,415 bp
Gene location (Mouse)
Chr.	Chromosome 15 (mouse)
End	92,239,848 bp
RNA expression pattern
	Top expressed in
	Brodmann area 23; ; endothelial cell; ; superior frontal gyrus; ; postcentral gyrus; ; entorhinal cortex; ; prefrontal cortex; ; cerebellar cortex; ; primary visual cortex; ; amygdala; ; cerebellar hemisphere;
	Top expressed in
	lateral geniculate nucleus; ; ventromedial nucleus; ; lateral septal nucleus; ; medial geniculate nucleus; ; mammillary body; ; ventral tegmental area; ; medial dorsal nucleus; ; lateral hypothalamus; ; anterior amygdaloid area; ; globus pallidus;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	carbohydrate binding ; protein binding ;
Cellular component	myelin sheath ; anchored component of membrane ; membrane raft ; plasma membrane ; extracellular exosome ; membrane ; anchored component of postsynaptic membrane ; anchored component of presynaptic membrane ;
Biological process	positive regulation of peptidyl-tyrosine phosphorylation ; nervous system development ; cell adhesion ; positive regulation of gene expression ; neuron projection development ; positive regulation of sodium ion transport ; cerebellum development ; positive regulation of neuron projection development ; Notch signaling pathway ;
	Sources:Amigo / QuickGO
Orthologs
	1272
	12805
	ENSG00000018236
	ENSMUSG00000055022
	Q12860
	P12960
	NM_001256063 ; NM_001256064 ; NM_001843 ; NM_175038
	NM_001159647 ; NM_001159648 ; NM_007727 ; NM_001358051
	NP_001242992 ; NP_001242993 ; NP_001834 ; NP_778203
	NP_001153119 ; NP_001153120 ; NP_031753 ; NP_001344980
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated August 10, 2024

Contactin 1 (CNTN1) is a protein which in humans is encoded by the CNTN1 gene.^[5]^[6]

Function

The protein encoded by this gene is a member of the immunoglobulin superfamily. It is a glycosylphosphatidylinositol (GPI)-anchored neuronal membrane protein that functions as a cell adhesion molecule. It may play a role in the formation of axon connections in the developing nervous system. Two alternatively spliced transcript variants encoding different isoforms have been described for this gene.^[6]

Interactions

CNTN1 has been shown to interact with PTPRB.^[7]^[8]

Related Research Articles

L1, also known as L1CAM, is a transmembrane protein member of the L1 protein family, encoded by the L1CAM gene. This protein, of 200 to 220 kDa, is a neuronal cell adhesion molecule with a strong implication in cell migration, adhesion, neurite outgrowth, myelination and neuronal differentiation. It also plays a key role in treatment-resistant cancers due to its function. It was first identified in 1984 by M. Schachner who found the protein in post-mitotic mice neurons.

<span class="mw-page-title-main">Protein tyrosine phosphatase</span> Class of enzymes

Protein tyrosine phosphatases (EC 3.1.3.48, systematic name protein-tyrosine-phosphate phosphohydrolase) are a group of enzymes that remove phosphate groups from phosphorylated tyrosine residues on proteins:

Semaphorins are a class of secreted and membrane proteins that were originally identified as axonal growth cone guidance molecules. They primarily act as short-range inhibitory signals and signal through multimeric receptor complexes. Semaphorins are usually cues to deflect axons from inappropriate regions, especially important in the neural system development. The major class of proteins that act as their receptors are called plexins, with neuropilins as their co-receptors in many cases. The main receptors for semaphorins are plexins, which have established roles in regulating Rho-family GTPases. Recent work shows that plexins can also influence R-Ras, which, in turn, can regulate integrins. Such regulation is probably a common feature of semaphorin signalling and contributes substantially to our understanding of semaphorin biology.

Protein tyrosine kinase 2 beta is an enzyme that in humans is encoded by the PTK2B gene.

Receptor-type tyrosine-protein phosphatase alpha is an enzyme that in humans is encoded by the PTPRA gene.

Receptor-type tyrosine-protein phosphatase F is an enzyme that, in humans, is encoded by the PTPRF gene.

Receptor-type tyrosine-protein phosphatase zeta also known as phosphacan is an enzyme that in humans is encoded by the PTPRZ1 gene.

Contactin-2 is a protein that in humans is encoded by the CNTN2 gene.

Neurofascin is a protein that in humans is encoded by the NFASC gene.

Receptor-type tyrosine-protein phosphatase mu is an enzyme that in humans is encoded by the PTPRM gene.

Neuronal cell adhesion molecule is a protein that in humans is encoded by the NRCAM gene.

Receptor-type tyrosine-protein phosphatase PCP-2, is an enzyme that in humans is encoded by the PTPRU gene.

Neurocan core protein is a protein that in humans is encoded by the NCAN gene.

Receptor-type tyrosine-protein phosphatase kappa is an enzyme that in humans is encoded by the PTPRK gene. PTPRK is also known as PTPkappa and PTPκ.

Receptor-type tyrosine-protein phosphatase T is an enzyme that in humans is encoded by the PTPRT gene.

Contactin-4 is a protein that in humans is encoded by the CNTN4 gene.

Tyrosine-protein phosphatase non-receptor type 14 is an enzyme that in humans is encoded by the PTPN14 gene.

Tenascin-R is a protein that in humans is encoded by the TNR gene.

Contactin 6 is a protein in humans that is encoded by the CNTN6 gene.

CASPR also known as Contactin associated protein 1, Paranodin and CASPR1 is a protein that in humans is encoded by the CNTNAP1 gene. CASPR is a part of the neurexin family of proteins, hence its another name "Neurexin IV". CASPR is a membrane protein found in the neuronal membrane in the paranodal section of the axon[[]] in myelinated neurons, between the Nodes of Ranvier containing Na+ channels, and juxtaparanode, which contains K+ channels. During myelination, caspr associates with contactin in a cis complex, though its precise role in myelination is not yet understood.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000018236 – Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000055022 – Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Berglund EO, Ranscht B (Jun 1994). "Molecular cloning and in situ localization of the human contactin gene (CNTN1) on chromosome 12q11-q12". Genomics. 21 (3): 571–82. doi:10.1006/geno.1994.1316. PMID 7959734.
1 2 "Entrez Gene: CNTN1 contactin 1".
↑ Sakurai T, Lustig M, Nativ M, Hemperly JJ, Schlessinger J, Peles E, Grumet M (Feb 1997). "Induction of neurite outgrowth through contactin and Nr-CAM by extracellular regions of glial receptor tyrosine phosphatase beta". The Journal of Cell Biology. 136 (4): 907–18. doi:10.1083/jcb.136.4.907. PMC 2132488 . PMID 9049255.
↑ Peles E, Nativ M, Campbell PL, Sakurai T, Martinez R, Lev S, Clary DO, Schilling J, Barnea G, Plowman GD, Grumet M, Schlessinger J (Jul 1995). "The carbonic anhydrase domain of receptor tyrosine phosphatase beta is a functional ligand for the axonal cell recognition molecule contactin". Cell. 82 (2): 251–60. doi: 10.1016/0092-8674(95)90312-7 . PMID 7628014. S2CID 18084292.

External links

Human CNTN1 genome location and CNTN1 gene details page in the UCSC Genome Browser .
Human F3 genome location and F3 gene details page in the UCSC Genome Browser .

Walsh FS, Doherty P (Nov 1991). "Glycosylphosphatidylinositol anchored recognition molecules that function in axonal fasciculation, growth and guidance in the nervous system". Cell Biology International Reports. 15 (11): 1151–66. doi:10.1016/0309-1651(91)90061-M. PMID 1838307.
Peles E, Schlessinger J, Grumet M (Apr 1998). "Multi-ligand interactions with receptor-like protein tyrosine phosphatase beta: implications for intercellular signaling". Trends in Biochemical Sciences. 23 (4): 121–4. doi: 10.1016/S0968-0004(98)01195-5 . PMID 9584610.
Olive S, Dubois C, Schachner M, Rougon G (Nov 1995). "The F3 neuronal glycosylphosphatidylinositol-linked molecule is localized to glycolipid-enriched membrane subdomains and interacts with L1 and fyn kinase in cerebellum". Journal of Neurochemistry. 65 (5): 2307–17. doi:10.1046/j.1471-4159.1995.65052307.x. PMID 7595520. S2CID 39142478.
Peles E, Nativ M, Campbell PL, Sakurai T, Martinez R, Lev S, Clary DO, Schilling J, Barnea G, Plowman GD, Grumet M, Schlessinger J (Jul 1995). "The carbonic anhydrase domain of receptor tyrosine phosphatase beta is a functional ligand for the axonal cell recognition molecule contactin". Cell. 82 (2): 251–60. doi: 10.1016/0092-8674(95)90312-7 . PMID 7628014. S2CID 18084292.
Berglund EO, Ranscht B (Jun 1994). "Molecular cloning and in situ localization of the human contactin gene (CNTN1) on chromosome 12q11-q12". Genomics. 21 (3): 571–82. doi:10.1006/geno.1994.1316. PMID 7959734.
Reid RA, Bronson DD, Young KM, Hemperly JJ (Jan 1994). "Identification and characterization of the human cell adhesion molecule contactin". Brain Research. Molecular Brain Research. 21 (1–2): 1–8. doi:10.1016/0169-328X(94)90372-7. PMID 8164510.
Yoshihara Y, Kawasaki M, Tamada A, Nagata S, Kagamiyama H, Mori K (Sep 1995). "Overlapping and differential expression of BIG-2, BIG-1, TAG-1, and F3: four members of an axon-associated cell adhesion molecule subgroup of the immunoglobulin superfamily". Journal of Neurobiology. 28 (1): 51–69. doi:10.1002/neu.480280106. PMID 8586965.
Sakurai T, Lustig M, Nativ M, Hemperly JJ, Schlessinger J, Peles E, Grumet M (Feb 1997). "Induction of neurite outgrowth through contactin and Nr-CAM by extracellular regions of glial receptor tyrosine phosphatase beta". The Journal of Cell Biology. 136 (4): 907–18. doi:10.1083/jcb.136.4.907. PMC 2132488 . PMID 9049255.
Xiao ZC, Taylor J, Montag D, Rougon G, Schachner M (Apr 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.
Xiao ZC, Hillenbrand R, Schachner M, Thermes S, Rougon G, Gomez S (Sep 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. S2CID 10209383.
Pierre K, Rougon G, Allard M, Bonhomme R, Gennarini G, Poulain DA, Theodosis DT (Jul 1998). "Regulated expression of the cell adhesion glycoprotein F3 in adult hypothalamic magnocellular neurons". The Journal of Neuroscience. 18 (14): 5333–43. doi:10.1523/JNEUROSCI.18-14-05333.1998. PMC 6793479 . PMID 9651216.
Revest JM, Faivre-Sarrailh C, Maeda N, Noda M, Schachner M, Rougon G (Apr 1999). "The interaction between F3 immunoglobulin domains and protein tyrosine phosphatases zeta/beta triggers bidirectional signalling between neurons and glial cells". The European Journal of Neuroscience. 11 (4): 1134–47. doi:10.1046/j.1460-9568.1999.00521.x. PMID 10103110. S2CID 23803785.
Berglund EO, Murai KK, Fredette B, Sekerková G, Marturano B, Weber L, Mugnaini E, Ranscht B (Nov 1999). "Ataxia and abnormal cerebellar microorganization in mice with ablated contactin gene expression". Neuron. 24 (3): 739–50. doi: 10.1016/S0896-6273(00)81126-5 . PMID 10595523. S2CID 16663068.
Pierre K, Dupouy B, Allard M, Poulain DA, Theodosis DT (Aug 2001). "Mobilization of the cell adhesion glycoprotein F3/contactin to axonal surfaces is activity dependent". The European Journal of Neuroscience. 14 (4): 645–56. doi:10.1046/j.0953-816x.2001.01682.x. PMID 11556889. S2CID 43151749.
Kazarinova-Noyes K, Malhotra JD, McEwen DP, Mattei LN, Berglund EO, Ranscht B, Levinson SR, Schachner M, Shrager P, Isom LL, Xiao ZC (Oct 2001). "Contactin associates with Na+ channels and increases their functional expression". The Journal of Neuroscience. 21 (19): 7517–25. doi: 10.1523/JNEUROSCI.21-19-07517.2001 . PMC 6762905 . PMID 11567041.
Pavlou O, Theodorakis K, Falk J, Kutsche M, Schachner M, Faivre-Sarrailh C, Karagogeos D (Jul 2002). "Analysis of interactions of the adhesion molecule TAG-1 and its domains with other immunoglobulin superfamily members". Molecular and Cellular Neurosciences. 20 (3): 367–81. doi:10.1006/mcne.2002.1105. PMID 12139915. S2CID 714233.
Garwood J, Heck N, Reichardt F, Faissner A (Jun 2003). "Phosphacan short isoform, a novel non-proteoglycan variant of phosphacan/receptor protein tyrosine phosphatase-beta, interacts with neuronal receptors and promotes neurite outgrowth". The Journal of Biological Chemistry. 278 (26): 24164–73. doi: 10.1074/jbc.M211721200 . PMID 12700241.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000018236 – Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000055022 – 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.

[pmid7959734-5] Berglund EO, Ranscht B (Jun 1994). "Molecular cloning and in situ localization of the human contactin gene (CNTN1) on chromosome 12q11-q12". Genomics. 21 (3): 571–82. doi:10.1006/geno.1994.1316. PMID 7959734.

[entrez-6] 1 2 "Entrez Gene: CNTN1 contactin 1".

[pmid9049255-7] Sakurai T, Lustig M, Nativ M, Hemperly JJ, Schlessinger J, Peles E, Grumet M (Feb 1997). "Induction of neurite outgrowth through contactin and Nr-CAM by extracellular regions of glial receptor tyrosine phosphatase beta". The Journal of Cell Biology. 136 (4): 907–18. doi:10.1083/jcb.136.4.907. PMC 2132488 . PMID 9049255.

[pmid7628014-8] Peles E, Nativ M, Campbell PL, Sakurai T, Martinez R, Lev S, Clary DO, Schilling J, Barnea G, Plowman GD, Grumet M, Schlessinger J (Jul 1995). "The carbonic anhydrase domain of receptor tyrosine phosphatase beta is a functional ligand for the axonal cell recognition molecule contactin". Cell. 82 (2): 251–60. doi: 10.1016/0092-8674(95)90312-7 . PMID 7628014. S2CID 18084292.

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